|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
1-503 |
0e+00 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 1111.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 1 MAITVPRRQLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRNNGKDWARATGAVRAKYLRA 80
Cdd:PLN02467 1 MAIPVPRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRNKGKDWARTTGAVRAKYLRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 81 IAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDTFKGYILKEPIGVVGMITP 160
Cdd:PLN02467 81 IAAKITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFKGYVLKEPLGVVGLITP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 161 WNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGST 240
Cdd:PLN02467 161 WNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 241 TTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKN 320
Cdd:PLN02467 241 ATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 321 IKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALC 400
Cdd:PLN02467 321 IKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 401 VKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYL 480
Cdd:PLN02467 401 VKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYL 480
|
490 500
....*....|....*....|...
gi 1789584901 481 SVKQVTQYISDEPWGWYKPPSKL 503
Cdd:PLN02467 481 SVKQVTKYISDEPWGWYPPPSKL 503
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
27-487 |
0e+00 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 879.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR-----WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKP 186
Cdd:cd07110 76 AAWDVDDVAGCFEYYADLAEQLDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 187 SELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSP 266
Cdd:cd07110 156 SELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 267 IIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVL 346
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 347 KFVSNARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVL 426
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1789584901 427 SNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVTQ 487
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQITR 456
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
4-486 |
0e+00 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 659.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 4 TVPRRQLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAA 83
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF-----PAWAATPPAERAAILLRAAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 84 KVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKQktpLSLPMDTFKGYILKEPIGVVGMITPWNY 163
Cdd:COG1012 77 LLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGET---IPSDAPGTRAYVRREPLGVVGAITPWNF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 164 PLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTG 243
Cdd:COG1012 154 PLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 244 SSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKI 323
Cdd:COG1012 234 RRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 324 SDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKT 403
Cdd:COG1012 314 GDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG-EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 404 FSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQP-CFCQAPWGGTKRSGFGRELGEWGLENYLSV 482
Cdd:COG1012 393 FDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTgAVPQAPFGGVKQSGIGREGGREGLEEYTET 472
|
....
gi 1789584901 483 KQVT 486
Cdd:COG1012 473 KTVT 476
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
11-497 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 625.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnNGKDWARATGAVRAKYLRAIAAKVIERKS 90
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAF---DSGEWPHLPAQERAALLFRIADKIREDAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 91 ELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKQktpLSLPMDTFKgYILKEPIGVVGMITPWNYPLLMAVW 170
Cdd:cd07119 78 ELARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEV---YDVPPHVIS-RTVREPVGVCGLITPWNYPLLQAAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 171 KVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSA 250
Cdd:cd07119 154 KLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 251 AKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEG 330
Cdd:cd07119 234 AGNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDAD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 331 CRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPE--HLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTED 408
Cdd:cd07119 314 TEMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 409 EAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVTQY 488
Cdd:cd07119 394 EAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININ 473
|
....*....
gi 1789584901 489 ISDEPWGWY 497
Cdd:cd07119 474 LSPQPIGWF 482
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
16-485 |
0e+00 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 623.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 16 WTEPVLrKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANL 95
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAF-----PAWRKTPAAERAAILRKAADLLEERKDELAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 96 EAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDakqktPLSLPMD-TFKGYILKEPIGVVGMITPWNYPLLMAVWKVAP 174
Cdd:pfam00171 75 ETLENGKPLAEARGEVDRAIDVLRYYAGLARRLD-----GETLPSDpGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 175 SLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLV 254
Cdd:pfam00171 150 ALAAGNTVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 255 KPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLG 334
Cdd:pfam00171 230 KRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 335 PVVSKGQYERVLKFVSNARNEGATVLCGGvrPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLA 414
Cdd:pfam00171 310 PLISKAQLERVLKYVEDAKEEGAKLLTGG--EAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789584901 415 NDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCF-CQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:pfam00171 388 NDTEYGLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDaDGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
9-486 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 594.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrNNGKdWARATGAVRAKYLRAIAaKVIER 88
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAF--ETGW-WRKMDPRERGRLLNKLA-DLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KS-ELANLEAIDCGKPLDEAA-WDMDDVAGCFEYYADLAEGLDAKqktplSLPMDT-FKGYILKEPIGVVGMITPWNYPL 165
Cdd:cd07091 81 DRdELAALESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGK-----TIPIDGnFLAYTRREPIGVCGQIIPWNFPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 166 LMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSS 245
Cdd:cd07091 156 LMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 246 IMTSAAKL-VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKIS 324
Cdd:cd07091 236 IMEAAAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 325 DPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRpeHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTF 404
Cdd:cd07091 316 DPFDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGER--HGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 405 STEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQ 484
Cdd:cd07091 394 KTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKA 473
|
..
gi 1789584901 485 VT 486
Cdd:cd07091 474 VT 475
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
50-486 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 592.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 50 AVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLD 129
Cdd:cd07078 3 AVAAARAAF-----KAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 130 AKQKTPlslPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPG 209
Cdd:cd07078 78 GEVIPS---PDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 210 VLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWT 289
Cdd:cd07078 155 VLNVVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 290 NGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHL 369
Cdd:cd07078 235 AGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 370 kKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNC 449
Cdd:cd07078 315 -KGYFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWIND 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 1789584901 450 SQPCFC-QAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07078 394 YSVGAEpSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-486 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 559.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAF-----PGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 A-AWDMDDVAGCFEYYADLAEGLDAKqktplSLPMDT-FKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAIL 184
Cdd:cd07093 76 ArTRDIPRAAANFRFFADYILQLDGE-----SYPQDGgALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 185 KPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGK 264
Cdd:cd07093 151 KPSEWTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 265 SPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYER 344
Cdd:cd07093 231 NPNIVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 345 VLKFVSNARNEGATVLCGGVRPE--HLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLA 422
Cdd:cd07093 311 VLGYVELARAEGATILTGGGRPElpDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1789584901 423 GAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07093 391 AYVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-485 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 559.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFTrnnGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFE---GGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYYADLAEGLDAkQKTPLSLPmDTFkGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKP 186
Cdd:cd07114 78 TRAQVRYLAEWYRYYAGLADKIEG-AVIPVDKG-DYL-NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 187 SELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSP 266
Cdd:cd07114 155 SEHTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 267 IIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVL 346
Cdd:cd07114 235 NIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 347 KFVSNARNEGATVLCGGVRPEH--LKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGA 424
Cdd:cd07114 315 RYVARAREEGARVLTGGERPSGadLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1789584901 425 VLSNDLERCDRVSKAFQAGIVWVNC---SQPCfcqAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNTyraLSPS---SPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
10-486 |
0e+00 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 541.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERK 89
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPA-----WSATSVEERAALLERIAEAYEARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLDEAAWDMDDVA-GCFEYYADLAEGLDAKQKTPLSLpmdtfkgyILKEPIGVVGMITPWNYPLLMA 168
Cdd:cd07138 76 DELAQAITLEMGAPITLARAAQVGLGiGHLRAAADALKDFEFEERRGNSL--------VVREPIGVCGLITPWNWPLNQI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 169 VWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMT 248
Cdd:cd07138 148 VLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 249 SAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFE 328
Cdd:cd07138 228 AAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 329 EGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGV-RPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTE 407
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGPgRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789584901 408 DEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFcQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07138 388 DEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
10-485 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 533.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAV-RAKYLRAIAAKVIER 88
Cdd:cd07144 10 LFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAF-----ESWWSKVTGEeRGELLDKLADLVEKN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDE-AAWDMDDVAGCFEYYADLAEGLDAKqktplSLPMDTFK-GYILKEPIGVVGMITPWNYPLL 166
Cdd:cd07144 85 RDLLAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGK-----TIPTSPNKlAYTLHEPYGVCGQIIPWNYPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 167 MAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSI 246
Cdd:cd07144 160 MAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 247 MTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTK-NIKISD 325
Cdd:cd07144 240 MKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 326 PFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGG-VRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTF 404
Cdd:cd07144 320 PFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGeKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 405 STEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQ 484
Cdd:cd07144 400 KTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKA 479
|
.
gi 1789584901 485 V 485
Cdd:cd07144 480 V 480
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
11-483 |
0e+00 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 527.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKS 90
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ-----GEWAAMSPMERGRILRRAADLIRERNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 91 ELANLEAIDCGKPLDEAAW-DMDDVAGCFEYYADLAEGLDAKQktpLSLPMDTFkGYILKEPIGVVGMITPWNYPLLMAV 169
Cdd:TIGR01804 76 ELAKLETLDTGKTLQETIVaDMDSGADVFEFFAGLAPALNGEI---IPLGGPSF-AYTIREPLGVCVGIGAWNYPLQIAS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 170 WKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTS 249
Cdd:TIGR01804 152 WKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 250 AAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEE 329
Cdd:TIGR01804 232 AAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 330 GCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEH--LKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTE 407
Cdd:TIGR01804 312 ATEMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENvgLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789584901 408 DEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVK 483
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
10-486 |
0e+00 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 521.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnNGKDWARATGAVRAKYLRAIAAKVIERK 89
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAF---DNGPWPRLSPAERAAVLRRLADALEARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLDEAAW-DMDDVAGCFEYYADLAEGLDAKQKTPlslPMDTFKGYILKEPIGVVGMITPWNYPLLMA 168
Cdd:cd07139 78 DELARLWTAENGMPISWSRRaQGPGPAALLRYYAALARDFPFEERRP---GSGGGHVLVRREPVGVVAAIVPWNAPLFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 169 VWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGlGTEAGAPLASHPHVDKIVFTGSTTTGSSIMT 248
Cdd:cd07139 155 ALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 249 SAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFE 328
Cdd:cd07139 234 VCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 329 EGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTED 408
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789584901 409 EAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFcQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDF-GAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
23-483 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 517.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 23 KTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnNGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGK 102
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAF---ESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 103 PL-DEAAWDMDDVAGCFEYYAdlaEGLDaKQ--KTPLSLPMDTfkGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAG 179
Cdd:cd07112 79 PIsDALAVDVPSAANTFRWYA---EAID-KVygEVAPTGPDAL--ALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 180 CTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKL-VKPVS 258
Cdd:cd07112 153 NSVVLKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 259 LELGGKSPIIVFDDV-DIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVV 337
Cdd:cd07112 233 LECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 338 SKGQYERVLKFVSNARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDS 417
Cdd:cd07112 313 SEAHFDKVLGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789584901 418 QYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVK 483
Cdd:cd07112 393 VYGLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-487 |
2.73e-180 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 513.13 E-value: 2.73e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAF-----KTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYYADLAEGLDAkqkTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKP 186
Cdd:cd07103 76 ARGEVDYAASFLEWFAEEARRIYG---RTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 187 SELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSP 266
Cdd:cd07103 153 AEETPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 267 IIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVL 346
Cdd:cd07103 233 FIVFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 347 KFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVL 426
Cdd:cd07103 313 ALVEDAVAKGAKVLTGGKRLG--LGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1789584901 427 SNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVTQ 487
Cdd:cd07103 391 TRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
9-486 |
3.41e-180 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 514.20 E-value: 3.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnnGKDWARATGAVRAKYLRAIAaKVIER 88
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKL--GSPWRTMDASERGRLLNKLA-DLIER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KS-ELANLEAIDCGKPLDEAAW-DMDDVAGCFEYYADLAEGLDAKqktplSLPMD-TFKGYILKEPIGVVGMITPWNYPL 165
Cdd:cd07141 85 DRaYLASLETLDNGKPFSKSYLvDLPGAIKVLRYYAGWADKIHGK-----TIPMDgDFFTYTRHEPVGVCGQIIPWNFPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 166 LMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSS 245
Cdd:cd07141 160 LMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 246 IMTSAAKL-VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKIS 324
Cdd:cd07141 240 IQQAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 325 DPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRpeHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTF 404
Cdd:cd07141 320 NPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKR--HGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 405 STEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQ 484
Cdd:cd07141 398 KTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
..
gi 1789584901 485 VT 486
Cdd:cd07141 478 VT 479
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
27-485 |
5.90e-178 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 507.61 E-value: 5.90e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQ-----KEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYYADLAEGLDAKQktpLSLPMDTFkGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKP 186
Cdd:cd07090 76 ARVDIDSSADCLEYYAGLAPTLSGEH---VPLPGGSF-AYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 187 SELASLTCLELADICREVGLPPGVLNILTGlGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSP 266
Cdd:cd07090 152 SPFTPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 267 IIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVL 346
Cdd:cd07090 231 LIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 347 KFVSNARNEGATVLCGGVR---PEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAG 423
Cdd:cd07090 311 GYIESAKQEGAKVLCGGERvvpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789584901 424 AVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07090 391 GVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
9-485 |
1.61e-176 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 504.72 E-value: 1.61e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRNngkDWARATGAVRAKYLRAIAAKVIER 88
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEG---PWPRMTGYERSRILLRFADLLEKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAAW-DMDDVAGCFEYYADLAEGLDAkqktpLSLPMD-TFKGYILKEPIGVVGMITPWNYPLL 166
Cdd:cd07142 82 ADELAALETWDNGKPYEQARYaEVPLAARLFRYYAGWADKIHG-----MTLPADgPHHVYTLHEPIGVVGQIIPWNFPLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 167 MAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSI 246
Cdd:cd07142 157 MFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 247 MTSAAKL-VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISD 325
Cdd:cd07142 237 MQLAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 326 PFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFS 405
Cdd:cd07142 317 PFRKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIG--SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 406 TEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07142 395 TVDEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
9-490 |
1.96e-175 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 501.87 E-value: 1.96e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIER 88
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAF-----KTWGKTSVAERANILNKIADRIEEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEA-AWDMDDVAGCFEYYADLAEGldakQKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLM 167
Cdd:cd07559 77 LELLAVAETLDNGKPIRETlAADIPLAIDHFRYFAGVIRA----QEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 168 AVWKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIM 247
Cdd:cd07559 153 AAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 248 TSAAKLVKPVSLELGGKSPIIVFDDV-----DIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIK 322
Cdd:cd07559 232 QYAAENLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 323 ISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEH--LKKGYFVEPAIVSNVTTSMEIWREEVFGPALC 400
Cdd:cd07559 312 VGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 401 VKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYL 480
Cdd:cd07559 392 VITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQ 471
|
490
....*....|
gi 1789584901 481 SVKQVtqYIS 490
Cdd:cd07559 472 QTKNI--LVS 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
10-485 |
2.94e-174 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 498.98 E-value: 2.94e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTrnngKDWARA-TGAVRAKYLRAIAaKVIER 88
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFE----TDWGLKvSGSKRGRCLSKLA-DLMER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSE-LANLEAIDCGKPLDEAA-WDMDDVAGCFEYYADLAEGLDAKqktplSLPMDTFK-GYILKEPIGVVGMITPWNYPL 165
Cdd:cd07143 84 NLDyLASIEALDNGKTFGTAKrVDVQASADTFRYYGGWADKIHGQ-----VIETDIKKlTYTRHEPIGVCGQIIPWNFPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 166 LMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSS 245
Cdd:cd07143 159 LMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 246 IMTSAAKL-VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKIS 324
Cdd:cd07143 239 VMEAAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 325 DPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRpeHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTF 404
Cdd:cd07143 319 DPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKR--HGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 405 STEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQ 484
Cdd:cd07143 397 KTEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKA 476
|
.
gi 1789584901 485 V 485
Cdd:cd07143 477 V 477
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
27-485 |
9.53e-174 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 496.58 E-value: 9.53e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA-----WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AA-WDMDDVAGCFEYYADLAEGLDAKqktplSLPMD-TFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAIL 184
Cdd:cd07115 76 ARrLDVPRAADTFRYYAGWADKIEGE-----VIPVRgPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 185 KPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGK 264
Cdd:cd07115 151 KPAELTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 265 SPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYER 344
Cdd:cd07115 231 SANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 345 VLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGA 424
Cdd:cd07115 311 VLDYVDVGREEGARLLTGGKRPG--ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAG 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1789584901 425 VLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07115 389 VWTRDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-486 |
1.76e-172 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 493.68 E-value: 1.76e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFES----GWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYYADLAEGLDAKqktplSLPM-DTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILK 185
Cdd:cd07109 77 ARADVEAAARYFEYYGGAADKLHGE-----TIPLgPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 186 PSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKS 265
Cdd:cd07109 152 PAEDAPLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 266 PIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISdPFEEGCRLGPVVSKGQYERV 345
Cdd:cd07109 232 PQIVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 346 LKFVSNARNEGATVLCGGVRPE-HLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGA 424
Cdd:cd07109 311 EGFVARARARGARIVAGGRIAEgAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789584901 425 VLSNDLERCDRVSKAFQAGIVWVNCSQPCF-CQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07109 391 VWTRDGDRALRVARRLRAGQVFVNNYGAGGgIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
27-483 |
1.01e-170 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 488.58 E-value: 1.01e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAF-----PGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYYADLAEGLDAKQKTplslpmDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKP 186
Cdd:cd07106 76 AQFEVGGAVAWLRYTASLDLPDEVIEDD------DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 187 SELASLTCLELADICREVgLPPGVLNILTGlGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSP 266
Cdd:cd07106 150 SPFTPLCTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 267 IIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVL 346
Cdd:cd07106 228 AIVLPDVDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 347 KFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVL 426
Cdd:cd07106 308 ELVEDAKAKGAKVLAGGEPLD--GPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVW 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1789584901 427 SNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVK 483
Cdd:cd07106 386 SSDLERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQ 442
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
27-486 |
2.83e-170 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 487.60 E-value: 2.83e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAF-----PSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAwdMDDVAG---CFEYYADLAEGLDAKQKTPLslpMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAI 183
Cdd:cd07092 76 VR--DDELPGavdNFRFFAGAARTLEGPAAGEY---LPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 184 LKPSELASLTCLELADICREVgLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGG 263
Cdd:cd07092 151 LKPSETTPLTTLLLAELAAEV-LPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 264 KSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYE 343
Cdd:cd07092 230 KAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 344 RVLKFVSNARnEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAG 423
Cdd:cd07092 310 RVAGFVERAP-AHARVLTGGRRAE--GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLAS 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789584901 424 AVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07092 387 SVWTRDVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVM 449
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
9-485 |
3.75e-169 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 485.95 E-value: 3.75e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEpVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIER 88
Cdd:PRK13473 4 KLLINGELVA-GEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE-----WSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEA-AWDMDDVAGCFEYYADLA---EGLDAKQKTPlslpmdTFKGYILKEPIGVVGMITPWNYP 164
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLAlNDEIPAIVDVFRFFAGAArclEGKAAGEYLE------GHTSMIRRDPVGVVASIAPWNYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 165 LLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGS 244
Cdd:PRK13473 152 LMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 245 SIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKIS 324
Cdd:PRK13473 231 HVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 325 DPFEEGCRLGPVVSKGQYERVLKFVSNARNEG-ATVLCGGVRPEHlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKT 403
Cdd:PRK13473 311 DPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDG--KGYYYEPTLLAGARQDDEIVQREVFGPVVSVTP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 404 FSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVK 483
Cdd:PRK13473 389 FDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
..
gi 1789584901 484 QV 485
Cdd:PRK13473 469 HV 470
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-486 |
8.68e-169 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 484.15 E-value: 8.68e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 30 PATEDIIGYIPAATSEDVELAVEAARKAFTRNNgkdWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAW 109
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGP---WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 110 DMDDVAGCFEYYADLAEGLDAKQKTplSLPMDTFkGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSEL 189
Cdd:cd07118 81 EIEGAADLWRYAASLARTLHGDSYN--NLGDDML-GLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 190 ASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIV 269
Cdd:cd07118 158 TSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 270 FDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFV 349
Cdd:cd07118 238 FADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 350 SNARNEGATVLCGGVRPEHLkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSND 429
Cdd:cd07118 318 DAGRAEGATLLLGGERLASA-AGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1789584901 430 LERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07118 397 IDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTVH 453
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
9-494 |
7.68e-168 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 483.55 E-value: 7.68e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrNNGKdWARATGAVRAKYLRAIAAKVIER 88
Cdd:PLN02766 22 KLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAF--DHGP-WPRMSGFERGRIMMKFADLIEEH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGK-PLDEAAWDMDDVAGCFEYYADLAEGLDAKqktplSLPMD-TFKGYILKEPIGVVGMITPWNYPLL 166
Cdd:PLN02766 99 IEELAALDTIDAGKlFALGKAVDIPAAAGLLRYYAGAADKIHGE-----TLKMSrQLQGYTLKEPIGVVGHIIPWNFPST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 167 MAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSI 246
Cdd:PLN02766 174 MFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKI 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 247 MTSAAKL-VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISD 325
Cdd:PLN02766 254 MQAAATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 326 PFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFS 405
Cdd:PLN02766 334 PFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGD--KGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 406 TEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:PLN02766 412 TVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
....*....
gi 1789584901 486 TQYISDEPW 494
Cdd:PLN02766 492 VTPLYNSPW 500
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
27-485 |
3.46e-165 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 475.19 E-value: 3.46e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnNGKDWARaTGAVRAKYLRAIAAKVIERKSELANLEAIDCGKP--L 104
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAF---DTGDWST-DAEERARCLRQLHEALEARKEELRALLVAEVGAPvmT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 105 DEAAWDmDDVAGCFEYYADLAEGLDakQKTPLSLPMDTFKGY---ILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCT 181
Cdd:cd07089 77 ARAMQV-DGPIGHLRYFADLADSFP--WEFDLPVPALRGGPGrrvVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 182 AILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLEL 261
Cdd:cd07089 154 VVLKPAPDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 262 GGKSPIIVFDDVDIDKAVEwTMFGCFWTN-GQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKG 340
Cdd:cd07089 234 GGKSANIVLDDADLAAAAP-AAVGVCMHNaGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 341 QYERVLKFVSNARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYG 420
Cdd:cd07089 313 QRDRVEGYIARGRDEGARLVTGGGRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYG 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789584901 421 LAGAVLSNDLERCDRVSKAFQAGIVWVN---CSQPcfcQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07089 393 LSGGVWSADVDRAYRVARRIRTGSVGINgggGYGP---DAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
11-485 |
3.68e-165 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 475.60 E-value: 3.68e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKS 90
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQ-----KAWERLPAIERAAYLRKLADLIRENAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 91 ELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLA---EGldakQKTPLSLPMDTFkgYILKEPIGVVGMITPWNYPLLM 167
Cdd:cd07088 76 ELAKLIVEEQGKTLSLARVEVEFTADYIDYMAEWArriEG----EIIPSDRPNENI--FIFKVPIGVVAGILPWNFPFFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 168 AVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIM 247
Cdd:cd07088 150 IARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 248 TSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPF 327
Cdd:cd07088 230 EAAAENITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 328 EEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEhLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTE 407
Cdd:cd07088 310 DAATDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPE-GEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSL 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789584901 408 DEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07088 389 DEAIELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
4-485 |
7.03e-165 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 475.52 E-value: 7.03e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 4 TVPRRQLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAA 83
Cdd:PRK13252 3 RQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ-----KIWAAMTAMERSRILRRAVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 84 KVIERKSELANLEAIDCGKPLDEA-AWDMDDVAGCFEYYADLAEGLDAKQktpLSLPMDTFkGYILKEPIGVVGMITPWN 162
Cdd:PRK13252 78 ILRERNDELAALETLDTGKPIQETsVVDIVTGADVLEYYAGLAPALEGEQ---IPLRGGSF-VYTRREPLGVCAGIGAWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 163 YPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGtEAGAPLASHPHVDKIVFTGSTTT 242
Cdd:PRK13252 154 YPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 243 GSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIK 322
Cdd:PRK13252 233 GKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 323 ISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVR--PEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALC 400
Cdd:PRK13252 313 IGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERltEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 401 VKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYL 480
Cdd:PRK13252 393 VLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYT 472
|
....*
gi 1789584901 481 SVKQV 485
Cdd:PRK13252 473 QIKSV 477
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-486 |
2.82e-162 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 464.40 E-value: 2.82e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 52 EAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAeglDAK 131
Cdd:cd06534 1 AAARAAF-----KAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLA---DKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 132 QKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVL 211
Cdd:cd06534 73 GGPELPSPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 212 NILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNG 291
Cdd:cd06534 153 NVVPGGGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 292 QICSATSRLLVHERIADEFLDKLVkwtknikisdpfeegcrlgpvvskgqyervlkfvsnarnegatvlcggvrpehlkk 371
Cdd:cd06534 233 QICTAASRLLVHESIYDEFVEKLV-------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 372 gyfvepAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQ 451
Cdd:cd06534 257 ------TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSS 330
|
410 420 430
....*....|....*....|....*....|....*.
gi 1789584901 452 PCFC-QAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd06534 331 IGVGpEAPFGGVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
9-490 |
2.77e-161 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 465.78 E-value: 2.77e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIER 88
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAF-----KTWRKTTVAERANILNKIADIIDEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEA-AWDMDDVAGCFEYYAD--LAEGLDAKQ--KTPLSLpmdtfkgyILKEPIGVVGMITPWNY 163
Cdd:cd07117 77 KELLAMVETLDNGKPIRETrAVDIPLAADHFRYFAGviRAEEGSANMidEDTLSI--------VLREPIGVVGQIIPWNF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 164 PLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTG 243
Cdd:cd07117 149 PFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 244 SSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKI 323
Cdd:cd07117 228 RDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 324 SDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVR--PEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCV 401
Cdd:cd07117 308 GNPLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRltENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 402 KTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLS 481
Cdd:cd07117 388 IKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQ 467
|
....*....
gi 1789584901 482 VKQVtqYIS 490
Cdd:cd07117 468 MKNI--YID 474
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
27-486 |
7.70e-159 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 458.76 E-value: 7.70e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAF-----PEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYYADLAEGLDAKqktplSLPMDTFK-GYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILK 185
Cdd:cd07107 76 MLGDVMVAAALLDYFAGLVTELKGE-----TIPVGGRNlHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 186 PSELASLTCLELADICREVgLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKS 265
Cdd:cd07107 151 PPEQAPLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 266 PIIVFDDVDIDKAVEWTMFG--CFWTnGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYE 343
Cdd:cd07107 230 ALIVFPDADPEAAADAAVAGmnFTWC-GQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 344 RVLKFVSNARNEGATVLCGGVRPE--HLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGL 421
Cdd:cd07107 309 RVMHYIDSAKREGARLVTGGGRPEgpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGL 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1789584901 422 AGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07107 389 TAAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVN 453
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
11-485 |
5.51e-156 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 452.09 E-value: 5.51e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPvlRKTLPVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERK 89
Cdd:cd07097 4 YIDGEWVAG--GDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPA-----WRRTSPEARADILDKAGDELEARK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLDEAAWDMDDVAGCFEYYAdlAEGLDAKQKTPLSLPMDTFKgYILKEPIGVVGMITPWNYPLLMAV 169
Cdd:cd07097 77 EELARLLTREEGKTLPEARGEVTRAGQIFRYYA--GEALRLSGETLPSTRPGVEV-ETTREPLGVVGLITPWNFPIAIPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 170 WKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTS 249
Cdd:cd07097 154 WKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 250 AAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEE 329
Cdd:cd07097 234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 330 GCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDE 409
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDE 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789584901 410 AIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNC-SQPCFCQAPWGGTKRSGFG-RELGEWGLENYLSVKQV 485
Cdd:cd07097 394 ALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLpTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
7-485 |
3.79e-155 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 451.07 E-value: 3.79e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 7 RRQLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTrnngkDWARATGAVRAKYLRAIAAKVI 86
Cdd:PLN02278 24 RTQGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP-----SWSKLTASERSKILRRWYDLII 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 87 ERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADlaeglDAKQK----TPLSLPmDTfKGYILKEPIGVVGMITPWN 162
Cdd:PLN02278 99 ANKEDLAQLMTLEQGKPLKEAIGEVAYGASFLEYFAE-----EAKRVygdiIPSPFP-DR-RLLVLKQPVGVVGAITPWN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 163 YPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTT 242
Cdd:PLN02278 172 FPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 243 GSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIK 322
Cdd:PLN02278 252 GKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 323 ISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRpeHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVK 402
Cdd:PLN02278 332 VGDGFEEGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKR--HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLT 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 403 TFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSV 482
Cdd:PLN02278 410 RFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEI 489
|
...
gi 1789584901 483 KQV 485
Cdd:PLN02278 490 KYV 492
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
11-486 |
1.34e-152 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 443.71 E-value: 1.34e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPVLRKTLPVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERK 89
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAF-----PEWRKVPAPRRAEYLFRAAELLKKRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLDEAAWDMDDVAGCFEYYAdlAEGLDAK-QKTPLSLPmDTFkGYILKEPIGVVGMITPWNYPLLMA 168
Cdd:cd07131 77 EELARLVTREMGKPLAEGRGDVQEAIDMAQYAA--GEGRRLFgETVPSELP-NKD-AMTRRQPIGVVALITPWNFPVAIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 169 VWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMT 248
Cdd:cd07131 153 SWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 249 SAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFE 328
Cdd:cd07131 233 TCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 329 EGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEH--LKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFST 406
Cdd:cd07131 313 EETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 407 EDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNcsQPCF---CQAPWGGTKRSGFG-RELGEWGLENYLSV 482
Cdd:cd07131 393 LEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTIgaeVHLPFGGVKKSGNGhREAGTTALDAFTEW 470
|
....
gi 1789584901 483 KQVT 486
Cdd:cd07131 471 KAVY 474
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
9-494 |
2.28e-148 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 435.39 E-value: 2.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRNngkDWARATGAVRAKYLRAIAAKVIER 88
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEG---PWPKMTAYERSRILLRFADLLEKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAAW-DMDDVAGCFEYYADLAEGLDAkqktpLSLPMD-TFKGYILKEPIGVVGMITPWNYPLL 166
Cdd:PLN02466 136 NDELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHG-----LTVPADgPHHVQTLHEPIGVAGQIIPWNFPLL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 167 MAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSI 246
Cdd:PLN02466 211 MFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 247 MTSAAKL-VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISD 325
Cdd:PLN02466 291 LELAAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 326 PFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFS 405
Cdd:PLN02466 371 PFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFG--SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 406 TEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:PLN02466 449 DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
....*....
gi 1789584901 486 TQYISDEPW 494
Cdd:PLN02466 529 VTPLKNPAW 537
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
27-486 |
2.60e-148 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 432.17 E-value: 2.60e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPL-D 105
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF-----PEWAATPARERGKLLARIADALEARSEELARLLALETGNALrT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 106 EAAWDMDDVAGCFEYYADLAEglDAKQKTplsLPM--DTFKgYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAI 183
Cdd:cd07108 76 QARPEAAVLADLFRYFGGLAG--ELKGET---LPFgpDVLT-YTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 184 LKPSELASLTCLELADICREVgLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGG 263
Cdd:cd07108 150 LKAAEDAPLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 264 KSPIIVFDDVDIDKAVEWTMFGCFWT-NGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQY 342
Cdd:cd07108 229 KSPMIVFPDADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 343 ERVLKFVSNARNE-GATVLCGGVRPE--HLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQY 419
Cdd:cd07108 309 AKVCGYIDLGLSTsGATVLRGGPLPGegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHY 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1789584901 420 GLAGAVLSNDLERCDRVSKAFQAGIVWVNcsqPCFCQAP---WGGTKRSGFGRELG-EWGLENYLSVKQVT 486
Cdd:cd07108 389 GLAAYVWTRDLGRALRAAHALEAGWVQVN---QGGGQQPgqsYGGFKQSGLGREASlEGMLEHFTQKKTVN 456
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
10-480 |
4.44e-148 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 432.59 E-value: 4.44e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERK 89
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAF-----ESWSALPGHVRARHLYRIARHIQKHQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLDEAAwDMD--DVAGCFEYYADLAEGLDAKqktplslpmdtFKGYilkEPIGVVGMITPWNYPLLM 167
Cdd:cd07111 99 RLFAVLESLDNGKPIRESR-DCDipLVARHFYHHAGWAQLLDTE-----------LAGW---KPVGVVGQIVPWNFPLLM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 168 AVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGtEAGAPLASHPHVDKIVFTGSTTTGSSIM 247
Cdd:cd07111 164 LAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNG-SFGSALANHPGVDKVAFTGSTEVGRALR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 248 TSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPF 327
Cdd:cd07111 243 RATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 328 EEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTE 407
Cdd:cd07111 323 DKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP--SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789584901 408 DEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYL 480
Cdd:cd07111 401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
27-483 |
3.34e-141 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 413.75 E-value: 3.34e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDE 106
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAF-----KTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYYADLAEGLDAKQKTPlslPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKP 186
Cdd:TIGR01780 76 AKGEILYAASFLEWFAEEAKRVYGDTIPS---PQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 187 SELASLTCLELADICREVGLPPGVLNILTG-LGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKS 265
Cdd:TIGR01780 153 AEQTPLSALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 266 PIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERV 345
Cdd:TIGR01780 233 PFIVFDDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 346 LKFVSNARNEGATVLCGGVRpeHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAV 425
Cdd:TIGR01780 313 EKHIADAVEKGAKVVTGGKR--HELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYF 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1789584901 426 LSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVK 483
Cdd:TIGR01780 391 FSRDLSRIWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
11-479 |
1.79e-137 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 405.41 E-value: 1.79e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPvLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKS 90
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF-----KEWRKVPAPRRGEIVRQIGEALRKKKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 91 ELANLEAIDCGKPLDEA------AWDMddvagcfeyyADLAEGLD---AKQKTPLSLPmdtfkGYILKE---PIGVVGMI 158
Cdd:cd07086 76 ALGRLVSLEMGKILPEGlgevqeMIDI----------CDYAVGLSrmlYGLTIPSERP-----GHRLMEqwnPLGVVGVI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 159 TPWNYPllMAV--WKVAPSLAAGCTAILKPSELASLTCLELADICREV----GLPPGVLNILTGlGTEAGAPLASHPHVD 232
Cdd:cd07086 141 TAFNFP--VAVpgWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 233 KIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLD 312
Cdd:cd07086 218 LVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 313 KLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWRE 392
Cdd:cd07086 298 RLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 393 EVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAF--QAGIVWVNCsqPCF---CQAPWGGTKRSGF 467
Cdd:cd07086 378 ETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKgsDCGIVNVNI--PTSgaeIGGAFGGEKETGG 455
|
490
....*....|..
gi 1789584901 468 GRELGEWGLENY 479
Cdd:cd07086 456 GRESGSDAWKQY 467
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
46-486 |
2.29e-137 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 403.06 E-value: 2.29e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 46 DVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLA 125
Cdd:cd07104 1 DVDRAYAAAAAAQ-----KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 126 ---EGLDakqktplsLPMDTfKG---YILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTC-LELA 198
Cdd:cd07104 76 rrpEGEI--------LPSDV-PGkesMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 199 DICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKA 278
Cdd:cd07104 147 EIFEEAGLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 279 VEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGAT 358
Cdd:cd07104 227 VSAAAFGAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGAR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 359 VLCGGVRpehlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSK 438
Cdd:cd07104 307 LLTGGTY-----EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAE 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1789584901 439 AFQAGIVWVNCsQP--CFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07104 382 RLETGMVHIND-QTvnDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWIT 430
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
10-489 |
2.51e-137 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 406.22 E-value: 2.51e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEpvLRKTLPVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIER 88
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAF-----PTWRRTPPEERARLLLRAAALLRRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDtfkGYILkEPIGVVGMITPWNYPLLMA 168
Cdd:cd07124 108 RFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDN---RYVY-RPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 169 VWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMT 248
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 249 SAAKL------VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIK 322
Cdd:cd07124 264 RAAKVqpgqkwLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 323 ISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGaTVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVK 402
Cdd:cd07124 344 VGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 403 TFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVN--CSQPCFCQAPWGGTKRSGFG-RELGEWGLENY 479
Cdd:cd07124 423 KAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTGsKAGGPDYLLQF 502
|
490
....*....|
gi 1789584901 480 LSVKQVTQYI 489
Cdd:cd07124 503 MQPKTVTENF 512
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
25-470 |
2.73e-137 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 404.04 E-value: 2.73e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 25 LPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPL 104
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV-----MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 105 DEAAWDMDDVAGCFEYYADLAEGLDAKqktplSLPMDTFKG------YILKEPIGVVGMITPWNYPLLMAVWKVAPSLAA 178
Cdd:cd07145 76 KQSRVEVERTIRLFKLAAEEAKVLRGE-----TIPVDAYEYnerriaFTVREPIGVVGAITPFNFPANLFAHKIAPAIAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 179 GCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVS 258
Cdd:cd07145 151 GNSVVVKPSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 259 LELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVS 338
Cdd:cd07145 231 LELGGSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLIS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 339 KGQYERVLKFVSNARNEGATVLCGGVRPEhlkkGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQ 418
Cdd:cd07145 311 PEAVERMENLVNDAVEKGGKILYGGKRDE----GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1789584901 419 YGLAGAVLSNDLERCDRVSKAFQAGIVWVNcSQPCFCQ--APWGGTKRSGFGRE 470
Cdd:cd07145 387 YGLQASVFTNDINRALKVARELEAGGVVIN-DSTRFRWdnLPFGGFKKSGIGRE 439
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
28-487 |
5.24e-136 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 400.57 E-value: 5.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 28 VNPATEDIIGYIPAATSEDVELAVEAARKAFTRNngkDWARATgAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEA 107
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDET---DWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 108 AWDMDDVAGCFEYYADLAEGLDAKQKTP----LSLpmdtfkgyILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAI 183
Cdd:cd07120 78 RFEISGAISELRYYAGLARTEAGRMIEPepgsFSL--------VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 184 LKPSELASLTCLELADICREV-GLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELG 262
Cdd:cd07120 150 VKPAGQTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 263 GKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQY 342
Cdd:cd07120 230 GKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 343 ERVLKFVSNARNEGATVLC-GGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGL 421
Cdd:cd07120 310 DRVDRMVERAIAAGAEVVLrGGPVTEGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGL 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789584901 422 AGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVTQ 487
Cdd:cd07120 390 AASVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-483 |
2.64e-134 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 397.21 E-value: 2.64e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERKS 90
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA-----WGKTSVAERANILNKIADRMEANLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 91 ELANLEAIDCGKPLDEA-AWDMDDVAGCFEYYAdlaeGLDAKQKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAV 169
Cdd:cd07116 79 MLAVAETWDNGKPVRETlAADIPLAIDHFRYFA----GCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 170 WKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTS 249
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 250 AAKLVKPVSLELGGKSPIIVFDDVD------IDKAVE-WTMFGcfWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIK 322
Cdd:cd07116 234 ASENIIPVTLELGGKSPNIFFADVMdaddafFDKALEgFVMFA--LNQGEVCTCPSRALIQESIYDRFMERALERVKAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 323 ISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVR---PEHLKKGYFVEPAIVSNvtTSMEIWREEVFGPAL 399
Cdd:cd07116 312 QGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelGGLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 400 CVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENY 479
Cdd:cd07116 390 AVTTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHY 469
|
....
gi 1789584901 480 LSVK 483
Cdd:cd07116 470 QQTK 473
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-486 |
1.49e-133 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 394.28 E-value: 1.49e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 28 VNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEA 107
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQ-----RAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 108 AWDMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPS 187
Cdd:cd07099 76 GLEVLLALEAIDWAARNAPRVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 188 ELASLTCLELADICREVGLPPGVLNILTGLGtEAGAPLASHPhVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPI 267
Cdd:cd07099 156 EVTPLVGELLAEAWAAAGPPQGVLQVVTGDG-ATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 268 IVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLK 347
Cdd:cd07099 234 IVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 348 FVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLS 427
Cdd:cd07099 314 HVDDAVAKGAKALTGGARSN--GGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1789584901 428 NDLERCDRVSKAFQAGIVWVNC--SQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
29-486 |
2.16e-133 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 394.00 E-value: 2.16e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 29 NPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAA 108
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAF-----PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 109 WDMDDVAGCFEYYADLAEGLdaKQKTPLSLPMDTFKgYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSE 188
Cdd:cd07150 80 FETTFTPELLRAAAGECRRV--RGETLPSDSPGTVS-MSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 189 LASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPII 268
Cdd:cd07150 157 ETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 269 VFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKF 348
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 349 VSNARNEGATVLCGGVRpehlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSN 428
Cdd:cd07150 317 VEDAVAKGAKLLTGGKY-----DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789584901 429 DLERCDRVSKAFQAGIVWVNCS----QPcfcQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPtildEA---HVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
47-485 |
2.22e-133 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 392.98 E-value: 2.22e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 47 VELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAE 126
Cdd:cd07100 1 IEAALDRAHAAF-----LAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 127 GLDAKQKTPLSLPmdtfKGYILKEPIGVVGMITPWNYPLlmavWKV----APSLAAGCTAILKPSELASLTCLELADICR 202
Cdd:cd07100 76 AFLADEPIETDAG----KAYVRYEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 203 EVGLPPGVL-NILtgLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEW 281
Cdd:cd07100 148 EAGFPEGVFqNLL--IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 282 TMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLC 361
Cdd:cd07100 226 AVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 362 GGVRPEHlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQ 441
Cdd:cd07100 306 GGKRPDG--PGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLE 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1789584901 442 AGIVWVN---CSQPcfcQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07100 384 AGMVFINgmvKSDP---RLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
9-486 |
5.92e-133 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 394.17 E-value: 5.92e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnNGKDWARATGAVRAKYLRAIAAKVIER 88
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAF---ENGEWGKMNARDRGRLMYRLADLMEEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAawdMDDVAG----CFEYYADLAEGLDAKqktplSLPMDTFK-----GYILKEPIGVVGMIT 159
Cdd:cd07140 84 QEELATIESLDSGAVYTLA---LKTHVGmsiqTFRYFAGWCDKIQGK-----TIPINQARpnrnlTLTKREPIGVCGIVI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 160 PWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGS 239
Cdd:cd07140 156 PWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 240 TTTGSSIMTSAAKL-VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWT 318
Cdd:cd07140 236 TPIGKHIMKSCAVSnLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 319 KNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPA 398
Cdd:cd07140 316 KKMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVD--RPGFFFEPTVFTDVEDHMFIAKEESFGPI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 399 LCVKTFSTED--EAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGL 476
Cdd:cd07140 394 MIISKFDDGDvdGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEAL 473
|
490
....*....|
gi 1789584901 477 ENYLSVKQVT 486
Cdd:cd07140 474 NEYLKTKTVT 483
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
11-485 |
4.92e-132 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 391.39 E-value: 4.92e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPvlRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnNGkDWARATGAVRAKYLRAIAAKVIERKS 90
Cdd:TIGR03216 4 FINGAFVES--GKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAAL---KG-PWGKMTVAERADLLYAVADEIERRFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 91 ELANLEAIDCGKPLDEAA-WDMDDVAGCFEYYADLAegldaKQKTPLSLPMDTFKG-----YILKEPIGVVGMITPWNYP 164
Cdd:TIGR03216 78 DFLAAEVADTGKPRSLAShLDIPRGAANFRVFADVV-----KNAPTECFEMATPDGkgalnYAVRKPLGVVGVISPWNLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 165 LLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTE-AGAPLASHPHVDKIVFTGSTTTG 243
Cdd:TIGR03216 153 LLLMTWKVGPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPDsAGEFLTRHPGVDAITFTGETRTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 244 SSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKI 323
Cdd:TIGR03216 233 SAIMKAAADGVKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 324 SDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPE---HLKKGYFVEPAIVSNVTTSMEIWREEVFGPALC 400
Cdd:TIGR03216 313 GVPDDPATNMGPLISAEHRDKVLSYYALAVEEGATVVTGGGVPDfgdALAGGAWVQPTIWTGLPDSARVVTEEIFGPCCH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 401 VKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYL 480
Cdd:TIGR03216 393 IAPFDSEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYT 472
|
....*
gi 1789584901 481 SVKQV 485
Cdd:TIGR03216 473 ELTNV 477
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-486 |
1.18e-131 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 389.65 E-value: 1.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 25 LPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRNngkdwARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPL 104
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM-----KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 105 DEAawdMDDVAGCFEYYADLAEglDAKQKTPLSLPMDTFK------GYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAA 178
Cdd:cd07149 76 KDA---RKEVDRAIETLRLSAE--EAKRLAGETIPFDASPggegriGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 179 GCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAklVKPVS 258
Cdd:cd07149 151 GNAVVLKPASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 259 LELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVS 338
Cdd:cd07149 229 LELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 339 KGQYERVLKFVSNARNEGATVLCGGVRpehlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQ 418
Cdd:cd07149 309 EAEAERIEEWVEEAVEGGARLLTGGKR-----DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSP 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789584901 419 YGLAGAVLSNDLERCDRVSKAFQAGIVWVN-CSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07149 384 YGLQAGVFTNDLQKALKAARELEVGGVMINdSSTFRVDHMPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
10-486 |
9.08e-130 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 385.64 E-value: 9.08e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTrnngKDWARATGAVRAKYLRAIAAKVIERK 89
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV----SAWAKTTPAERGRILLRLADLIEQHG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLD-EAAWDMDDVAGCFEYYADLAEGLDAKQKTPlSLPM---DTFKGYILKEPIGVVGMITPWNYPL 165
Cdd:cd07113 78 EELAQLETLCSGKSIHlSRAFEVGQSANFLRYFAGWATKINGETLAP-SIPSmqgERYTAFTRREPVGVVAGIVPWNFSV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 166 LMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGtEAGAPLASHPHVDKIVFTGSTTTGSS 245
Cdd:cd07113 157 MIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVATGKK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 246 IMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISD 325
Cdd:cd07113 236 IGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 326 PFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFS 405
Cdd:cd07113 316 PMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA--GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 406 TEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07113 394 DEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
.
gi 1789584901 486 T 486
Cdd:cd07113 474 M 474
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
14-486 |
9.86e-125 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 372.02 E-value: 9.86e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 14 GQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAftrnnGKDWARATGAVRAKYLRAIAAKVIERKSELA 93
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA-----QKEWAATLPQERAEILEKAAQILEERRDEIV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 94 NLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKQktplsLPMDTfKG---YILKEPIGVVGMITPWNYPLLMAVW 170
Cdd:cd07151 76 EWLIRESGSTRIKANIEWGAAMAITREAATFPLRMEGRI-----LPSDV-PGkenRVYREPLGVVGVISPWNFPLHLSMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 171 KVAPSLAAGCTAILKPSELASLTC-LELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTS 249
Cdd:cd07151 150 SVAPALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 250 AAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEE 329
Cdd:cd07151 230 AGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 330 GCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRpehlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDE 409
Cdd:cd07151 310 DTVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEA-----EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEE 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789584901 410 AIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNcSQPCFCQ--APWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07151 385 ALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-DQPVNDEphVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
46-486 |
1.44e-122 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 365.36 E-value: 1.44e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 46 DVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLA 125
Cdd:cd07105 1 DADQAVEAAAAAF-----PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 126 EgldakQKTPLSLPMDTFKGY--ILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICRE 203
Cdd:cd07105 76 T-----QIIGGSIPSDKPGTLamVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 204 VGLPPGVLNILTGlgTEAGAP-----LASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKA 278
Cdd:cd07105 151 AGLPKGVLNVVTH--SPEDAPevveaLIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 279 VEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIkisdpFEEGCRLGPVVSKGQYERVLKFVSNARNEGAT 358
Cdd:cd07105 229 ANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKL-----FAGPVVLGSLVSAAAADRVKELVDDALSKGAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 359 VLCGGvRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSK 438
Cdd:cd07105 304 LVVGG-LADESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAK 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1789584901 439 AFQAGIVWVNCS----QPcfcQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07105 383 RIESGAVHINGMtvhdEP---TLPHGGVKSSGYGRFNGKWGIDEFTETKWIT 431
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
30-487 |
1.42e-118 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 356.23 E-value: 1.42e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 30 PATEDIIGYIPAATSEDVELAVEAARKAftrnnGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAW 109
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAA-----QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 110 DMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDTfKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSEL 189
Cdd:cd07101 78 EVLDVAIVARYYARRAERLLKPRRRRGAIPVLT-RTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 190 ASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHphVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIV 269
Cdd:cd07101 157 TALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 270 FDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFV 349
Cdd:cd07101 235 LEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 350 SNARNEGATVLCGGV-RPehlKKG-YFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLS 427
Cdd:cd07101 315 DDAVAKGATVLAGGRaRP---DLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789584901 428 NDLERCDRVSKAFQAGIVWVNCS-QPCFC--QAPWGGTKRSGFGRELGEWGLENYLSVKQVTQ 487
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNEGyAAAWAsiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
22-479 |
1.59e-118 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 358.42 E-value: 1.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 22 RKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAftrnnGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCG 101
Cdd:PRK09407 31 GPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA-----QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 102 KPLDEAAWDMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDTfKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCT 181
Cdd:PRK09407 106 KARRHAFEEVLDVALTARYYARRAPKLLAPRRRAGALPVLT-KTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 182 AILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLAshPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLEL 261
Cdd:PRK09407 185 VVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALV--DNADYLMFTGSTATGRVLAEQAGRRLIGFSLEL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 262 GGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQ 341
Cdd:PRK09407 263 GGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 342 YERVLKFVSNARNEGATVLCGGV-RPEhlkKG-YFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQY 419
Cdd:PRK09407 343 LETVSAHVDDAVAKGATVLAGGKaRPD---LGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPY 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1789584901 420 GLAGAVLSNDLERCDRVSKAFQAGIVWVN-------CSQpcfcQAPWGGTKRSGFGRELGEWGLENY 479
Cdd:PRK09407 420 GLNASVWTGDTARGRAIAARIRAGTVNVNegyaaawGSV----DAPMGGMKDSGLGRRHGAEGLLKY 482
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
25-486 |
3.21e-118 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 355.20 E-value: 3.21e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 25 LPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPL 104
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAEN-----RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 105 DEAAWDMDDVAGCFEYYADLAEGLDAKqktplSLPMDTFKG------YILKEPIGVVGMITPWNYPLLMAVWKVAPSLAA 178
Cdd:cd07094 76 KDARVEVDRAIDTLRLAAEEAERIRGE-----EIPLDATQGsdnrlaWTIREPVGVVLAITPFNFPLNLVAHKLAPAIAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 179 GCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKlvKPVS 258
Cdd:cd07094 151 GCPVVLKPASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 259 LELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVS 338
Cdd:cd07094 229 LELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 339 KGQYERVLKFVSNARNEGATVLCGGVRpehlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQ 418
Cdd:cd07094 309 EEAAERVERWVEEAVEAGARLLCGGER-----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTD 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 419 YGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSqPCFCQ--APWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07094 384 YGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS-SAFRTdwMPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
7-483 |
6.63e-117 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 352.67 E-value: 6.63e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 7 RRQLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVI 86
Cdd:PRK11241 10 RQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA-----WRALTAKERANILRRWFNLMM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 87 ERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAkqktplslpmDTFKGY-------ILKEPIGVVGMIT 159
Cdd:PRK11241 85 EHQDDLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYG----------DTIPGHqadkrliVIKQPIGVTAAIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 160 PWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGS 239
Cdd:PRK11241 155 PWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 240 TTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTK 319
Cdd:PRK11241 235 TEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 320 NIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGvRPeHLKKGYFVEPAIVSNVTTSMEIWREEVFGPAL 399
Cdd:PRK11241 315 KLHIGDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGG-KA-HELGGNFFQPTILVDVPANAKVAKEETFGPLA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 400 CVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENY 479
Cdd:PRK11241 393 PLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDY 472
|
....
gi 1789584901 480 LSVK 483
Cdd:PRK11241 473 LEIK 476
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
9-492 |
7.30e-117 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 353.05 E-value: 7.30e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRNngkDWARATGAVRAKYLRAIAAKVIER 88
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERG---DWSLSSPAKRKAVLNKLADLMEAH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAAwdMDDVAG---CFEYYADLAEGL--DAKQKTPLSLPMdtfkgyILKEPIGVVGMITPWNY 163
Cdd:PRK09847 98 AEELALLETLDTGKPIRHSL--RDDIPGaarAIRWYAEAIDKVygEVATTSSHELAM------IVREPVGVIAAIVPWNF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 164 PLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTG 243
Cdd:PRK09847 170 PLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 244 SSIMTSAAKL-VKPVSLELGGKSPIIVFDDV-DIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNI 321
Cdd:PRK09847 250 KQLLKDAGDSnMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 322 KISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHLKKGyfvePAIVSNVTTSMEIWREEVFGPALCV 401
Cdd:PRK09847 330 QPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIG----PTIFVDVDPNASLSREEIFGPVLVV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 402 KTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLS 481
Cdd:PRK09847 406 TRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTE 485
|
490
....*....|.
gi 1789584901 482 VKqvTQYISDE 492
Cdd:PRK09847 486 LK--TIWISLE 494
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
11-470 |
1.54e-116 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 351.49 E-value: 1.54e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPVlRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAftrnnGKDWARA-TGAVRAKYLRAIAAKVIERK 89
Cdd:cd07082 5 LINGEWKESS-GKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDA-----GRGWWPTmPLEERIDCLHKFADLLKENK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKqktplSLPMDTFK------GYILKEPIGVVGMITPWNY 163
Cdd:cd07082 79 EEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGD-----SLPGDWFPgtkgkiAQVRREPLGVVLAIGPFNY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 164 PLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTG 243
Cdd:cd07082 154 PLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 244 SSIMTSAAklVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKI 323
Cdd:cd07082 234 NRLKKQHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 324 SDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRpehlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKT 403
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGR----EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIR 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789584901 404 FSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSqpcfCQA-----PWGGTKRSGFGRE 470
Cdd:cd07082 388 VNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSK----CQRgpdhfPFLGRKDSGIGTQ 455
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-483 |
2.77e-115 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 347.70 E-value: 2.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 28 VNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEA 107
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQ-----KGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 108 AWDMDDVAGCFEYYADLAEGLDAKQKTPlslPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPS 187
Cdd:cd07102 76 GGEIRGMLERARYMISIAEEALADIRVP---EKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 188 ELASLTCLELADICREVGLPPGVLNILTgLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPI 267
Cdd:cd07102 153 PQTPLCGERFAAAFAEAGLPEGVFQVLH-LSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 268 IVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLK 347
Cdd:cd07102 232 YVRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 348 FVSNARNEGATVLCGGVR-PEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVL 426
Cdd:cd07102 312 QIADAIAKGARALIDGALfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVW 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789584901 427 SNDLERCDRVSKAFQAGIVWVNCsqpcfCQA-----PWGGTKRSGFGRELGEWGLENYLSVK 483
Cdd:cd07102 392 TKDIARAEALGEQLETGTVFMNR-----CDYldpalAWTGVKDSGRGVTLSRLGYDQLTRPK 448
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
34-472 |
1.49e-112 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 340.04 E-value: 1.49e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 34 DIIGYIPAATSEDVELAVEAARKAftrnnGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDD 113
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA-----QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 114 VAG-CFEyyadlAEGLdAKQKTPLSLPMDTFKGYILKE-PIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELAS 191
Cdd:cd07152 77 AIGeLHE-----AAGL-PTQPQGEILPSAPGRLSLARRvPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 192 LTC-LELADICREVGLPPGVLNILTGlGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVF 270
Cdd:cd07152 151 VSGgVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 271 DDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVS 350
Cdd:cd07152 230 DDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 351 NARNEGATVLCGGVRpehlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDL 430
Cdd:cd07152 310 DSVAAGARLEAGGTY-----DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDV 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1789584901 431 ERCDRVSKAFQAGIVWVNcSQP--CFCQAPWGGTKRSGFGRELG 472
Cdd:cd07152 385 GRAMALADRLRTGMLHIN-DQTvnDEPHNPFGGMGASGNGSRFG 427
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
27-486 |
2.58e-111 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 337.41 E-value: 2.58e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 27 VVNPATEDIIGYIPAATSEDVELAVEAA---RKAFTRNNgkdwaratgavRAKYLRAIAAKVIERKSELANLEAIDCGKP 103
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALAasyRSTLTRYQ-----------RSAILNKAAALLEARREEFARLITLESGLC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 104 LDEAAWDMDDVAGCFEYYADLAEGLDAKQ-KTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTA 182
Cdd:cd07146 72 LKDTRYEVGRAADVLRFAAAEALRDDGESfSCDLTANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 183 ILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAklVKPVSLELG 262
Cdd:cd07146 152 VLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 263 GKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQY 342
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 343 ERVLKFVSNARNEGATVLCGGVRpehlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLA 422
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQR-----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLS 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1789584901 423 GAVLSNDLERCDRVSKAFQAGIVWVNcSQPCF--CQAPWGGTKRSGFG-RELGEWGLENYLSVKQVT 486
Cdd:cd07146 385 SGVCTNDLDTIKRLVERLDVGTVNVN-EVPGFrsELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYS 450
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
25-483 |
4.52e-111 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 336.91 E-value: 4.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 25 LPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdwARATGA-VRAKYLRAIAAKVIERKSELANLEAIDCGKP 103
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRP------MRALPAhRRAAILLHCVARLEERFEELAETIVLEAGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 104 LDEAAWDMDDVAGCFEYYADLAEGLDAKQktplsLPMDT------FKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLA 177
Cdd:cd07147 75 IKDARGEVARAIDTFRIAAEEATRIYGEV-----LPLDIsargegRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 178 AGCTAILKPSELASLTCLELADICREVGLPPGVLNILTgLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKlvKPV 257
Cdd:cd07147 150 AGCPFVLKPASRTPLSALILGEVLAETGLPKGAFSVLP-CSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 258 SLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVV 337
Cdd:cd07147 227 VLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 338 SKGQYERVLKFVSNARNEGATVLCGGVRpehlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDS 417
Cdd:cd07147 307 SESEAERVEGWVNEAVDAGAKLLTGGKR-----DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDS 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789584901 418 QYGLAGAVLSNDLERCDRVSKAFQAGIVWVNcSQPCFC--QAPWGGTKRSGFGRELGEWGLENYLSVK 483
Cdd:cd07147 382 KFGLQAGVFTRDLEKALRAWDELEVGGVVIN-DVPTFRvdHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
10-466 |
1.19e-109 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 334.98 E-value: 1.19e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEpvLRKTLPVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIER 88
Cdd:PRK03137 39 LIIGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAF-----ETWKKWSPEDRARILLRAAAIIRRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAAwdmDDVAGC---FEYYAdlAEGLDAKQKTPLsLPMDTFKGYILKEPIGVVGMITPWNYPL 165
Cdd:PRK03137 112 KHEFSAWLVKEAGKPWAEAD---ADTAEAidfLEYYA--RQMLKLADGKPV-ESRPGEHNRYFYIPLGVGVVISPWNFPF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 166 -LMAVWKVAPsLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGS 244
Cdd:PRK03137 186 aIMAGMTLAA-IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 245 SIMTSAAKL------VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWT 318
Cdd:PRK03137 265 RIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 319 KNIKISDPfEEGCRLGPVVSKGQYERVLKFVSNARNEGaTVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPA 398
Cdd:PRK03137 345 KELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDD--SKGYFIQPTIFADVDPKARIMQEEIFGPV 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 399 LCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVN--CSQPCFCQAPWGGTKRSG 466
Cdd:PRK03137 421 VAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSG 490
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-486 |
3.41e-107 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 327.33 E-value: 3.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 28 VNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEA 107
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQ-----REWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 108 AwdMDDV-AGCFEYYADLAEGLDAKQKTPLSLPMDTF--KGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAIL 184
Cdd:cd07098 76 S--LGEIlVTCEKIRWTLKHGEKALRPESRPGGLLMFykRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 185 KPSELASLTCLELADICREV----GLPPGVLNILTGLGtEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLE 260
Cdd:cd07098 154 KVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 261 LGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKG 340
Cdd:cd07098 233 LGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 341 QYERVLKFVSNARNEGATVLCGGVRPEHLK--KGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQ 418
Cdd:cd07098 313 RFDRLEELVADAVEKGARLLAGGKRYPHPEypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 419 YGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCF--CQAPWGGTKRSGFGRELGEWGLENYLSVKQVT 486
Cdd:cd07098 393 YGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYyvQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
78-485 |
2.21e-106 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 323.23 E-value: 2.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 78 LRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLA---EGldakQKTPLSLPMDTFkgYILKEPIGV 154
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWArryEG----EIIQSDRPGENI--LLFKRALGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 155 VGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKI 234
Cdd:PRK10090 75 TTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 235 VFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKL 314
Cdd:PRK10090 155 SMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 315 VKWTKNIKISDPFEEG-CRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREE 393
Cdd:PRK10090 235 GEAMQAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE--GKGYYYPPTLLLDVRQEMSIMHEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 394 VFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGE 473
Cdd:PRK10090 313 TFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGK 392
|
410
....*....|..
gi 1789584901 474 WGLENYLSVKQV 485
Cdd:PRK10090 393 HGLHEYLQTQVV 404
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
9-468 |
1.62e-105 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 323.31 E-value: 1.62e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIER 88
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAF-----PAWSATPVLKRQQVMFKFRQLLEEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDTfkgYILKEPIGVVGMITPWNYPLLMA 168
Cdd:cd07085 77 LDELARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDT---YSYRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 169 VWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGlGTEAGAPLASHPHVDKIVFTGSTTTGSSIMT 248
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 249 SAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTM---FGCfwtNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISD 325
Cdd:cd07085 233 RAAANGKRVQALGGAKNHAVVMPDADLEQTANALVgaaFGA---AGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 326 PFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGG--VRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKT 403
Cdd:cd07085 310 GDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGrgVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789584901 404 FSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPC----FcqaPWGGTKRSGFG 468
Cdd:cd07085 390 VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPVplafF---SFGGWKGSFFG 455
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
10-489 |
1.62e-99 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 309.10 E-value: 1.62e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEPvlRKTLPVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIER 88
Cdd:TIGR01237 35 LVINGERVET--ENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAF-----EAWKKTDPEERAAILFKAAAIVRRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLdAKQKTPLSLPMDTfKGYIlKEPIGVVGMITPWNYPLLMA 168
Cdd:TIGR01237 108 RHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIEL-AKGKPVNSREGET-NQYV-YTPTGVTVVISPWNFPFAIM 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 169 VWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMT 248
Cdd:TIGR01237 185 VGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 249 SAAKL------VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIK 322
Cdd:TIGR01237 265 RAAKVqpgqkhLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 323 ISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPehlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVK 402
Cdd:TIGR01237 345 VGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLVSGGCGDD---SKGYFIGPTIFADVDRKARLAQEEIFGPVVAFI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 403 TFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVN--CSQPCFCQAPWGGTKRSGFGRELGewG---LE 477
Cdd:TIGR01237 422 RASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnITGAIVGYQPFGGFKMSGTDSKAG--GpdyLA 499
|
490
....*....|..
gi 1789584901 478 NYLSVKQVTQYI 489
Cdd:TIGR01237 500 LFMQAKTVTEMF 511
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
28-485 |
9.58e-93 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 289.72 E-value: 9.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 28 VNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEA 107
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARF-----RDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 108 AWDMDDVAGCFEYYADLAEGLDAKQktplslPMD-----TFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTA 182
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADE------PADaaavgASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 183 ILKPSELASLTCLELADICREVGLPPGVLNILTgLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELG 262
Cdd:PRK09406 155 LLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 263 GKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQY 342
Cdd:PRK09406 234 GSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 343 ERVLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLA 422
Cdd:PRK09406 314 DEVEKQVDDAVAAGATILCGGKRPD--GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789584901 423 GAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
13-472 |
7.79e-88 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 277.55 E-value: 7.79e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 13 GGQWTEPvlRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSEL 92
Cdd:cd07130 4 DGEWGGG--GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAF-----KEWRDVPAPKRGEIVRQIGDALRKKKEAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 93 ANLEAIDCGKPLDEAA---WDMDDVAgcfeyyaDLAEGLdAKQKTPLSLPMDTfKGYILKE---PIGVVGMITPWNYPll 166
Cdd:cd07130 77 GKLVSLEMGKILPEGLgevQEMIDIC-------DFAVGL-SRQLYGLTIPSER-PGHRMMEqwnPLGVVGVITAFNFP-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 167 MAV--WKVAPSLAAGCTAILKPSELASLTCLE----LADICREVGLPPGVLNILTGlGTEAGAPLASHPHVDKIVFTGST 240
Cdd:cd07130 146 VAVwgWNAAIALVCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGST 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 241 TTGSSI-MTSAAKLVKPVsLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTK 319
Cdd:cd07130 225 AVGRQVgQAVAARFGRSL-LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 320 NIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHlkKGYFVEPAIVSnVTTSMEIWREEVFGPAL 399
Cdd:cd07130 304 QVRIGDPLDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDG--PGNYVEPTIVE-GLSDAPIVKEETFAPIL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 400 CVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERcdrvskAFQ--------AGIVWVNCSQP------CFcqapwGGTKRS 465
Cdd:cd07130 381 YVLKFDTLEEAIAWNNEVPQGLSSSIFTTDLRN------AFRwlgpkgsdCGIVNVNIGTSgaeiggAF-----GGEKET 449
|
....*..
gi 1789584901 466 GFGRELG 472
Cdd:cd07130 450 GGGRESG 456
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
46-469 |
1.19e-83 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 265.29 E-value: 1.19e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 46 DVELAVEAARKAFTrnngkDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGcfeyYADLA 125
Cdd:cd07095 1 QVDAAVAAARAAFP-----GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAG----KIDIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 126 EgLDAKQKTPL-SLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREV 204
Cdd:cd07095 72 I-KAYHERTGErATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 205 GLPPGVLNILTGlGTEAGAPLASHPHVDKIVFTGSTTTGSSI-MTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTM 283
Cdd:cd07095 151 GLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 284 FGCFWTNGQICSATSRLLVHE-RIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCG 362
Cdd:cd07095 230 QSAFLTAGQRCTCARRLIVPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 363 GVRPEhlKKGYFVEPAIVsNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQA 442
Cdd:cd07095 310 MERLV--AGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRA 386
|
410 420 430
....*....|....*....|....*....|
gi 1789584901 443 GIvwVNCSQP---CFCQAPWGGTKRSGFGR 469
Cdd:cd07095 387 GI--VNWNRPttgASSTAPFGGVGLSGNHR 414
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
10-472 |
7.71e-81 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 260.20 E-value: 7.71e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTEPVLRKTlpVVNP-ATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIER 88
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAF-----KTWKDWPQEDRARLLLKAADLLRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 89 KSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDTFKGYIlkEPIGVVGMITPWNYPLLMA 168
Cdd:cd07083 94 RRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFY--VGLGAGVVISPWNFPVAIF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 169 VWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMT 248
Cdd:cd07083 172 TGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 249 SAAKL------VKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIK 322
Cdd:cd07083 252 AAARLapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 323 ISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGaTVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVK 402
Cdd:cd07083 332 VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLE--GEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVI 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1789584901 403 TFSTED--EAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQ--PCFCQAPWGGTKRSGFGRELG 472
Cdd:cd07083 409 RYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKItgALVGVQPFGGFKLSGTNAKTG 482
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
28-485 |
5.52e-77 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 249.01 E-value: 5.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 28 VNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEA 107
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGF-----RDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 108 AWDMDDVAGCFEYYADLAEGLDAKQKTPLslpmDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPS 187
Cdd:PRK13968 87 RAEVAKSANLCDWYAEHGPAMLKAEPTLV----ENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 188 ELASLTCLELADICREVGLPPGVLNILTGlgTEAGAPLA-SHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSP 266
Cdd:PRK13968 163 PNVMGCAQLIAQVFKDAGIPQGVYGWLNA--DNDGVSQMiNDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 267 IIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVL 346
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 347 KFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVL 426
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIA--GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1789584901 427 SNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
10-466 |
1.62e-76 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 248.33 E-value: 1.62e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQWTE---PVLRKTlpvvNPATEDIIGYIPAATSEDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVI 86
Cdd:PRK09457 3 LWINGDWIAgqgEAFESR----NPVSGEVLWQGNDATAAQVDAAVRAARAAF-----PAWARLSFEERQAIVERFAALLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 87 ERKSELANLEAIDCGKPLDEAAWDMDDVAGcfeyyadlaegldakqKTPLSL------------PMDTFKGYILKEPIGV 154
Cdd:PRK09457 74 ENKEELAEVIARETGKPLWEAATEVTAMIN----------------KIAISIqayhertgekrsEMADGAAVLRHRPHGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 155 VGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGlGTEAGAPLASHPHVDKI 234
Cdd:PRK09457 138 VAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 235 VFTGSTTTGSSIMTS-AAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERI-ADEFLD 312
Cdd:PRK09457 217 LFTGSANTGYLLHRQfAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 313 KLVKWTKNIKISDPFEEGCR-LGPVVSKGQYERVLKFVSNARNEGATVLcggVRPEHLKKGY-FVEPAIVsNVTTSMEIW 390
Cdd:PRK09457 297 RLVAVAKRLTVGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSL---LEMTQLQAGTgLLTPGII-DVTGVAELP 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1789584901 391 REEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIvwVNCSQP---CFCQAPWGGTKRSG 466
Cdd:PRK09457 373 DEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGI--VNWNKPltgASSAAPFGGVGASG 449
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
60-475 |
1.94e-75 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 244.06 E-value: 1.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 60 RNNGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAawDMDDVAGCFEYYADLAEGLDA-----KQKT 134
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEV--DLTEILPVLSEINHAIKHLKKwmkpkRVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 135 PLSLPMDtfKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPGVLNIL 214
Cdd:cd07134 86 PLLLFGT--KSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREA-FDEDEVAVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 215 TGlGTEAGAPLASHPhVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQIC 294
Cdd:cd07134 163 EG-DAEVAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 295 SATSRLLVHERIADEFLDKLVKW-TKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHlkkGY 373
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEiEKFYGKDAARKASPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAA---QR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 374 FVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNcsqPC 453
Cdd:cd07134 318 YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN---DV 394
|
410 420
....*....|....*....|....*..
gi 1789584901 454 FCQA-----PWGGTKRSGFGRELGEWG 475
Cdd:cd07134 395 VLHFlnpnlPFGGVNNSGIGSYHGVYG 421
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
50-478 |
9.73e-75 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 242.05 E-value: 9.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 50 AVEAARKAFtrnngkdwarATG-----AVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWdmddvagcFEYYADL 124
Cdd:cd07087 3 LVARLRETF----------LTGktrslEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYL--------TEIAVVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 125 AEGLDAKQK-------TPLSLPMDTF--KGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCL 195
Cdd:cd07087 65 GEIDHALKHlkkwmkpRRVSVPLLLQpaKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 196 ELADICREVgLPPGVLNILTGLGTEAGAPLAsHPhVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDI 275
Cdd:cd07087 145 LLAKLIPKY-FDPEAVAVVEGGVEVATALLA-EP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 276 DKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCrLGPVVSKGQYERVLKFVsnarnE 355
Cdd:cd07087 222 EVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPD-YGRIINERHFDRLASLL-----D 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 356 GATVLCGGvrpEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDR 435
Cdd:cd07087 296 DGKVVIGG---QVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQER 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1789584901 436 VSKAFQAGIVWVNcsqPCFCQA-----PWGGTKRSGFGRELGEWGLEN 478
Cdd:cd07087 373 VLAETSSGGVCVN---DVLLHAaipnlPFGGVGNSGMGAYHGKAGFDT 417
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
45-475 |
2.69e-72 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 235.96 E-value: 2.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 45 EDVELAVEAARKAFTRNNGKD--WaratgavRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAawDMDDVAGCFEYYA 122
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDleY-------RLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFET--LLTEVSGVKNDIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 123 DLAEGLD--AKQKTP--LSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELA 198
Cdd:cd07135 76 HMLKNLKkwAKDEKVkdGPLAFMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 199 DICREvGLPPGVLNILTGLGTEAGAPLASHphVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKA 278
Cdd:cd07135 156 ELVPK-YLDPDAFQVVQGGVPETTALLEQK--FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 279 VEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGcRLGPVVSKGQYERVLKFVSNARnegAT 358
Cdd:cd07135 233 AKRILWGKFGNAGQICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDTTK---GK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 359 VLCGGVRPEHLKkgyFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSK 438
Cdd:cd07135 309 VVIGGEMDEATR---FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILT 385
|
410 420 430
....*....|....*....|....*....|....*....
gi 1789584901 439 AFQAGIVWVNCS--QPCFCQAPWGGTKRSGFGRELGEWG 475
Cdd:cd07135 386 RTRSGGVVINDTliHVGVDNAPFGGVGDSGYGAYHGKYG 424
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
11-480 |
4.11e-72 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 237.86 E-value: 4.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPvlRKTLPVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERK 89
Cdd:cd07125 36 IINGEETET--GEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAG-----WSATPVEERAEILEKAADLLEANR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLDEAawdMDDV--AGCF-EYYADLAEGLDAKQKTPLslPMDTFKGYILkEPIGVVGMITPWNYPLL 166
Cdd:cd07125 109 GELIALAAAEAGKTLADA---DAEVreAIDFcRYYAAQARELFSDPELPG--PTGELNGLEL-HGRGVFVCISPWNFPLA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 167 MAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSI 246
Cdd:cd07125 183 IFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 247 MTSAAKLVK---PVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKI 323
Cdd:cd07125 263 NRALAERDGpilPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 324 SDPFEEGCRLGPVVSKGQYERVLKFVSNARNEgATVLCGGVRPEhlKKGYFVEPAIVSNVttsmEIW--REEVFGPALCV 401
Cdd:cd07125 343 GDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDD--GNGYFVAPGIIEIV----GIFdlTTEVFGPILHV 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 402 KTFSTE--DEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVN--------CSQPcFcqapwGGTKRSGFGREL 471
Cdd:cd07125 416 IRFKAEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINrnitgaivGRQP-F-----GGWGLSGTGPKA 489
|
....*....
gi 1789584901 472 GEWgleNYL 480
Cdd:cd07125 490 GGP---NYL 495
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
11-468 |
5.19e-70 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 231.57 E-value: 5.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAftrnnGKDWARATGAVRAKYLRAIAAKVIERKS 90
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA-----QKAWAKTPLWKRAELLHKAAAILKEHKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 91 ELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADlaEGLDAKQKTPLsLPMDTFKG-----YIL--KEPIGVVGMITPWNY 163
Cdd:PLN00412 94 PIAECLVKEIAKPAKDAVTEVVRSGDLISYTAE--EGVRILGEGKF-LVSDSFPGnernkYCLtsKIPLGVVLAIPPFNY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 164 PLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGStTTG 243
Cdd:PLN00412 171 PVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 244 SSIMTSAAKLvkPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKI 323
Cdd:PLN00412 250 IAISKKAGMV--PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 324 SDPfEEGCRLGPVVSKGQYERVLKFVSNARNEGATvlcggVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKT 403
Cdd:PLN00412 328 GPP-EDDCDITPVVSESSANFIEGLVMDAKEKGAT-----FCQEWKREGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIR 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 404 FSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNcSQPC-----FcqaPWGGTKRSGFG 468
Cdd:PLN00412 402 INSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQIN-SAPArgpdhF---PFQGLKDSGIG 467
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
55-475 |
3.65e-69 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 227.75 E-value: 3.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 55 RKAFTRNNGKDWAratgaVRAKYLRAIAAKVIERKSELAnlEAI--DCG-KPLDEAawDMDDVAGCFEYYADLAEGLD-- 129
Cdd:cd07133 8 KAAFLANPPPSLE-----ERRDRLDRLKALLLDNQDALA--EAIsaDFGhRSRHET--LLAEILPSIAGIKHARKHLKkw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 130 ---AKQKTPLSL-PMdtfKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVg 205
Cdd:cd07133 79 mkpSRRHVGLLFlPA---KAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 206 LPPGVLNILTGlGTEAGAPLASHPhVDKIVFTGSTTTGSSIMTSAAK-LVkPVSLELGGKSPIIVFDDVDIDKAVEWTMF 284
Cdd:cd07133 155 FDEDEVAVVTG-GADVAAAFSSLP-FDHLLFTGSTAVGRHVMRAAAEnLT-PVTLELGGKSPAIIAPDADLAKAAERIAF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 285 GCFWTNGQICSATSRLLVHERIADEFLDKLVKWTK----NIKISDPFeegcrlGPVVSKGQYERVLKFVSNARNEGATVL 360
Cdd:cd07133 232 GKLLNAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAkmypTLADNPDY------TSIINERHYARLQGLLEDARAKGARVI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 361 CGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAF 440
Cdd:cd07133 306 ELNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRT 385
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1789584901 441 QAGIVWVN-----CSQPcfcQAPWGGTKRSGFGRELGEWG 475
Cdd:cd07133 386 HSGGVTINdtllhVAQD---DLPFGGVGASGMGAYHGKEG 422
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
131-479 |
1.41e-63 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 213.52 E-value: 1.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 131 KQKTPLS-LPMdtfKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPG 209
Cdd:cd07136 82 RVKTPLLnFPS---KSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 210 VLNILTGLGTEAGAPLASHphVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWT 289
Cdd:cd07136 158 YVAVVEGGVEENQELLDQK--FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 290 NGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGcRLGPVVSKGQYERVLKFVsnarnEGATVLCGGvrpEHL 369
Cdd:cd07136 236 AGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESP-DYGRIINEKHFDRLAGLL-----DNGKIVFGG---NTD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 370 KKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVN- 448
Cdd:cd07136 307 RETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINd 386
|
330 340 350
....*....|....*....|....*....|....*
gi 1789584901 449 ----CSQPcfcQAPWGGTKRSGFGRELGEWGLENY 479
Cdd:cd07136 387 timhLANP---YLPFGGVGNSGMGSYHGKYSFDTF 418
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
25-468 |
1.14e-62 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 211.12 E-value: 1.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 25 LPVVNPATEDIIGYIPAATSEDVELAVEAARKAF-TRNNgkdWARATGavRAKYLRAIAAKVIERKSELANLEAIDCGKP 103
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNN---WLPAHE--RIAILERLADLMEERADELALLIAREGGKP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 104 LDEAAWD----MDDVAGCFEYYADLAeGLDakqktplsLPMDTFK------GYILKEPIGVVGMITPWNYPLLMAVWKVA 173
Cdd:cd07148 76 LVDAKVEvtraIDGVELAADELGQLG-GRE--------IPMGLTPasagriAFTTREPIGVVVAISAFNHPLNLIVHQVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 174 PSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTgLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKL 253
Cdd:cd07148 147 PAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLAPG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 254 VKpVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRL 333
Cdd:cd07148 226 TR-CALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 334 GPVVSKGQYERVLKFVSNARNEGATVLCGGVRpehLKKGYFvEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQL 413
Cdd:cd07148 305 GPLIRPREVDRVEEWVNEAVAAGARLLCGGKR---LSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQ 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1789584901 414 ANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNcSQPCFCQ--APWGGTKRSGFG 468
Cdd:cd07148 381 ANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVN-DHTAFRVdwMPFAGRRQSGYG 436
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-493 |
1.62e-60 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 209.22 E-value: 1.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 6 PRRQLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKV 85
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL-----WRNTPITTRQRVMLKFQELI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 86 IERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEgLDAKQKTP-LSLPMDTfkgYILKEPIGVVGMITPWNYP 164
Cdd:PLN02419 187 RKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMAT-LQMGEYLPnVSNGVDT---YSIREPLGVCAGICPFNFP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 165 LLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGApLASHPHVDKIVFTGSTTTGS 244
Cdd:PLN02419 263 AMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGM 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 245 SIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRlLVHERIADEFLDKLVKWTKNIKIS 324
Cdd:PLN02419 342 HIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALST-VVFVGDAKSWEDKLVERAKALKVT 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 325 DPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGG---VRPEHlKKGYFVEPAIVSNVTTSMEIWREEVFGPALCV 401
Cdd:PLN02419 421 CGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGrdiVVPGY-EKGNFIGPTILSGVTPDMECYKEEIFGPVLVC 499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 402 KTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGREL---GEWGLEN 478
Cdd:PLN02419 500 MQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLnfyGKAGVDF 579
|
490
....*....|....*
gi 1789584901 479 YLSVKQVTQYISDEP 493
Cdd:PLN02419 580 FTQIKLVTQKQKDIH 594
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
41-487 |
5.65e-59 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 202.57 E-value: 5.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 41 AATSEDVELAVEAARKAFtrNNGKDWARATgavRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAawdmddvagCF-E 119
Cdd:PTZ00381 3 PDNPEIIPPIVKKLKESF--LTGKTRPLEF---RKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFET---------KMtE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 120 YYADLAE------GLD---AKQKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELA 190
Cdd:PTZ00381 69 VLLTVAEiehllkHLDeylKPEKVDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 191 SLTCLELADICREVgLPPGVLNILTGlGTEAGAPLASHPhVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVF 270
Cdd:PTZ00381 149 PHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTELLKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 271 DDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCrLGPVVSKGQYERVLKFVs 350
Cdd:PTZ00381 226 KSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSED-YSRIVNEFHTKRLAELI- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 351 naRNEGATVLCGGvrpEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDL 430
Cdd:PTZ00381 304 --KDHGGKVVYGG---EVDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDK 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789584901 431 ERCDRVSKAFQAGIVWVNcsqPCFCQA-----PWGGTKRSGFGRELGEWGLENYLSVKQVTQ 487
Cdd:PTZ00381 379 RHKELVLENTSSGAVVIN---DCVFHLlnpnlPFGGVGNSGMGAYHGKYGFDTFSHPKPVLN 437
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
26-451 |
4.46e-54 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 196.19 E-value: 4.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 26 PVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPL 104
Cdd:PRK11904 565 PVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPA-----WSRTPVEERAAILERAADLLEANRAELIALCVREAGKTL 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 105 DEAawdMDDV--AGCF-EYYADLAEGLDAKqktPLSLPMDTfkG---YILKEPIGVVGMITPWNYPLLMAVWKVAPSLAA 178
Cdd:PRK11904 640 QDA---IAEVreAVDFcRYYAAQARRLFGA---PEKLPGPT--GesnELRLHGRGVFVCISPWNFPLAIFLGQVAAALAA 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 179 GCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSI-MTSAAKLVKPV 257
Cdd:PRK11904 712 GNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTLAARDGPIV 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 258 SL--ELGGKSPII---------VFDDVdIDKAvewtmfgcFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDP 326
Cdd:PRK11904 792 PLiaETGGQNAMIvdstalpeqVVDDV-VTSA--------FRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDP 862
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 327 FEEGCRLGPVVSKGQYERVLKFVSNARNEgATVLCGGVRPEHLKKGYFVEPAIVSnvTTSMEIWREEVFGPALCVKTFST 406
Cdd:PRK11904 863 RLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPLPAGTENGHFVAPTAFE--IDSISQLEREVFGPILHVIRYKA 939
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1789584901 407 ED-----EAIqlaNDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQ 451
Cdd:PRK11904 940 SDldkviDAI---NATGYGLTLGIHSRIEETADRIADRVRVGNVYVNRNQ 986
|
|
| D1pyr5carbox1 |
TIGR01236 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two ... |
10-466 |
1.39e-53 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 1; This model represents one of two related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. The two branches are not as closely related to each other as some aldehyde dehydrogenases are to this branch, and separate models are built for this reason. The enzyme is the second of two in the degradation of proline to glutamate. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273517 Cd Length: 532 Bit Score: 188.84 E-value: 1.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 10 LFIGGQ--WTEPVlrkTLPVVNPATED-IIGYIPAATSEDVELAVEAARKAftrnnGKDWARATGAVRAK-YLRAIAAKV 85
Cdd:TIGR01236 34 LVIGGEevYDSNE---RIPQVNPHNHQaVLAKATNATEEDAMKAVEAALDA-----KKDWSNLPFYDRAAiFLKAADLLS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 86 IERKSELANLEAIDCGKPLDEAawDMDDVAGC---FEYYADLAEGLDAKQktPLSLPMDTFKgyILKEPI-GVVGMITPW 161
Cdd:TIGR01236 106 GPYRYEILAATMLGQSKTVYQA--EIDAVAELidfFRFNVKYARELYAQQ--PISAPGEWNR--TEYRPLeGFVYAISPF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 162 NYPLLMAVWKVAPSLAaGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTT 241
Cdd:TIGR01236 180 NFTAIAGNLAGAPALM-GNTVVWKPSQTAALSNYLLMRILEEAGLPPGVINFVPGDGVQVSDQVLADPDLAGIHFTGSTN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 242 TGSSIMTS-AAKLVK----P-VSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLV 315
Cdd:TIGR01236 259 TFKHLWKKvAQNLDRyhnfPrIVGETGGKDFHLVHPSADISHAVLGTIRGAFEYQGQKCSAASRLYVPHSKWPEFKSDLL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 316 KWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARN--EGATVLCGGVRPEhlKKGYFVEPAIVSNVTTSMEIWREE 393
Cdd:TIGR01236 339 AELQSVKVGDPDDFRGFMGAVIDEQSFDKIVKYIEDAKKdpEALTILYGGKYDD--SQGYFVEPTVVESKDPDHPLMSEE 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 394 VFGPALCVKTFSTE--DEAIQLA-NDSQYGLAGAVLSNDLERCDRVSKA--FQAGIVWVN--CSQPCFCQAPWGGTKRSG 466
Cdd:TIGR01236 417 IFGPVLTVYVYPDDkyKEILDLVdSTSQYGLTGAVFAKDRKAILEADKKlrFAAGNFYINdkCTGAVVGQQPFGGARMSG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
50-477 |
1.50e-51 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 181.27 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 50 AVEAARKAFtrNNGK----DWaratgavRAKYLRAIAAKVIERKSELanLEAI--DCGKPLDEAAwdMDDVAGCFEYYAD 123
Cdd:cd07132 3 AVRRAREAF--SSGKtrplEF-------RIQQLEALLRMLEENEDEI--VEALakDLRKPKFEAV--LSEILLVKNEIKY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 124 LAEGLDA-----KQKTPLSLPMDTFkgYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELA 198
Cdd:cd07132 70 AISNLPEwmkpePVKKNLATLLDDV--YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 199 DIcrevgLP----PGVLNILTGlGTEAGAPLASHpHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVD 274
Cdd:cd07132 148 EL-----IPkyldKECYPVVLG-GVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 275 IDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPfEEGCRLGPVVSKGQYERVLKFVsnarn 354
Cdd:cd07132 221 IDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDP-KESPDYGRIINDRHFQRLKKLL----- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 355 EGATVLCGGvrpEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCD 434
Cdd:cd07132 295 SGGKVAIGG---QTDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVIN 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1789584901 435 RVSKAFQAGIVwvnCSQPCFCQA-----PWGGTKRSGFGRELGEWGLE 477
Cdd:cd07132 372 KILSNTSSGGV---CVNDTIMHYtldslPFGGVGNSGMGAYHGKYSFD 416
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
47-485 |
4.96e-51 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 179.53 E-value: 4.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 47 VELAVEAARKAFT--RNNGKDWaratgavRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAwdMDDVaGCFEYYADL 124
Cdd:cd07137 1 APRLVRELRETFRsgRTRSAEW-------RKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESF--RDEV-SVLVSSCKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 125 A-EGLD---AKQKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADI 200
Cdd:cd07137 71 AiKELKkwmAPEKVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 201 CREVgLPPGVLNILTGlGTEAGAPLASHpHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVE 280
Cdd:cd07137 151 IPEY-LDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 281 WTM---FGCfwTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCrLGPVVSKGQYERVLKFVSNARNEgA 357
Cdd:cd07137 228 RIAggkWGC--NNGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKD-LSRIVNSHHFQRLSRLLDDPSVA-D 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 358 TVLCGGVRPEhlkKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVS 437
Cdd:cd07137 304 KIVHGGERDE---KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIV 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1789584901 438 KAFQAGIVWVN-CSQPCFCQA-PWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:cd07137 381 AETSSGGVTFNdTVVQYAIDTlPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
18-448 |
3.26e-50 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 185.14 E-value: 3.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 18 EPVLRKTLPVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERKSELANL- 95
Cdd:COG4230 565 EAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPA-----WSATPVEERAAILERAADLLEAHRAELMALl 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 96 --EAidcGKPLDEAawdmddVAgcfE---------YYADLAEGLDAkQKTPLslpmdtfkgyilkEPIGVVGMITPWNYP 164
Cdd:COG4230 640 vrEA---GKTLPDA------IA---EvreavdfcrYYAAQARRLFA-APTVL-------------RGRGVFVCISPWNFP 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 165 LLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGS 244
Cdd:COG4230 694 LAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETAR 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 245 SI-MTSAAKLVKPVSL--ELGGKSPIIV---------FDDVdIDKAvewtmfgcFWTNGQICSATSRLLVHERIADEFLD 312
Cdd:COG4230 774 LInRTLAARDGPIVPLiaETGGQNAMIVdssalpeqvVDDV-LASA--------FDSAGQRCSALRVLCVQEDIADRVLE 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 313 KLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGaTVLCGGVRPEHLKKGYFVEPAIVsnvttsmEIWR- 391
Cdd:COG4230 845 MLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RLVHQLPLPEECANGTFVAPTLI-------EIDSi 916
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1789584901 392 ----EEVFGPALCVKTFSTED-----EAIqlaNDSQYGLAGAVLS-NDlERCDRVSKAFQAGIVWVN 448
Cdd:COG4230 917 sdleREVFGPVLHVVRYKADEldkviDAI---NATGYGLTLGVHSrID-ETIDRVAARARVGNVYVN 979
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
7-468 |
5.11e-50 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 184.30 E-value: 5.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 7 RRQLFIGGQWT-------EPVLRKTLPVVNPA-TEDIIGYIPAATSEDVELAVEAARKAFTrnngkDWARATGAVRAKYL 78
Cdd:PRK11905 544 ALNAFAAKTWHaapllagGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFP-----EWSATPAAERAAIL 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 79 RAIAAKVIERKSELANLEAIDCGKPLdeaawdMDDVAGCFE------YYADLAEGLDAKQKTplslpmdtfkgyilkEPI 152
Cdd:PRK11905 619 ERAADLMEAHMPELFALAVREAGKTL------ANAIAEVREavdflrYYAAQARRLLNGPGH---------------KPL 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 153 GVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVD 232
Cdd:PRK11905 678 GPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIA 757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 233 KIVFTGSTTTGSSI-MTSAAKLVKPVSL--ELGGKSPIIV---------FDDVdIDKAvewtmfgcFWTNGQICSATSRL 300
Cdd:PRK11905 758 GVMFTGSTEVARLIqRTLAKRSGPPVPLiaETGGQNAMIVdssalpeqvVADV-IASA--------FDSAGQRCSALRVL 828
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 301 LVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVrPEHLKKGYFVEPAIV 380
Cdd:PRK11905 829 CLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPL-PAETEKGTFVAPTLI 907
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 381 SnvTTSMEIWREEVFGPALCVKTFSTE--DEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVN--------CS 450
Cdd:PRK11905 908 E--IDSISDLEREVFGPVLHVVRFKADelDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniigavvGV 985
|
490
....*....|....*...
gi 1789584901 451 QpcfcqaPWGGTKRSGFG 468
Cdd:PRK11905 986 Q------PFGGEGLSGTG 997
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-480 |
9.22e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.10 E-value: 9.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWtepvlRKTLPVV---NPATEDIIGYIPAATSEDVELAVEAARKAftrnnGKDWARATGAVRAKYLRAIAAKVIE 87
Cdd:PLN02315 24 YVGGEW-----RANGPLVssvNPANNQPIAEVVEASLEDYEEGLRACEEA-----AKIWMQVPAPKRGEIVRQIGDALRA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 88 RKSELANLEAIDCGKPLDEAAWDMDDVAGcfeyYADLAEGLdAKQKTPLSLPMDTFKGYILK--EPIGVVGMITPWNYPL 165
Cdd:PLN02315 94 KLDYLGRLVSLEMGKILAEGIGEVQEIID----MCDFAVGL-SRQLNGSIIPSERPNHMMMEvwNPLGIVGVITAFNFPC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 166 LMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREV----GLPPGVLNILTGlGTEAGAPLASHPHVDKIVFTGSTT 241
Cdd:PLN02315 169 AVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 242 TGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNI 321
Cdd:PLN02315 248 VGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 322 KISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEhlKKGYFVEPAIVSnVTTSMEIWREEVFGPALCV 401
Cdd:PLN02315 328 KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE--SEGNFVQPTIVE-ISPDADVVKEELFGPVLYV 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 402 KTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRV--SKAFQAGIVWVNC-SQPCFCQAPWGGTKRSGFGRELGEWGLEN 478
Cdd:PLN02315 405 MKFKTLEEAIEINNSVPQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQ 484
|
..
gi 1789584901 479 YL 480
Cdd:PLN02315 485 YM 486
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
3-466 |
4.33e-49 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 176.62 E-value: 4.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 3 ITVPrrqLFIGGQ--WTEpvlrKTLPVVNPAT-EDIIGYIPAATSEDVELAVEAARKAftrnnGKDWARATGAVRAK-YL 78
Cdd:cd07123 31 VEIP---LVIGGKevRTG----NTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA-----RKEWARMPFEDRAAiFL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 79 RAiaAKVIERK--SELANLEAIDCGKPLDEAAWDmddvAGC-----FEYYADLAEGLDAKQktPLSLPMDTfKGYILKEP 151
Cdd:cd07123 99 KA--ADLLSGKyrYELNAATMLGQGKNVWQAEID----AACelidfLRFNVKYAEELYAQQ--PLSSPAGV-WNRLEYRP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 152 I-GVVGMITPWNYPLLMAVWKVAPSLAaGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPH 230
Cdd:cd07123 170 LeGFVYAVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 231 VDKIVFTGSTTTGSSIMTSAA----------KLVKpvslELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRL 300
Cdd:cd07123 249 LAGLHFTGSTPTFKSLWKQIGenldryrtypRIVG----ETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 301 LVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNE-GATVLCGGVRPEhlKKGYFVEPAI 379
Cdd:cd07123 325 YVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDD--SVGYFVEPTV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 380 VsnVTT--SMEIWREEVFGPALCVKTFSTED--EAIQLAND-SQYGLAGAVLSND---LERCDRVSKaFQAGIVWVN--C 449
Cdd:cd07123 403 I--ETTdpKHKLMTEEIFGPVLTVYVYPDSDfeETLELVDTtSPYALTGAIFAQDrkaIREATDALR-NAAGNFYINdkP 479
|
490
....*....|....*..
gi 1789584901 450 SQPCFCQAPWGGTKRSG 466
Cdd:cd07123 480 TGAVVGQQPFGGARASG 496
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
26-472 |
1.70e-48 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 174.33 E-value: 1.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 26 PVVNPAT-EDIIGYIPAATSEDVELAVEAARKAFTrnngkDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPL 104
Cdd:TIGR01238 54 PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFP-----TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 105 DEAAWDMDDVAGCFEYYADLAEGldakqktplSLPMDTfkgyilKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAIL 184
Cdd:TIGR01238 129 HNAIAEVREAVDFCRYYAKQVRD---------VLGEFS------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 185 KPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSI-MTSAAKLVKPVSL--EL 261
Cdd:TIGR01238 194 KPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInQTLAQREDAPVPLiaET 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 262 GGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQ 341
Cdd:TIGR01238 274 GGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 342 YERVLKFVSNARNEGATV----LCGGVRPEHlkkGYFVEPAIVSnvTTSMEIWREEVFGPALCVKTFSTE--DEAIQLAN 415
Cdd:TIGR01238 354 KQNLLAHIEHMSQTQKKIaqltLDDSRACQH---GTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKARelDQIVDQIN 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1789584901 416 DSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQ--PCFCQAPWGGTKRSGFGRELG 472
Cdd:TIGR01238 429 QTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQvgAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
137-487 |
1.90e-41 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 154.88 E-value: 1.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 137 SLPMDTF--KGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPGVLNIL 214
Cdd:PLN02203 92 KLPLVAFpaTAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKY-LDSKAVKVI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 215 TGlGTEAGAPLASHPHvDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIvFDDVDIDKAVEWT---MFGCFWT-- 289
Cdd:PLN02203 171 EG-GPAVGEQLLQHKW-DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCI-VDSLSSSRDTKVAvnrIVGGKWGsc 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 290 NGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCrLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHL 369
Cdd:PLN02203 248 AGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKKL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 370 kkgyFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSND-------LERCDRVSKAFQA 442
Cdd:PLN02203 327 ----FIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNeklkrriLSETSSGSVTFND 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1789584901 443 GIVWVNCSqpcfcQAPWGGTKRSGFGRELGEWGLENYLSVKQVTQ 487
Cdd:PLN02203 403 AIIQYACD-----SLPFGGVGESGFGRYHGKYSFDTFSHEKAVLR 442
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
47-472 |
2.13e-41 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 153.93 E-value: 2.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 47 VELAVEAARKAftrnnGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDeAAWDMDDVAGCFEYYADLAE 126
Cdd:cd07084 1 PERALLAADIS-----TKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWM-FAENICGDQVQLRARAFVIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 127 GLDAKQKTPLSLPMD-TFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVG 205
Cdd:cd07084 75 SYRIPHEPGNHLGQGlKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 206 -LPPGVLNILTGLGtEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLvkPVSLELGGKSPIIVFDDVDIDKAVEW--- 281
Cdd:cd07084 155 lLPPEDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAVDYVAWqcv 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 282 -TMFGCfwtNGQICSATSRLLVHERIADE-FLDKLVKWTKNIKISDpfeegcrlgPVVSKGQYERVLKFVSNARNEGATV 359
Cdd:cd07084 232 qDMTAC---SGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLED---------LLLGPVQTFTTLAMIAHMENLLGSV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 360 LCGGVRPEHLKKGYFVEPAIVSN--VTTSMEIWR------EEVFGPALCVKTFSTEDEA--IQLANDSQYGLAGAVLSND 429
Cdd:cd07084 300 LLFSGKELKNHSIPSIYGACVASalFVPIDEILKtyelvtEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSND 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1789584901 430 LERCDRVSKAFQ-AGIVWVNCSQPC---FCQAPWGGTKRSGFGRELG 472
Cdd:cd07084 380 PIFLQELIGNLWvAGRTYAILRGRTgvaPNQNHGGGPAADPRGAGIG 426
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
130-485 |
2.76e-37 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 143.26 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 130 AKQKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPG 209
Cdd:PLN02174 91 APEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQY-LDSS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 210 VLNILTGLGTEAGAPLASHphVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTM---FGC 286
Cdd:PLN02174 170 AVRVVEGAVTETTALLEQK--WDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIagkWGC 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 287 fwTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGcRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRP 366
Cdd:PLN02174 248 --NNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEKEVSDKIVYGGEKDR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 367 EHLKkgyfVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVW 446
Cdd:PLN02174 325 ENLK----IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIV 400
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1789584901 447 VN--CSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQV 485
Cdd:PLN02174 401 VNdiAVHLALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
26-448 |
2.09e-35 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 141.26 E-value: 2.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 26 PVVNPA-TEDIIGYIPAATSEDVELAVEAARkaftrNNGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPL 104
Cdd:PRK11809 662 PVINPAdPRDIVGYVREATPAEVEQALESAV-----NAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTF 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 105 DEAAWDMDDVAGCFEYYADLAEGldakqktplSLPMDTFKgyilkePIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAIL 184
Cdd:PRK11809 737 SNAIAEVREAVDFLRYYAGQVRD---------DFDNDTHR------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 185 KPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLV----KPVSL- 259
Cdd:PRK11809 802 KPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgRPIPLi 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 260 -ELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVS 338
Cdd:PRK11809 882 aETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVID 961
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 339 KGQYERVLKFVSNARNEGATVLcGGVRPE--HLKKGYFVEPAIVSnvTTSMEIWREEVFGPALCVKTFSTE--DEAIQLA 414
Cdd:PRK11809 962 AEAKANIERHIQAMRAKGRPVF-QAARENseDWQSGTFVPPTLIE--LDSFDELKREVFGPVLHVVRYNRNqlDELIEQI 1038
|
410 420 430
....*....|....*....|....*....|....
gi 1789584901 415 NDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVN 448
Cdd:PRK11809 1039 NASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1072
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
9-429 |
5.04e-34 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 134.32 E-value: 5.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 9 QLFIGGQWTEPVLRKTlPVVNPATEDIIGyipAATSEDVELAveAARkAFTRNNGKDWARA-TGAVRAKYLRAIAAKVIE 87
Cdd:cd07128 2 QSYVAGQWHAGTGDGR-TLHDAVTGEVVA---RVSSEGLDFA--AAV-AYAREKGGPALRAlTFHERAAMLKALAKYLME 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 88 RKSELANLeAIDCGKPLDEAAWDMDDVAGCFEYYADLA--EGLDAK---QKTPLSLPMD-TFKG-YILKEPIGVVGMITP 160
Cdd:cd07128 75 RKEDLYAL-SAATGATRRDSWIDIDGGIGTLFAYASLGrrELPNAHflvEGDVEPLSKDgTFVGqHILTPRRGVAVHINA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 161 WNYPllmaVW----KVAPSLAAGCTAILKPselASLTCL---ELADICREVG-LPPGVLNILTGlgteAGAPLASH-PHV 231
Cdd:cd07128 154 FNFP----VWgmleKFAPALLAGVPVIVKP---ATATAYlteAVVKDIVESGlLPEGALQLICG----SVGDLLDHlGEQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 232 DKIVFTGSTTTGSSIMTSAAKLVK--PVSLE--------LGgksPIIVFDDVDIDK-----AVEWTMfgcfwTNGQICSA 296
Cdd:cd07128 223 DVVAFTGSAATAAKLRAHPNIVARsiRFNAEadslnaaiLG---PDATPGTPEFDLfvkevAREMTV-----KAGQKCTA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 297 TSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARnEGATVLCGG-----VRPEHLKK 371
Cdd:cd07128 295 IRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLL-AEAEVVFGGpdrfeVVGADAEK 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1789584901 372 GYFVEPAIV-----SNVTTSMEIwreEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSND 429
Cdd:cd07128 374 GAFFPPTLLlcddpDAATAVHDV---EAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
11-429 |
9.61e-27 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 113.26 E-value: 9.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 11 FIGGQWTEPVLRKTlPVVNPATEDIIGyipAATSEDVELAveaARKAFTRNNGKDWARA-TGAVRAKYLRAIAAKVIERK 89
Cdd:PRK11903 8 YVAGRWQAGSGAGT-PLFDPVTGEELV---RVSATGLDLA---AAFAFAREQGGAALRAlTYAQRAALLAAIVKVLQANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 90 SELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGL-DA---KQKTPLSLPMD-TFKG-YILKEPIGVVGMITPWNY 163
Cdd:PRK11903 81 DAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALgDArllRDGEAVQLGKDpAFQGqHVLVPTRGVALFINAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 164 PLlMAVW-KVAPSLAAGCTAILKP-SELASLTCLELADICREVGLPPGVLNILTGlgteAGAPLASHPH-VDKIVFTGST 240
Cdd:PRK11903 161 PA-WGLWeKAAPALLAGVPVIVKPaTATAWLTQRMVKDVVAAGILPAGALSVVCG----SSAGLLDHLQpFDVVSFTGSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 241 TTGSSIMTSAAKLVKPVSLELGGKS--PIIVFDDVDIDKAV----------EWTMfgcfwTNGQICSATSRLLVHERIAD 308
Cdd:PRK11903 236 ETAAVLRSHPAVVQRSVRVNVEADSlnSALLGPDAAPGSEAfdlfvkevvrEMTV-----KSGQKCTAIRRIFVPEALYD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 309 EFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARnEGATVLCGGVRPEHLK----KGYFVEPAI--VSN 382
Cdd:PRK11903 311 AVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALR-AQAEVLFDGGGFALVDadpaVAACVGPTLlgASD 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1789584901 383 VTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSND 429
Cdd:PRK11903 390 PDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
47-415 |
1.06e-24 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 106.47 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 47 VELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLA- 125
Cdd:cd07129 1 VDAAAAAAAAAF-----ESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 126 EG------LDAKQKTPLSLP-MDTFKGYIlkePIGVVGMITPWNYPLLMAVW--KVAPSLAAGCTAILK--PSELAslTC 194
Cdd:cd07129 76 EGswldarIDPADPDRQPLPrPDLRRMLV---PLGPVAVFGASNFPLAFSVAggDTASALAAGCPVVVKahPAHPG--TS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 195 LELADICREV----GLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLV--KPVSLELGGKSPII 268
Cdd:cd07129 151 ELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPepIPFYAELGSVNPVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 269 VFDDVDIDKAVEWT-------MFGCfwtnGQICSATSRLLVherIADEFLDKLVKWTKNiKISDpFEEGCRLGPVVSKGQ 341
Cdd:cd07129 231 ILPGALAERGEAIAqgfvgslTLGA----GQFCTNPGLVLV---PAGPAGDAFIAALAE-ALAA-APAQTMLTPGIAEAY 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1789584901 342 YERVLKFVSNArneGATVLCGGVRPEHlkkGYFVEPAIVSnVTTSM----EIWREEVFGPALCVKTFSTEDEAIQLAN 415
Cdd:cd07129 302 RQGVEALAAAP---GVRVLAGGAAAEG---GNQAAPTLFK-VDAAAfladPALQEEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
150-317 |
9.18e-16 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 79.46 E-value: 9.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 150 EPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICRE----VGLPPGVLNILTGLGTEAGAPL 225
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREaavaAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 226 ASHPHVDKIVFTGstttGSSIMTSAAKLVKPVsleLG---GKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLV 302
Cdd:cd07122 174 MKHPDVDLILATG----GPGMVKAAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIV 246
|
170
....*....|....*
gi 1789584901 303 HERIADEFLDKLVKW 317
Cdd:cd07122 247 DDEIYDEVRAELKRR 261
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
50-314 |
5.30e-15 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 76.92 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 50 AVEAARKAftrnnGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYyadlaeGLD 129
Cdd:cd07081 4 AVAAAKVA-----QQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYIY------NVY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 130 AKQKTPLSLPMD-TFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREV---- 204
Cdd:cd07081 73 KDEKTCGVLTGDeNGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 205 GLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGstttGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMF 284
Cdd:cd07081 153 GAPENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVK 228
|
250 260 270
....*....|....*....|....*....|
gi 1789584901 285 GCFWTNGQICSATSRLLVHERIADEFLDKL 314
Cdd:cd07081 229 SKTFDNGVICASEQSVIVVDSVYDEVMRLF 258
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
60-363 |
3.43e-14 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 74.18 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 60 RNNGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFE-YYADLAEGL----DAKQKT 134
Cdd:cd07077 4 KNAQRTLAVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSEsKLYKNIDTErgitASVGHI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 135 PLSLPMDTFKGYILKEPIGVVGMITPWNYPLLmAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVgLPPGVLNIL 214
Cdd:cd07077 84 QDVLLPDNGETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAA-DAAHGPKIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 215 TGLGTEAGAPLA----SHPHVDKIVFTGSTTTGSSIMTSAAKlvKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWtN 290
Cdd:cd07077 162 VLYVPHPSDELAeellSHPKIDLIVATGGRDAVDAAVKHSPH--IPVIGFGAGNSPVVVDETADEERASGSVHDSKFF-D 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 291 GQICSATSRLLVHERIAD----EFLDKL----VKWTKNIKI-------SDPFEEGCRLGPVVSkgQYeRVLKFVSNARNE 355
Cdd:cd07077 239 QNACASEQNLYVVDDVLDplyeEFKLKLvvegLKVPQETKPlskettpSFDDEALESMTPLEC--QF-RVLDVISAVENA 315
|
....*...
gi 1789584901 356 GATVLCGG 363
Cdd:cd07077 316 WMIIESGG 323
|
|
| ALDH_F18-19_ProA-GPR |
cd07079 |
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; ... |
48-472 |
9.79e-13 |
|
Gamma-glutamyl phosphate reductase (GPR), aldehyde dehydrogenase families 18 and 19; Gamma-glutamyl phosphate reductase (GPR), a L-proline biosynthetic pathway (PBP) enzyme that catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The glutamate route of the PBP involves two enzymatic steps catalyzed by gamma-glutamyl kinase (GK, EC 2.7.2.11) and GPR (EC 1.2.1.41). These enzymes are fused into the bifunctional enzyme, ProA or delta(1)-pyrroline-5-carboxylate synthetase (P5CS) in plants and animals, whereas they are separate enzymes in bacteria and yeast. In humans, the P5CS (ALDH18A1), an inner mitochondrial membrane enzyme, is essential to the de novo synthesis of the amino acids proline and arginine. Tomato (Lycopersicon esculentum) has both the prokaryotic-like polycistronic operons encoding GK and GPR (PRO1, ALDH19) and the full-length, bifunctional P5CS (PRO2, ALDH18B1).
Pssm-ID: 143398 Cd Length: 406 Bit Score: 69.77 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 48 ELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSEL--AN---LE-AIDCGKP--------LDEAAWDmdd 113
Cdd:cd07079 1 EELAKRAKAAS-----RALATLSTEQKNAALLAIADALEANRDEIleANakdLAaAREAGLSealldrllLTPERIE--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 114 vagcfeyyaDLAEGLD--AKQKTPLSLPMDTFK---GYILKE---PIGVVGMItpwnY---PllmavwKVAP-----SLA 177
Cdd:cd07079 73 ---------AMAEGLRqvAALPDPVGEVLRGWTlpnGLQIEKvrvPLGVIGII----YesrP------NVTVdaaalCLK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 178 AGCTAILKPSELASLTCLELADICREV----GLPPGVLNILTGLGTEA-GAPLASHPHVDKIVFTGStttgssimtsaAK 252
Cdd:cd07079 134 SGNAVILRGGSEALHSNRALVEIIQEAleeaGLPEDAVQLIPDTDREAvQELLKLDDYIDLIIPRGG-----------AG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 253 LVKPVSLElgGKSPII----------VFDDVDIDKAVEWTMfgcfwtNGQ-----ICSATSRLLVHERIADEFLDKLVK- 316
Cdd:cd07079 203 LIRFVVEN--ATIPVIkhgdgnchvyVDESADLEMAVRIVV------NAKtqrpsVCNALETLLVHRDIAEEFLPKLAEa 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 317 -WTKNIKIsdpfeEGCrlgpvvskgqyERVLKFVSNArnegatvlcggvrpehlkkgyfvEPAIVSNvttsmeiWREEVF 395
Cdd:cd07079 275 lREAGVEL-----RGD-----------EETLAILPGA-----------------------KPATEED-------WGTEYL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 396 GPALCVKTFSTEDEAIQLANdsQYGlAG---AVLSNDLERCDRVSKAFQAGIVWVNCSqPCFCQapwGGtkRSGFGRELG 472
Cdd:cd07079 309 DLILAVKVVDSLDEAIAHIN--RYG-SGhteAIVTENYETAERFLREVDSAAVYVNAS-TRFTD---GG--EFGLGAEIG 379
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
45-316 |
1.88e-12 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 69.19 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 45 EDVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGkpldeaawdMDDVAgcfeyyADL 124
Cdd:cd07121 4 ATVDDAVAAAKAAQ-----KQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG---------MGRVE------DKI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 125 AEGLDAKQKTPLSLPMDTF-----KGYILKE--PIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLE- 196
Cdd:cd07121 64 AKNHLAAEKTPGTEDLTTTawsgdNGLTLVEyaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 197 ---LADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVkpvslelG---GKSPIIVF 270
Cdd:cd07121 144 velINKAIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTGGPAVVKAALSSGKKAI-------GagaGNPPVVVD 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1789584901 271 DDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVK 316
Cdd:cd07121 217 ETADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQR 262
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
151-436 |
5.36e-12 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 67.91 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 151 PIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPL-ASHP 229
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILlEANP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 230 HVdkIVFTGSTTTGSSImtsAAKLVKPVSLELGGKSPIIVFDDV-DIDkAVEWT----MFGCfwtNGQICSATSRLLVHE 304
Cdd:cd07126 222 RM--TLFTGSSKVAERL---ALELHGKVKLEDAGFDWKILGPDVsDVD-YVAWQcdqdAYAC---SGQKCSAQSILFAHE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 305 RIADE-FLDKLVKWTKNIKISDpfeegCRLGPVVSKGQyERVLKFVSN-ARNEGATVLCGGvRP--EHLKKGYF--VEPA 378
Cdd:cd07126 293 NWVQAgILDKLKALAEQRKLED-----LTIGPVLTWTT-ERILDHVDKlLAIPGAKVLFGG-KPltNHSIPSIYgaYEPT 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1789584901 379 IV------SNVTTSMEIWREEVFGPALCVKTFSTEDE--AIQLANDSQYGLAGAVLSNDLERCDRV 436
Cdd:cd07126 366 AVfvpleeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEV 431
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
46-450 |
9.29e-12 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 67.12 E-value: 9.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 46 DVELAVEAARKAFtrnngKDWARATGAVRAKYLRAIAAKVIERKSELANL------------------EAIDCG-KPLDE 106
Cdd:cd07127 85 DPDALLAAARAAM-----PGWRDAGARARAGVCLEILQRLNARSFEMAHAvmhttgqafmmafqaggpHAQDRGlEAVAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 107 AAWDMDDVAGCFEYyadlaeglDAKQKTPLSLPMD-TFkgYILKEPIG-VVGMIT--PWN-YPLLMAvwkvapSLAAGCT 181
Cdd:cd07127 160 AWREMSRIPPTAEW--------EKPQGKHDPLAMEkTF--TVVPRGVAlVIGCSTfpTWNgYPGLFA------SLATGNP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 182 AILKPSELASLTCLELADICREV----GLPPgvlNILTGLGTEAGAP----LASHPHVDKIVFTGSTTTGSSIMTSAAKl 253
Cdd:cd07127 224 VIVKPHPAAILPLAITVQVAREVlaeaGFDP---NLVTLAADTPEEPiaqtLATRPEVRIIDFTGSNAFGDWLEANARQ- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 254 vKPVSLELGGKSPIIVfDDVDIDKAVEWTM-FGCFWTNGQICSATSRLLV---------HERIADEFLDKLVKWTKNIkI 323
Cdd:cd07127 300 -AQVYTEKAGVNTVVV-DSTDDLKAMLRNLaFSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAADLAAAIDGL-L 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 324 SDPFEEGCRLGPVVSKGQYERVLKfvsnARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSME-IWREEVFGP-ALCV 401
Cdd:cd07127 377 ADPARAAALLGAIQSPDTLARIAE----ARQLGEVLLASEAVAHPEFPDARVRTPLLLKLDASDEaAYAEERFGPiAFVV 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1789584901 402 KTFSTeDEAIQLANDS--QYG-LAGAVLSNDLERCDRVSKAFQA----------GIVWVNCS 450
Cdd:cd07127 453 ATDST-DHSIELARESvrEHGaMTVGVYSTDPEVVERVQEAALDagvalsinltGGVFVNQS 513
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
45-316 |
1.30e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.22 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 45 EDVELAVEAARKAFTRnngkdWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGkpldeaawdMDDVAgcfeyyADL 124
Cdd:PRK15398 36 ASVDDAVAAAKVAQQR-----YQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG---------MGRVE------DKI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 125 AEGLDAKQKTP--LSLPMDTF---KGYILKE--PIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLEL 197
Cdd:PRK15398 96 AKNVAAAEKTPgvEDLTTEALtgdNGLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 198 A----DICREVGlppGVLNILTGLGT---EAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVkpvslelG---GKSPI 267
Cdd:PRK15398 176 IellnEAIVAAG---GPENLVVTVAEptiETAQRLMKHPGIALLVVTGGPAVVKAAMKSGKKAI-------GagaGNPPV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1789584901 268 IVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVK 316
Cdd:PRK15398 246 VVDETADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEK 294
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
141-354 |
9.09e-07 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 51.72 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 141 DTFKGYI-LKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREV----GLPPGVLNILT 215
Cdd:PRK13805 97 DDEFGIIeIAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAavaaGAPKDIIQWIE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 216 GLGTEAGAPLASHPHVDKIVFTGstttGSSIMTSAAKLVKPvSLELG-GKSPIIVFDDVDIDKAVEWTMFGCFWTNGQIC 294
Cdd:PRK13805 177 EPSVELTNALMNHPGIALILATG----GPGMVKAAYSSGKP-ALGVGaGNVPAYIDKTADIKRAVNDILLSKTFDNGMIC 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1789584901 295 SATSRLLVHERIADEFLDKLVKWtknikisdpfeeGCRLgpvVSKGQYERVLKFVSNARN 354
Cdd:PRK13805 252 ASEQAVIVDDEIYDEVKEEFASH------------GAYF---LNKKELKKLEKFIFGKEN 296
|
|
| |
