|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
13-487 |
0e+00 |
|
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: 875.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 13 YGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:cd07117 81 AMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVP 252
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 253 ATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQ 332
Cdd:cd07117 241 ATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 333 TGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIA 412
Cdd:cd07117 321 VNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613258995 413 NDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYIDT 487
Cdd:cd07117 401 NDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
13-487 |
0e+00 |
|
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: 848.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 13 YGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:cd07559 81 AVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVP 252
Cdd:cd07559 161 LAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAENLIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 253 ATLELGGKSANIILDDA-----NLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEAT 327
Cdd:cd07559 241 VTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPET 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 328 QMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQE 407
Cdd:cd07559 321 MMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKDEEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 408 AIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYIDT 487
Cdd:cd07559 401 AIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNILVSY 480
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
13-487 |
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: 636.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 13 YGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:COG1012 6 YPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAiDIPFAARHFHYFASVIETEEGTVNDID-KDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAP 171
Cdd:COG1012 86 AALLTLETGKPLAEARG-EVDRAADFLRYYAGEARRLYGETIPSDaPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 172 AIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHL 250
Cdd:COG1012 165 ALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAENL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMG 330
Cdd:COG1012 245 KRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 331 SQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTEnglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAID 410
Cdd:COG1012 325 PLISEAQLERVLAYIEDAVAEGAELLTGGRRPDG---EGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613258995 411 IANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEG-APFGGYKKSGIGRETYKGALSNYQQVKNIYIDT 487
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
21-483 |
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: 626.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 21 FVKGSSdETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNN 100
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 101 GKPIRETTAiDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIV 180
Cdd:pfam00171 80 GKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 181 IQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGG 259
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAgLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 260 KSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLD 339
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 340 KIQSYIDAAKESDAQILAGGHRltenGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGL 419
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEA----GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGL 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613258995 420 AGGVFSQNITRALNIAKAVRTGRIWINTYNQV-PEGAPFGGYKKSGIGRETYKGALSNYQQVKNI 483
Cdd:pfam00171 395 AAGVFTSDLERALRVARRLEAGMVWINDYTTGdADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
32-485 |
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: 577.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFES--WSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTA 109
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGgaWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 110 iDIPFAARHFHYFASVIETEEGTVNDIDK-DTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTP 188
Cdd:cd07114 81 -QVRYLAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 189 LSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILD 267
Cdd:cd07114 160 ASTLELAKLAEEAgFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 268 DANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDA 347
Cdd:cd07114 240 DADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 348 AKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQN 427
Cdd:cd07114 320 AREEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRD 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 613258995 428 ITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07114 400 LARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
12-485 |
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: 574.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 12 NYGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSL--TSKSERAQMLRDIGDKLMAQK 89
Cdd:cd07091 3 PTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWrkMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 90 DKIAMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKI 169
Cdd:cd07091 83 DELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 170 APAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK 248
Cdd:cd07091 163 APALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 249 -HLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEAT 327
Cdd:cd07091 243 sNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 328 QMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLtengLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQE 407
Cdd:cd07091 323 FQGPQVSKAQFDKILSYIESGKKEGATLLTGGERH----GSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDE 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613258995 408 AIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07091 399 VIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVTI 476
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
53-485 |
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: 564.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 53 DHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETtAIDIPFAARHFHYFASVIETEEGT 132
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEA-LGEVARAADTFRYYAGLARRLHGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 133 V-NDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNIL 210
Cdd:cd07078 80 ViPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLNVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 211 TGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVC 290
Cdd:cd07078 160 TGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 291 SAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLtenGLDKG 370
Cdd:cd07078 240 TAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRL---EGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 371 FFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQ 450
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 613258995 451 VPE-GAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07078 397 GAEpSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
16-495 |
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: 558.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFES--WSLTSKSERAQMLRDIGDKLMAQKDKIA 93
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 94 MIETLNNGKPIRETTaIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAI 173
Cdd:cd07119 81 RLETLNTGKTLRESE-IDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 174 AAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVP 252
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAgLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 253 ATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQ 332
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 333 TGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIA 412
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 413 NDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYIDTSNALK 492
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSPQPI 479
|
...
gi 613258995 493 GLY 495
Cdd:cd07119 480 GWF 482
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
28-485 |
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: 529.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 28 ETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFES--WSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIR 105
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 106 ETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSS 185
Cdd:cd07112 82 DALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 186 STPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK-HLVPATLELGGKSAN 263
Cdd:cd07112 162 QSPLTALRLAELALEAgLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 264 IILDDA-NLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQ 342
Cdd:cd07112 242 IVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 343 SYIDAAKESDAQILAGGHRLTENGldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGG 422
Cdd:cd07112 322 GYIESGKAEGARLVAGGKRVLTET--GGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613258995 423 VFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTTWI 462
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
34-485 |
0e+00 |
|
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: 526.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 34 NPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAIDIP 113
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRLDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 114 FAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLE 193
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 194 VAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLD 272
Cdd:cd07115 163 IAELMAEAgFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 273 LAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESD 352
Cdd:cd07115 243 AAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 353 AQILAGGHRLTEngldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRAL 432
Cdd:cd07115 323 ARLLTGGKRPGA----RGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAH 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 613258995 433 NIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07115 399 RVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWV 451
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
32-485 |
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: 526.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAID 111
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDAN 270
Cdd:cd07093 161 WLLAELANEAgLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 271 LDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKE 350
Cdd:cd07093 241 LDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 351 SDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITR 430
Cdd:cd07093 321 EGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGR 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 613258995 431 ALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07093 401 AHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
13-485 |
8.20e-180 |
|
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: 512.77 E-value: 8.20e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 13 YGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:cd07116 81 AVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVP 252
Cdd:cd07116 161 LAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASENIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 253 ATLELGGKSANIIL------DDANLDLAVEGIQLgILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEA 326
Cdd:cd07116 241 VTLELGGKSPNIFFadvmdaDDAFFDKALEGFVM-FALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 327 TQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAvpdNHHKLA--QEEIFGPVLTVIKVKD 404
Cdd:cd07116 320 TMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFK---GGNKMRifQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 405 DQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIY 484
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLL 476
|
.
gi 613258995 485 I 485
Cdd:cd07116 477 V 477
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
15-485 |
7.00e-175 |
|
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: 499.79 E-value: 7.00e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFES--WSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIET---EE-------GTVndidkdtmsIVRHEPIGVVGAVVAWNFPM 162
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDfpfEErrpgsggGHV---------LVRREPVGVVAAIVPWNAPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 163 LLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGYQ 241
Cdd:cd07139 152 FLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAgLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 242 VAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGN 321
Cdd:cd07139 231 IAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 322 PQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIK 401
Cdd:cd07139 311 PLDPATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPA--GLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 402 VKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPeGAPFGGYKKSGIGRETYKGALSNYQQVK 481
Cdd:cd07139 389 YDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDF-GAPFGGFKQSGIGREGGPEGLDAYLETK 467
|
....
gi 613258995 482 NIYI 485
Cdd:cd07139 468 SIYL 471
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
32-483 |
9.69e-173 |
|
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: 493.79 E-value: 9.69e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETtAID 111
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEA-AWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASVIE----TEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSST 187
Cdd:cd07110 80 VDDVAGCFEYYADLAEqldaKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 188 PLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIIL 266
Cdd:cd07110 160 SLTELELAEIAAEAgLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 267 DDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYID 346
Cdd:cd07110 240 DDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 347 AAKESDAQILAGGHRLteNGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQ 426
Cdd:cd07110 320 RGKEEGARLLCGGRRP--AHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 613258995 427 NITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNI 483
Cdd:cd07110 398 DAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
12-486 |
3.61e-172 |
|
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: 493.58 E-value: 3.61e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 12 NYGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFE-SWSLT-SKSERAQMLRDIGDKLMAQK 89
Cdd:cd07143 6 PTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFEtDWGLKvSGSKRGRCLSKLADLMERNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 90 DKIAMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKI 169
Cdd:cd07143 86 DYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 170 APAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK 248
Cdd:cd07143 166 APALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 249 -HLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEAT 327
Cdd:cd07143 246 sNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 328 QMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRlteNGlDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQE 407
Cdd:cd07143 326 FQGPQVSQIQYERIMSYIESGKAEGATVETGGKR---HG-NEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613258995 408 AIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYID 486
Cdd:cd07143 402 AIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
13-485 |
6.39e-171 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 490.55 E-value: 6.39e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 13 YGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:PRK13252 7 QSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:PRK13252 87 AALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGsESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLV 251
Cdd:PRK13252 167 LAAGNAMIFKPSEVTPLTALKLAEIYTEAgLPDGVFNVVQGDG-RVGAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 252 PATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGS 331
Cdd:PRK13252 246 EVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 332 QTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDI 411
Cdd:PRK13252 326 LVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIAR 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613258995 412 ANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:PRK13252 406 ANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
15-485 |
1.80e-170 |
|
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: 489.17 E-value: 1.80e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFE---SWSLTSKSERAQMLRDIGDKLMAQKDK 91
Cdd:cd07141 9 IFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 92 IAMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAP 171
Cdd:cd07141 89 LASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAAWKLAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 172 AIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK-H 249
Cdd:cd07141 169 ALACGNTVVLKPAEQTPLTALYLASLIKEAgFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGKsN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 250 LVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQM 329
Cdd:cd07141 249 LKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQ 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 330 GSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAI 409
Cdd:cd07141 329 GPQIDEEQFKKILELIESGKKEGAKLECGGKRHG----DKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 410 DIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07141 405 ERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
15-484 |
2.85e-170 |
|
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: 488.17 E-value: 2.85e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAM 94
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 95 IETLNNGKPIRETTAIDIPFAARHFHYFASVIET--EEGTVNDidkdtmSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:cd07138 81 AITLEMGAPITLARAAQVGLGIGHLRAAADALKDfeFEERRGN------SLVVREPIGVCGLITPWNWPLNQIVLKVAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLV 251
Cdd:cd07138 155 LAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 252 PATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGS 331
Cdd:cd07138 235 RVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 332 QTGKDQLDKIQSYIDAAKESDAQILAGGHRLTEnGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDI 411
Cdd:cd07138 315 LASAAQFDRVQGYIQKGIEEGARLVAGGPGRPE-GLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAI 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613258995 412 ANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPeGAPFGGYKKSGIGRETYKGALSNYQQVKNIY 484
Cdd:cd07138 394 ANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFNP-GAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
32-485 |
2.94e-170 |
|
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: 487.51 E-value: 2.94e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSL-TSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAi 110
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLrLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 111 DIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLS 190
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 191 LLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDA 269
Cdd:cd07109 160 ALRLAELAEEAgLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 270 NLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEAtQMGSQTGKDQLDKIQSYIDAAK 349
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDP-DLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 350 ESDAQILAGGHRLtENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNIT 429
Cdd:cd07109 319 ARGARIVAGGRIA-EGAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613258995 430 RALNIAKAVRTGRIWINTYnqvpeGA------PFGGYKKSGIGREtyKG--ALSNYQQVKNIYI 485
Cdd:cd07109 398 RALRVARRLRAGQVFVNNY-----GAgggielPFGGVKKSGHGRE--KGleALYNYTQTKTVAV 454
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
32-488 |
5.63e-169 |
|
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: 484.50 E-value: 5.63e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIrETTAID 111
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPI-EEARVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07090 80 IDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LEVAKIFQEV-LPKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDAN 270
Cdd:cd07090 160 LLLAEILTEAgLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 271 LDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKE 350
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 351 SDAQILAGGHRLT-ENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNIT 429
Cdd:cd07090 319 EGAKVLCGGERVVpEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 613258995 430 RALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYIDTS 488
Cdd:cd07090 399 RAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
14-486 |
1.57e-168 |
|
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: 484.22 E-value: 1.57e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 14 GLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFES-WSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESwWSKVTGEERGELLDKLADLVEKNRDLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:cd07144 89 AAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAPA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLV 251
Cdd:cd07144 169 LAAGNTVVIKPAENTPLSLLYFANLVKEAgFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 252 PATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAF-SNIKVGNPQDEATQMG 330
Cdd:cd07144 249 AVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 331 SQTGKDQLDKIQSYIDAAKESDAQILAGGHRLtENGLDKGFFFEPTLIA-VPDNhHKLAQEEIFGPVLTVIKVKDDQEAI 409
Cdd:cd07144 329 PQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKA-PEGLGKGYFIPPTIFTdVPQD-MRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613258995 410 DIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYID 486
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHIN 483
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
32-483 |
5.57e-168 |
|
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: 482.13 E-value: 5.57e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWS-LTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAI 110
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDwSTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 111 DIPFAARHFHYFASVIETEEGTVNDIDKD-----TMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSS 185
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPAlrggpGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 186 STPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANI 264
Cdd:cd07089 161 DTPLSALLLGEIIAETdLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 265 ILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSY 344
Cdd:cd07089 241 VLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEGY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 345 IDAAKESDAQILAGGHRLTenGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVF 424
Cdd:cd07089 321 IARGRDEGARLVTGGGRPA--GLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 613258995 425 SQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNI 483
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
15-484 |
5.18e-165 |
|
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: 475.06 E-value: 5.18e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFE--SWSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:cd07142 86 AALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGPA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK-HL 250
Cdd:cd07142 166 LACGNTIVLKPAEQTPLSALLAAKLAAEAgLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKsNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMG 330
Cdd:cd07142 246 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 331 SQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAID 410
Cdd:cd07142 326 PQVDKEQFEKILSYIEHGKEEGATLITGGDRIG----SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613258995 411 IANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIY 484
Cdd:cd07142 402 RANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
16-481 |
7.66e-164 |
|
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: 471.99 E-value: 7.66e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMI 95
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 96 ETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAA 175
Cdd:TIGR01804 81 ETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 176 GNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPAT 254
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAgLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 255 LELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTG 334
Cdd:TIGR01804 241 MELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 335 KDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIAND 414
Cdd:TIGR01804 321 AAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613258995 415 SEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVK 481
Cdd:TIGR01804 401 TEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
32-485 |
9.59e-164 |
|
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: 471.07 E-value: 9.59e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAID 111
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LEVAKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANL 271
Cdd:cd07108 161 LLLAEILAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 272 DLAVEGIQLGILFN-QGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKE 350
Cdd:cd07108 241 DDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLGLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 351 -SDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNIT 429
Cdd:cd07108 321 tSGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 613258995 430 RALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRE-TYKGALSNYQQVKNIYI 485
Cdd:cd07108 401 RALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREaSLEGMLEHFTQKKTVNI 457
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
32-483 |
1.64e-163 |
|
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: 470.27 E-value: 1.64e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAID 111
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASVIETEEGTV-NDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLS 190
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAaGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 191 LLEVAKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDAN 270
Cdd:cd07092 161 TLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 271 LDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKE 350
Cdd:cd07092 241 LDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 351 sDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITR 430
Cdd:cd07092 321 -HARVLTGGRRAE----GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 613258995 431 ALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNI 483
Cdd:cd07092 396 AMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
7-477 |
1.07e-162 |
|
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: 469.18 E-value: 1.07e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 7 DYIAENYGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLM 86
Cdd:cd07111 16 DAHDRSFGHFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 87 AQKDKIAMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDidkdtmsivrHEPIGVVGAVVAWNFPMLLAA 166
Cdd:cd07111 96 KHQRLFAVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTELAG----------WKPVGVVGQIVPWNFPLLMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 167 WKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSeSGNAIFNHDGVDKLSFTGSTDVGYQVAEA 245
Cdd:cd07111 166 WKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 246 AAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDE 325
Cdd:cd07111 245 TAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 326 ATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDD 405
Cdd:cd07111 325 AIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP----SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613258995 406 QEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNY 477
Cdd:cd07111 401 KEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEY 472
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
15-488 |
1.24e-161 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 466.31 E-value: 1.24e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSdETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAM 94
Cdd:PRK13473 5 LLINGELVAGEG-EKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 95 IETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTV-NDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAI 173
Cdd:PRK13473 84 LESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKAaGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLAPAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 174 AAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPA 253
Cdd:PRK13473 164 AAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADSVKRT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 254 TLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQT 333
Cdd:PRK13473 244 HLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 334 GKDQLDKIQSYIDAAKE-SDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIA 412
Cdd:PRK13473 324 SAAHRDRVAGFVERAKAlGHIRVVTGGEAPD----GKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 413 NDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYIDTS 488
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHVMVKHT 475
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
32-485 |
2.13e-160 |
|
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: 462.00 E-value: 2.13e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAiD 111
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASvIETEEGTVNDiDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07106 80 VGGAVAWLRYTAS-LDLPDEVIED-DDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LEVAKIFQEVLPKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANL 271
Cdd:cd07106 158 LKLGELAQEVLPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 272 DLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKES 351
Cdd:cd07106 237 DAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 352 DAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRA 431
Cdd:cd07106 317 GAKVLAGGEPLD----GPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 613258995 432 LNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
32-483 |
2.08e-158 |
|
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: 457.28 E-value: 2.08e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAiD 111
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFAsvietEEG------TVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSS 185
Cdd:cd07103 80 VDYAASFLEWFA-----EEArriygrTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 186 STPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANI 264
Cdd:cd07103 155 ETPLSALALAELAEEAgLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 265 ILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSY 344
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 345 IDAAKESDAQILAGGHRLTenglDKGFFFEPTLIA-VPDNhHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGV 423
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLG----LGGYFYEPTVLTdVTDD-MLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 424 FSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNI 483
Cdd:cd07103 390 FTRDLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
35-485 |
3.97e-155 |
|
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: 449.10 E-value: 3.97e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 35 PATGETLSHITRAKDKDVDHAVEVAQEAFES--WSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAiDI 112
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 113 PFAARHFHYFASVIETEEG-TVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07118 83 EGAADLWRYAASLARTLHGdSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDAN 270
Cdd:cd07118 163 LMLAELLIEAgLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 271 LDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKE 350
Cdd:cd07118 243 LDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 351 SDAQILAGGHRLTENgldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITR 430
Cdd:cd07118 323 EGATLLLGGERLASA---AGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDT 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 431 ALNIAKAVRTGRIWINTY-NQVPEgAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07118 400 ALTVARRIRAGTVWVNTFlDGSPE-LPFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
16-485 |
1.80e-153 |
|
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: 445.54 E-value: 1.80e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGssDETIEVTNPA-TGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAM 94
Cdd:cd07097 4 YIDGEWVAG--GDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 95 IETLNNGKPIRETTAiDIPFAARHFHYFASVIETEEG-TVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAI 173
Cdd:cd07097 82 LLTREEGKTLPEARG-EVTRAGQIFRYYAGEALRLSGeTLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 174 AAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVP 252
Cdd:cd07097 161 AYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 253 ATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQ 332
Cdd:cd07097 241 VQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 333 TGKDQLDKIQSYIDAAKESDAQILAGGHRLTenGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIA 412
Cdd:cd07097 321 VSERQLEKDLRYIEIARSEGAKLVYGGERLK--RPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613258995 413 NDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN-TYNQVPEGAPFGGYKKSGIG-RETYKGALSNYQQVKNIYI 485
Cdd:cd07097 399 NDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTVYV 473
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
57-485 |
1.55e-152 |
|
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: 438.97 E-value: 1.55e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 57 EVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAiDIPFAARHFHYFASVIETEEG-TVND 135
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALG-EVARAIDTFRYAAGLADKLGGpELPS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 136 IDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKG 214
Cdd:cd06534 80 PDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVVNVVPGGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 215 SESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGS 294
Cdd:cd06534 160 DEVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAAS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 295 RLLVHEKIYDQLVPRLQeafsnikvgnpqdeatqmgsqtgkdqldkiqsyidaakesdaqilagghrltengldkgfffe 374
Cdd:cd06534 240 RLLVHESIYDEFVEKLV--------------------------------------------------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 375 pTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYN-QVPE 453
Cdd:cd06534 257 -TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSiGVGP 335
|
410 420 430
....*....|....*....|....*....|..
gi 613258995 454 GAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd06534 336 EAPFGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
16-485 |
1.94e-152 |
|
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: 442.86 E-value: 1.94e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMI 95
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 96 ETLNNGKPIRETTaIDIPFAARHFHYFASVIETEEGTV--NDIDKDTMSIVRhEPIGVVGAVVAWNFPMLLAAWKIAPAI 173
Cdd:cd07088 81 IVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIipSDRPNENIFIFK-VPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 174 AAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVP 252
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAgLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 253 ATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQ 332
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 333 TGKDQLDKIQSYIDAAKESDAQILAGGHRLTengLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIA 412
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPE---GEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613258995 413 NDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
14-495 |
1.69e-150 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 439.17 E-value: 1.69e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 14 GLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAF-----ESWSLTSKSERAQMLRDIGDKLMAQ 88
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 89 KDKIAMIETLNNGKPIRETtAIDIPFAARHFHYFASVIETEEGTVN---DIDKDTM-SIVRHEPIGVVGAVVAWNFPMLL 164
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEA-AWDMDDVAGCFEYYADLAEALDAKQKapvSLPMETFkGYVLKEPLGVVGLITPWNYPLLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 165 AAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVA 243
Cdd:PLN02467 168 ATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIM 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 244 EAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQ 323
Cdd:PLN02467 248 TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 324 DEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRltENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVK 403
Cdd:PLN02467 328 EEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKR--PEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 404 DDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNI 483
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
490
....*....|..
gi 613258995 484 YIDTSNALKGLY 495
Cdd:PLN02467 486 TKYISDEPWGWY 497
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
15-481 |
1.32e-149 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 438.09 E-value: 1.32e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFES--WSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEgpWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:PLN02466 140 AALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK-HL 250
Cdd:PLN02466 220 LACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKsNL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMG 330
Cdd:PLN02466 300 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 331 SQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAID 410
Cdd:PLN02466 380 PQIDSEQFEKILRYIKSGVESGATLECGGDRFG----SKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIR 455
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613258995 411 IANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVK 481
Cdd:PLN02466 456 RANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
16-488 |
2.45e-148 |
|
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: 432.54 E-value: 2.45e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSSDETIEVTNPATGETLSHITRAKDK-DVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAM 94
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVGTFPLSTAsDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 95 IETLNNGKPIRETTAiDIPFAARHFHYFASVIETEEGTVND---IDKDTMSIVRhePIGVVGAVVAWNFPMLLAAWKIAP 171
Cdd:cd07131 82 LVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPselPNKDAMTRRQ--PIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 172 AIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHL 250
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMG 330
Cdd:cd07131 239 KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 331 SQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAID 410
Cdd:cd07131 319 PLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 411 IANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINtynqVPE-GA----PFGGYKKSGIG-RETYKGALSNYQQVKNIY 484
Cdd:cd07131 399 IANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN----APTiGAevhlPFGGVKKSGNGhREAGTTALDAFTEWKAVY 474
|
....
gi 613258995 485 IDTS 488
Cdd:cd07131 475 VDYS 478
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
15-483 |
4.71e-147 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 430.40 E-value: 4.71e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFE--SWSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:PLN02766 23 LFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:PLN02766 103 AALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK-HL 250
Cdd:PLN02766 183 LAAGCTMVVKPAEQTPLSALFYAHLAKLAgVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAATsNL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 251 VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMG 330
Cdd:PLN02766 263 KQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 331 SQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAID 410
Cdd:PLN02766 343 PQVDKQQFEKILSYIEHGKREGATLLTGGKPCG----DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIK 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613258995 411 IANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNI 483
Cdd:PLN02766 419 KANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
32-485 |
2.01e-143 |
|
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: 419.47 E-value: 2.01e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAiD 111
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07107 80 VMVAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LEVAKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANL 271
Cdd:cd07107 160 LRLAELAREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 272 DLAVEGIQLGILFN-QGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKE 350
Cdd:cd07107 240 EAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAKR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 351 SDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITR 430
Cdd:cd07107 320 EGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQ 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 613258995 431 ALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07107 400 AHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
34-484 |
6.95e-142 |
|
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: 415.20 E-value: 6.95e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 34 NPATGETLSHITRAKDKDVDHAVEVAQEAFE--SWSlTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETtAID 111
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-RFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LEVAKIFQEV--LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDA 269
Cdd:cd07120 161 AAIIRILAEIpsLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 270 NLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAK 349
Cdd:cd07120 241 DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERAI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 350 ESDAQILAGGHRLTEnGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNIT 429
Cdd:cd07120 321 AAGAEVVLRGGPVTE-GLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 613258995 430 RALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIY 484
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
16-488 |
2.37e-138 |
|
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: 407.33 E-value: 2.37e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVkGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMI 95
Cdd:cd07086 2 VIGGEWV-GSGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 96 ETLNNGKPIRET-----TAIDI-PFAA---RHFHyfASVIETEEGtvndiDKDTMSIvRHePIGVVGAVVAWNFPMLLAA 166
Cdd:cd07086 81 VSLEMGKILPEGlgevqEMIDIcDYAVglsRMLY--GLTIPSERP-----GHRLMEQ-WN-PLGVVGVITAFNFPVAVPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 167 WKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVL-----PKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGYQ 241
Cdd:cd07086 152 WNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLeknglPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 242 VAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGN 321
Cdd:cd07086 231 VGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 322 PQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIK 401
Cdd:cd07086 311 PLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRID--GGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 402 VKDDQEAIDIANDSEYGLAGGVFSQNITRALNI--AKAVRTGRIWINTYNQVPE-GAPFGGYKKSGIGRETYKGALSNYQ 478
Cdd:cd07086 389 FDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNIPTSGAEiGGAFGGEKETGGGRESGSDAWKQYM 468
|
490
....*....|
gi 613258995 479 QVKNIYIDTS 488
Cdd:cd07086 469 RRSTCTINYS 478
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
14-485 |
1.15e-136 |
|
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: 402.98 E-value: 1.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 14 GLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFES-WSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:cd07113 1 GHFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFAsvieteeGTVNDIDKDTM-------------SIVRHEPIGVVGAVVAWN 159
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFA-------GWATKINGETLapsipsmqgerytAFTRREPVGVVAGIVPWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 160 FPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGsESGNAIFNHDGVDKLSFTGSTDV 238
Cdd:cd07113 154 FSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKG-AVGAQLISHPDVAKVSFTGSVAT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 239 GYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIK 318
Cdd:cd07113 233 GKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 319 VGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTEngldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLT 398
Cdd:cd07113 313 VGSPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAG----EGYFVQPTLVLARSADSRLMREETFGPVVS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 399 VIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQ 478
Cdd:cd07113 389 FVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYT 468
|
....*..
gi 613258995 479 QVKNIYI 485
Cdd:cd07113 469 ELKSVMI 475
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
30-485 |
2.08e-136 |
|
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: 401.34 E-value: 2.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 30 IEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTa 109
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 110 IDIPFAARHFHYFAS---VIETEEGTVNDID--KDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPS 184
Cdd:cd07145 80 VEVERTIRLFKLAAEeakVLRGETIPVDAYEynERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 185 SSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSAN 263
Cdd:cd07145 160 SNTPLTAIELAKILEEAgLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 264 IILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQS 343
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 344 YIDAAKESDAQILAGGHRltenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGV 423
Cdd:cd07145 320 LVNDAVEKGGKILYGGKR------DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613258995 424 FSQNITRALNIAKAVRTGRIWINTYNQV-PEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
51-468 |
6.64e-136 |
|
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: 399.21 E-value: 6.64e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 51 DVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIamIETLnngkpIRET------TAIDIPFAARHFHYFAS 124
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEI--ADWL-----IRESgstrpkAAFEVGAAIAILREAAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 125 VIETEEGTV--NDIDkDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL-LEVAKIFQEV 201
Cdd:cd07104 74 LPRRPEGEIlpSDVP-GKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 202 -LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQL 280
Cdd:cd07104 153 gLPKGVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 281 GILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGH 360
Cdd:cd07104 233 GAFLHQGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 361 RltengldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRT 440
Cdd:cd07104 313 Y-------EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLET 385
|
410 420 430
....*....|....*....|....*....|
gi 613258995 441 GRIWIN--TYNQVPEgAPFGGYKKSGIGRE 468
Cdd:cd07104 386 GMVHINdqTVNDEPH-VPFGGVKASGGGRF 414
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-485 |
2.69e-132 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 392.34 E-value: 2.69e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFES--WSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:PRK09847 102 ALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQV-AEAAAKHL 250
Cdd:PRK09847 182 LAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLlKDAGDSNM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 251 VPATLELGGKSANIILDDA-NLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQM 329
Cdd:PRK09847 262 KRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 330 GSQTGKDQLDKIQSYIDAAkESDAQILAGGHRLTENGldkgfFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAI 409
Cdd:PRK09847 342 GTLIDCAHADSVHSFIREG-ESKGQLLLDGRNAGLAA-----AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 410 DIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:PRK09847 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWI 491
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-466 |
8.31e-129 |
|
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: 383.88 E-value: 8.31e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 5 VRDYIAENYGLFINGEFVKGssDETIEVTNPA-TGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGD 83
Cdd:cd07124 25 VREELGREYPLVIGGKEVRT--EEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 84 KLMAQKDKIAMIETLNNGKPIRETTAiDIPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVvGAVVA-WNFPM 162
Cdd:cd07124 103 LLRRRRFELAAWMVLEVGKNWAEADA-DVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGV-GAVISpWNFPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 163 LLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQ 241
Cdd:cd07124 181 AILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 242 VAEAAAK------HLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFS 315
Cdd:cd07124 261 IYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTK 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 316 NIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKeSDAQILAGGHRLTENglDKGFFFEPTLIAVPDNHHKLAQEEIFGP 395
Cdd:cd07124 341 ALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGK-SEGRLLLGGEVLELA--AEGYFVQPTIFADVPPDHRLAQEEIFGP 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 396 VLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNitRAlNIAKA---VRTGRIWIN--TYNQVPEGAPFGGYKKSGIG 466
Cdd:cd07124 418 VLAVIKAKDFDEALEIANDTEYGLTGGVFSRS--PE-HLERArreFEVGNLYANrkITGALVGRQPFGGFKMSGTG 490
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
19-485 |
7.94e-128 |
|
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: 379.73 E-value: 7.94e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 19 GEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIamIETL 98
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEI--VEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 99 nngkpIRET------TAIDIPFAARHFHYFASVIETEEGTV--NDIDKDTMSIVRhEPIGVVGAVVAWNFPMLLAAWKIA 170
Cdd:cd07151 79 -----IRESgstrikANIEWGAAMAITREAATFPLRMEGRIlpSDVPGKENRVYR-EPLGVVGVISPWNFPLHLSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 171 PAIAAGNTIVIQPSSSTPLS--LLeVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAA 247
Cdd:cd07151 153 PALALGNAVVLKPASDTPITggLL-LAKIFEEAgLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 248 KHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEAT 327
Cdd:cd07151 232 RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 328 QMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRltengldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQE 407
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 408 AIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN--TYNQVPEgAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07151 385 ALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINdqPVNDEPH-VPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
13-486 |
4.57e-127 |
|
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: 378.76 E-value: 4.57e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 13 YGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFES--WSLTSKSERAQMLRDIGDKLMAQKD 90
Cdd:cd07140 6 HQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 91 KIAMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDK----DTMSIVRHEPIGVVGAVVAWNFPMLLAA 166
Cdd:cd07140 86 ELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQarpnRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 167 WKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEA 245
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 246 AAK-HLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQD 324
Cdd:cd07140 246 CAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 325 EATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTEngldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKD 404
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDR----PGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 405 D--QEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKN 482
Cdd:cd07140 402 GdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKT 481
|
....
gi 613258995 483 IYID 486
Cdd:cd07140 482 VTIE 485
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
52-468 |
5.44e-125 |
|
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: 371.41 E-value: 5.44e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 52 VDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAiDIPFAARHFHYFA-------- 123
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAenaeafla 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 124 -SVIETEEGTvndidkdtmSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV- 201
Cdd:cd07100 80 dEPIETDAGK---------AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 202 LPKGV-VNILTGkgSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQL 280
Cdd:cd07100 151 FPEGVfQNLLID--SDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 281 GILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGH 360
Cdd:cd07100 229 GRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 361 RLTEngldKGFFFEPTLIAV--PDNhhKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAV 438
Cdd:cd07100 309 RPDG----PGAFYPPTVLTDvtPGM--PAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRL 382
|
410 420 430
....*....|....*....|....*....|
gi 613258995 439 RTGRIWINTYNQVPEGAPFGGYKKSGIGRE 468
Cdd:cd07100 383 EAGMVFINGMVKSDPRLPFGGVKRSGYGRE 412
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
30-485 |
3.62e-124 |
|
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: 370.00 E-value: 3.62e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 30 IEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRE--- 106
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDark 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 107 --TTAID-IPFA---ARHFHyfasvieteeGTVNDID-----KDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAA 175
Cdd:cd07149 81 evDRAIEtLRLSaeeAKRLA----------GETIPFDaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 176 GNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAkhLVPAT 254
Cdd:cd07149 151 GNAVVLKPASQTPLSALKLAELLLEAgLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 255 LELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTG 334
Cdd:cd07149 229 LELGSNAAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 335 KDQLDKIQSYIDAAKESDAQILAGGHRltengldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIAND 414
Cdd:cd07149 309 EAEAERIEEWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMAND 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613258995 415 SEYGLAGGVFSQNITRALNIAKAVRTGRIWIN---TYNQvpEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07149 382 SPYGLQAGVFTNDLQKALKAARELEVGGVMINdssTFRV--DHMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
16-481 |
2.69e-123 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 369.40 E-value: 2.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMI 95
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 96 ETLNNGKPIRETTAiDIPFAARHFHYFAsvietEEG--TVNDI----DKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKI 169
Cdd:PLN02278 108 MTLEQGKPLKEAIG-EVAYGASFLEYFA-----EEAkrVYGDIipspFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 170 APAIAAGNTIVIQPSSSTPLSLLEVAKI-FQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK 248
Cdd:PLN02278 182 GPALAAGCTVVVKPSELTPLTALAAAELaLQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 249 HLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQ 328
Cdd:PLN02278 262 TVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 329 MGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEA 408
Cdd:PLN02278 342 QGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHS----LGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEA 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613258995 409 IDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVK 481
Cdd:PLN02278 418 IAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIK 490
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
31-468 |
1.62e-121 |
|
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: 363.19 E-value: 1.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 31 EVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKiaMIETLnngkpIRETTAI 110
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADD--LIDLL-----IDEGGST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 111 dIPFAARHFHYFASVIETEEG--------TVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQ 182
Cdd:cd07150 75 -YGKAWFETTFTPELLRAAAGecrrvrgeTLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 183 PSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKS 261
Cdd:cd07150 154 PSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 262 ANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKI 341
Cdd:cd07150 234 PLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 342 QSYIDAAKESDAQILAGGHRltengldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAG 421
Cdd:cd07150 314 KRQVEDAVAKGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSA 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 613258995 422 GVFSQNITRALNIAKAVRTGRIWIN--TYNQVPEgAPFGGYKKSGIGRE 468
Cdd:cd07150 387 AILTNDLQRAFKLAERLESGMVHINdpTILDEAH-VPFGGVKASGFGRE 434
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
16-468 |
1.76e-121 |
|
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: 363.81 E-value: 1.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFvKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSK-SERAQMLRDIGDKLMAQKDKIAM 94
Cdd:cd07082 5 LINGEW-KESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTMPlEERIDCLHKFADLLKENKEEVAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 95 IETLNNGKP--------------IRETTaidipFAARHFHYFASVIETEEGTvndidKDTMSIVRHEPIGVVGAVVAWNF 160
Cdd:cd07082 84 LLMWEIGKTlkdalkevdrtidyIRDTI-----EELKRLDGDSLPGDWFPGT-----KGKIAQVRREPLGVVLAIGPFNY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 161 PMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVG 239
Cdd:cd07082 154 PLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAgFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 240 YQVAEAAAKhlVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKV 319
Cdd:cd07082 234 NRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 320 GNPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENgldkgfFFEPTLIAVPDNHHKLAQEEIFGPVLTV 399
Cdd:cd07082 312 GMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREGGN------LIYPTLLDPVTPDMRLAWEEPFGPVLPI 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 400 IKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQV-PEGAPFGGYKKSGIGRE 468
Cdd:cd07082 386 IRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRgPDHFPFLGRKDSGIGTQ 455
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
33-467 |
3.75e-118 |
|
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: 354.61 E-value: 3.75e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 33 TNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPiRETTAIDI 112
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKP-RADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 113 PFAARHFHYFAS----VIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTP 188
Cdd:cd07099 80 LLALEAIDWAARnaprVLAPRKVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 189 LSLLEVAKIFQEV-LPKGVVNILTGKGsESGNAIFNHdGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILD 267
Cdd:cd07099 160 LVGELLAEAWAAAgPPQGVLQVVTGDG-ATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 268 DANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDA 347
Cdd:cd07099 238 DADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 348 AKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQN 427
Cdd:cd07099 318 AVAKGAKALTGGARSN----GGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 613258995 428 ITRALNIAKAVRTGRIWIN---TYNQVPEgAPFGGYKKSGIGR 467
Cdd:cd07099 394 LARAEAIARRLEAGAVSINdvlLTAGIPA-LPFGGVKDSGGGR 435
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
38-466 |
1.19e-111 |
|
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: 337.73 E-value: 1.19e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 38 GETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIEtlnngkpIRETTAI------D 111
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWI-------VRESGSIrpkagfE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 112 IPFAARHFHYFASVIETEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSL 191
Cdd:cd07152 74 VGAAIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 -LEVAKIFQEV-LPKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDA 269
Cdd:cd07152 154 gVVIARLFEEAgLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 270 NLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAK 349
Cdd:cd07152 233 DLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 350 ESDAQILAGGHRltengldKGFFFEPTLIA--VPDNhhKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQN 427
Cdd:cd07152 313 AAGARLEAGGTY-------DGLFYRPTVLSgvKPGM--PAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRD 383
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 613258995 428 ITRALNIAKAVRTGRIWIN--TYNQVPEgAPFGGYKKSGIG 466
Cdd:cd07152 384 VGRAMALADRLRTGMLHINdqTVNDEPH-NPFGGMGASGNG 423
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
51-485 |
2.63e-111 |
|
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: 336.47 E-value: 2.63e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 51 DVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPiRETTAIDIPFAARHFHYFASVIET-E 129
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQiI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 130 EGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVN 208
Cdd:cd07105 80 GGSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAgLPKGVLN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 209 ILTGKGSESG---NAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFN 285
Cdd:cd07105 160 VVTHSPEDAPevvEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 286 QGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGnpqdeATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTEn 365
Cdd:cd07105 240 SGQICMSTERIIVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADES- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 366 glDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWI 445
Cdd:cd07105 314 --PSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 613258995 446 NTYNQVPE-GAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07105 392 NGMTVHDEpTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
5-464 |
9.98e-109 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 332.67 E-value: 9.98e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 5 VRDYIAENYGLFINGEFVKGssDETIEVTNPA-TGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGD 83
Cdd:PRK03137 29 VEKELGQDYPLIIGGERITT--EDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 84 KLMAQKDKIAMIETLNNGKPIRETTAiDIPFAARHFHYFA-SVIETEEG-TVNDIDKDTMSIVrHEPIGVvGAVVA-WNF 160
Cdd:PRK03137 107 IIRRRKHEFSAWLVKEAGKPWAEADA-DTAEAIDFLEYYArQMLKLADGkPVESRPGEHNRYF-YIPLGV-GVVISpWNF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 161 PMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVG 239
Cdd:PRK03137 184 PFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 240 YQVAEAAAK------HLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEA 313
Cdd:PRK03137 264 LRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 314 FSNIKVGNPqDEATQMGSQTGKDQLDKIQSYIDAAKEsDAQILAGGHRLTEngldKGFFFEPTLIAVPDNHHKLAQEEIF 393
Cdd:PRK03137 344 TKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKE-EGRLVLGGEGDDS----KGYFIQPTIFADVDPKARIMQEEIF 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613258995 394 GPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNitRAlNIAKAVRTGRIWiNTY-NQVPEGA-----PFGGYKKSG 464
Cdd:PRK03137 418 GPVVAFIKAKDFDHALEIANNTEYGLTGAVISNN--RE-HLEKARREFHVG-NLYfNRGCTGAivgyhPFGGFNMSG 490
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
16-481 |
3.79e-107 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 327.63 E-value: 3.79e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMI 95
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 96 ETLNNGKPIRETTAiDIPFAARHFHYFAsvietEEG------TVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKI 169
Cdd:PRK11241 94 MTLEQGKPLAEAKG-EISYAASFIEWFA-----EEGkriygdTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 170 APAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK 248
Cdd:PRK11241 168 GPALAAGCTMVLKPASQTPFSALALAELAIRAgIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 249 HLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQ 328
Cdd:PRK11241 248 DIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 329 MGSQTGKDQLDKIQSYIDAAKESDAQILAGG--HRLtengldKGFFFEPT-LIAVPDNhHKLAQEEIFGPVLTVIKVKDD 405
Cdd:PRK11241 328 IGPLIDEKAVAKVEEHIADALEKGARVVCGGkaHEL------GGNFFQPTiLVDVPAN-AKVAKEETFGPLAPLFRFKDE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 406 QEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVK 481
Cdd:PRK11241 401 ADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
34-467 |
5.52e-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: 326.56 E-value: 5.52e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 34 NPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRE------- 106
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDaslgeil 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 107 TTAIDIPFAARHFHYfASVIETEEGTVNDIDKDTMsiVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSS 186
Cdd:cd07098 82 VTCEKIRWTLKHGEK-ALRPESRPGGLLMFYKRAR--VEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 187 TPLSLLEVAKIFQEVL-----PKGVVNILTGKGsESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKS 261
Cdd:cd07098 159 VAWSSGFFLSIIRECLaacghDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 262 ANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKI 341
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 342 QSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAG 421
Cdd:cd07098 318 EELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 613258995 422 GVFSQNITRALNIAKAVRTGRIWIN-----TYNQvpeGAPFGGYKKSGIGR 467
Cdd:cd07098 398 SVFGKDIKRARRIASQLETGMVAINdfgvnYYVQ---QLPFGGVKGSGFGR 445
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
22-467 |
7.87e-107 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 327.99 E-value: 7.87e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 22 VKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNG 101
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 102 KPIR----ETtaIDIPFAARHF-----HYFASviETEEGTVNDIdkdTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPA 172
Cdd:PRK09407 106 KARRhafeEV--LDVALTARYYarrapKLLAP--RRRAGALPVL---TKTTELRQPKGVVGVISPWNYPLTLAVSDAIPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHdgVDKLSFTGSTDVGYQVAEAAAKHLV 251
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAAVELLYEAgLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 252 PATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGS 331
Cdd:PRK09407 257 GFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 332 QTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGldkGFFFEPTLIA-VPDNhHKLAQEEIFGPVLTVIKVKDDQEAID 410
Cdd:PRK09407 337 LISEAQLETVSAHVDDAVAKGATVLAGGKARPDLG---PLFYEPTVLTgVTPD-MELAREETFGPVVSVYPVADVDEAVE 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613258995 411 IANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN-----TYNQVpeGAPFGGYKKSGIGR 467
Cdd:PRK09407 413 RANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegyaaAWGSV--DAPMGGMKDSGLGR 472
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
30-485 |
5.40e-106 |
|
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: 323.62 E-value: 5.40e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 30 IEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTa 109
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 110 IDIPFAARHFHYFASVIETEEGTVNDID-----KDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPS 184
Cdd:cd07094 80 VEVDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 185 SSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVpaTLELGGKSAN 263
Cdd:cd07094 160 SKTPLSALELAKILVEAgVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGGKRI--ALELGGNAPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 264 IILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQS 343
Cdd:cd07094 238 IVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVER 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 344 YIDAAKESDAQILAGGHRltengldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGV 423
Cdd:cd07094 318 WVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613258995 424 FSQNITRALNIAKAVRTGRIWIN---TYNQvpEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07094 391 FTRDLNVAFKAAEKLEVGGVMVNdssAFRT--DWMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
35-483 |
2.31e-105 |
|
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: 321.95 E-value: 2.31e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 35 PATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIR----ETTai 110
Cdd:cd07101 3 PFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRhafeEVL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 111 DIPFAARHFHYFA-SVIETEE--GTVNDIdkdTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSST 187
Cdd:cd07101 81 DVAIVARYYARRAeRLLKPRRrrGAIPVL---TRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 188 PLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHdgVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIIL 266
Cdd:cd07101 158 ALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 267 DDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYID 346
Cdd:cd07101 236 EDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 347 AAKESDAQILAGGHRLTENGldkGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQ 426
Cdd:cd07101 316 DAVAKGATVLAGGRARPDLG---PYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613258995 427 NITRALNIAKAVRTGRIWIN-----TYNQVpeGAPFGGYKKSGIGRETYKGALSNYQQVKNI 483
Cdd:cd07101 393 DGARGRRIAARLRAGTVNVNegyaaAWASI--DAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
15-466 |
2.31e-104 |
|
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: 320.23 E-value: 2.31e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAM 94
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 95 IETLNNGKPIRET------------TAIDIPFAARHfhyfasviETEEGTVNDIDkdtmSIVRHEPIGVVGAVVAWNFPM 162
Cdd:cd07085 83 LITLEHGKTLADArgdvlrglevveFACSIPHLLKG--------EYLENVARGID----TYSYRQPLGVVAGITPFNFPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 163 LLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGYQ 241
Cdd:cd07085 151 MIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAgLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 242 VAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIqLGILF-NQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVG 320
Cdd:cd07085 230 IYERAAANGKRVQALGGAKNHAVVMPDADLEQTANAL-VGAAFgAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 321 NPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIavpDN---HHKLAQEEIFGPVL 397
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTIL---DNvtpDMKIYKEEIFGPVL 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613258995 398 TVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINtynqVPEGAP-----FGGYKKSGIG 466
Cdd:cd07085 386 SIVRVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
30-485 |
1.25e-101 |
|
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: 312.26 E-value: 1.25e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 30 IEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTA 109
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 110 iDIPFAARHFHYFASVIETEEGTVNDIDKDTMS-----IVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPS 184
Cdd:cd07147 81 -EVARAIDTFRIAAEEATRIYGEVLPLDISARGegrqgLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 185 SSTPLSLLEVAKIFQE-VLPKGVVNILTGKgSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVpaTLELGGKSAN 263
Cdd:cd07147 160 SRTPLSALILGEVLAEtGLPKGAFSVLPCS-RDDADLLVTDERIKLLSFTGSPAVGWDLKARAGKKKV--VLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 264 IILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQS 343
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 344 YIDAAKESDAQILAGGHRltengldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGV 423
Cdd:cd07147 317 WVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 424 FSQNITRALNIAKAVRTGRIWIntyNQVP----EGAPFGGYKKSGIGRETYKGALSNYQQVKNIYI 485
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVI---NDVPtfrvDHMPYGGVKDSGIGREGVRYAIEEMTEPRLLVI 452
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
78-487 |
2.26e-101 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 310.13 E-value: 2.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 78 LRDIGDKLMAQKDKIAMIETLNNGKpIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDKDTMSI-VRHEPIGVVGAVV 156
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGK-IQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENIlLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 157 AWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGS 235
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 236 TDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFS 315
Cdd:PRK10090 160 VSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 316 NIKVGNP-QDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFG 394
Cdd:PRK10090 240 AVQFGNPaERNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 395 PVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGAL 474
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGL 395
|
410
....*....|...
gi 613258995 475 SNYQQVKNIYIDT 487
Cdd:PRK10090 396 HEYLQTQVVYLQS 408
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
34-466 |
1.39e-97 |
|
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: 301.86 E-value: 1.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 34 NPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAiDIP 113
Cdd:cd07102 2 SPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 114 FAARHFHYFASVIETEEGTVNDIDKDTM-SIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLL 192
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFeRYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 193 EVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDgVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANL 271
Cdd:cd07102 161 RFAAAFAEAgLPEGVFQVLHLSHETSAALIADPR-IDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 272 DLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKES 351
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 352 DAQILAGGHRLTENGlDKGFFFEPTLIAvpDNHHKLA--QEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNIT 429
Cdd:cd07102 320 GARALIDGALFPEDK-AGGAYLAPTVLT--NVDHSMRvmREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 613258995 430 RALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIG 466
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRG 433
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
30-485 |
3.61e-93 |
|
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: 290.41 E-value: 3.61e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 30 IEVTNPATGETLSHITRAkdkDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETtA 109
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAG---TEEALREALALAASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDT-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 110 IDIPFAARHFHYFASVIETEEGTVNDID-----KDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPS 184
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFSCDltangKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 185 SSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAA-KHLVpatLELGGKSA 262
Cdd:cd07146 157 EKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAGyKRQL---LELGGNDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 263 NIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQ 342
Cdd:cd07146 234 LIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 343 SYIDAAKESDAQILAGGHRltengldKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGG 422
Cdd:cd07146 314 NRVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613258995 423 VFSQNITRALNIAKAVRTGRIWIntyNQVP----EGAPFGGYKKSG-IGRETYKGALSNYQQVKNIYI 485
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNV---NEVPgfrsELSPFGGVKDSGlGGKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
18-468 |
6.57e-93 |
|
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: 290.26 E-value: 6.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 18 NGEFvkGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIET 97
Cdd:cd07130 4 DGEW--GGGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 98 LNNGKPIRETTA-----IDI-PFA---ARHFHyfASVIETEEgtvndidKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWK 168
Cdd:cd07130 82 LEMGKILPEGLGevqemIDIcDFAvglSRQLY--GLTIPSER-------PGHRMMEQWNPLGVVGVITAFNFPVAVWGWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 169 IAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVL-----PKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGYQVA 243
Cdd:cd07130 153 AAIALVCGNVVVWKPSPTTPLTAIAVTKIVARVLeknglPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 244 EAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQ 323
Cdd:cd07130 232 QAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 324 DEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPdNHHKLAQEEIFGPVLTVIKVK 403
Cdd:cd07130 312 DDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVID----GPGNYVEPTIVEGL-SDAPIVKEETFAPILYVLKFD 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613258995 404 DDQEAIDIANDSEYGLAGGVFSQNITRALNI--AKAVRTGRIWINTYNQVPE-GAPFGGYKKSGIGRE 468
Cdd:cd07130 387 TLEEAIAWNNEVPQGLSSSIFTTDLRNAFRWlgPKGSDCGIVNVNIGTSGAEiGGAFGGEKETGGGRE 454
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
30-468 |
7.15e-83 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 263.91 E-value: 7.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 30 IEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTA 109
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 110 iDIPFAARHFHYFAsviETEEGTVNDIDKDTMSI------VRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQP 183
Cdd:PRK09406 83 -EALKCAKGFRYYA---EHAEALLADEPADAAAVgasrayVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 184 SSSTPLSLLEVAKIFQEV-LPKGVVNILTgKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSA 262
Cdd:PRK09406 159 ASNVPQTALYLADLFRRAgFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 263 NIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMG---SQTGKDQLD 339
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGplaTEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 340 KiqsYIDAAKESDAQILAGGHRLTENgldkGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGL 419
Cdd:PRK09406 318 K---QVDDAVAAGATILCGGKRPDGP----GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGL 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 613258995 420 AGGVFSQNITRALNIAKAVRTGRIWIN----TYnqvPEgAPFGGYKKSGIGRE 468
Cdd:PRK09406 391 GSNAWTRDEAEQERFIDDLEAGQVFINgmtvSY---PE-LPFGGVKRSGYGRE 439
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
34-486 |
3.34e-78 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 252.09 E-value: 3.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 34 NPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAiDIP 113
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA-EVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 114 FAARHFHYFA----SVIETEEGTVndidKDTMSIVRHEPIGVVGAVVAWNFPMllaaWKI----APAIAAGNTIVIQPSS 185
Cdd:PRK13968 92 KSANLCDWYAehgpAMLKAEPTLV----ENQQAVIEYRPLGTILAIMPWNFPL----WQVmrgaVPILLAGNGYLLKHAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 186 STPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIfNHDGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANI 264
Cdd:PRK13968 164 NVMGCAQLIAQVFKDAgIPQGVYGWLNADNDGVSQMI-NDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 265 ILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSY 344
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 345 IDAAKESDAQILAGGHRLTenglDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVF 424
Cdd:PRK13968 323 VEATLAEGARLLLGGEKIA----GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613258995 425 SQNITRALNIAKAVRTGRIWINTYNQVPEGAPFGGYKKSGIGRETYKGALSNYQQVKNIYID 486
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKD 460
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
5-469 |
6.67e-76 |
|
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: 247.11 E-value: 6.67e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 5 VRDYIAENYGLFINGEFVKgSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDK 84
Cdd:cd07083 11 VKEEFGRAYPLVIGGEWVD-TKERMVSVSPFAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 85 LMAQKDKIAMIETLNNGKPIRETTAiDIPFAARHFHYFASV---IETEEGTVNDIDKDTMSIVrHEPIGVVGAVVAWNFP 161
Cdd:cd07083 90 LRRRRRELIATLTYEVGKNWVEAID-DVAEAIDFIRYYARAalrLRYPAVEVVPYPGEDNESF-YVGLGAGVVISPWNFP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 162 MLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGY 240
Cdd:cd07083 168 VAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAgFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 241 QVAEAAAKHL------VPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAF 314
Cdd:cd07083 248 KIYEAAARLApgqtwfKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 315 SNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESdAQILAGGHRLTENgldkGFFFEPTLIAVPDNHHKLAQEEIFG 394
Cdd:cd07083 328 ERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNE-GQLVLGGKRLEGE----GYFVAPTVVEEVPPKARIAQEEIFG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 395 PVLTVIKVKDDQ--EAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTyNQVpeGA-----PFGGYKKSGIGR 467
Cdd:cd07083 403 PVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINR-KIT--GAlvgvqPFGGFKLSGTNA 479
|
..
gi 613258995 468 ET 469
Cdd:cd07083 480 KT 481
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
51-467 |
5.11e-74 |
|
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: 239.87 E-value: 5.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 51 DVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTA--------IDIPFAARHfhyf 122
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDISIKAYH---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 123 asvieTEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV- 201
Cdd:cd07095 77 -----ERTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 202 LPKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHL-VPATLELGGKSANIILDDANLDLAVEGIQL 280
Cdd:cd07095 152 LPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPgKILALEMGGNNPLVVWDVADIDAAAYLIVQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 281 GILFNQGEVCSAGSRLLVHEKIY-DQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGG 359
Cdd:cd07095 231 SAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 360 HRLTEngldKGFFFEPTLIAVpDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVR 439
Cdd:cd07095 311 ERLVA----GTAFLSPGIIDV-TDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIR 385
|
410 420
....*....|....*....|....*....
gi 613258995 440 TGRI-WINTYNQVPEGAPFGGYKKSGIGR 467
Cdd:cd07095 386 AGIVnWNRPTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
16-466 |
8.16e-73 |
|
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: 239.40 E-value: 8.16e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFvkGSSDETIEVTNPATGE-TLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDK--- 91
Cdd:cd07125 36 IINGEE--TETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGElia 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 92 IAMIE---TLNNGKP-IREttAIDI----PFAAR-HFHYFASVIETEEgtVNDIDKdtmsivrhEPIGVVGAVVAWNFPM 162
Cdd:cd07125 114 LAAAEagkTLADADAeVRE--AIDFcryyAAQAReLFSDPELPGPTGE--LNGLEL--------HGRGVFVCISPWNFPL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 163 LLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQ 241
Cdd:cd07125 182 AIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAgVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 242 VAEAAAKH---LVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIK 318
Cdd:cd07125 262 INRALAERdgpILPLIAETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLK 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 319 VGNPQDEATQMGSQTGKDQLDKIQSYIDaAKESDAQILAGGHRLTENgldkGFFFEPTLIAVP-DNHHklaQEEIFGPVL 397
Cdd:cd07125 342 VGDPWDLSTDVGPLIDKPAGKLLRAHTE-LMRGEAWLIAPAPLDDGN----GYFVAPGIIEIVgIFDL---TTEVFGPIL 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 398 TVIKVKDDQ--EAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTyNQVpeGA-----PFGGYKKSGIG 466
Cdd:cd07125 414 HVIRFKAEDldEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-NIT--GAivgrqPFGGWGLSGTG 486
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
14-464 |
1.49e-72 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 237.93 E-value: 1.49e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 14 GLFINGEFVKGSSdETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIA 93
Cdd:PRK09457 2 TLWINGDWIAGQG-EAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 94 MIETLNNGKPIRET----TA----IDIPFAARHfhyfasvieTEEGTVNDIDKDTMSIVRHEPIGVVGAVVAWNFPMLLA 165
Cdd:PRK09457 81 EVIARETGKPLWEAatevTAminkIAISIQAYH---------ERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 166 AWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGkGSESGNAIFNHDGVDKLSFTGSTDVGY---- 240
Cdd:PRK09457 152 NGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYllhr 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 241 QVAEAAAKHLvpaTLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIY-DQLVPRLQEAFSNIKV 319
Cdd:PRK09457 231 QFAGQPEKIL---ALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 320 GNP-QDEATQMGSQTGKDQLDKIQsyidaakESDAQILA-GGHRLTE-NGLDKGF-FFEPTLI---AVPDnhhkLAQEEI 392
Cdd:PRK09457 308 GRWdAEPQPFMGAVISEQAAQGLV-------AAQAQLLAlGGKSLLEmTQLQAGTgLLTPGIIdvtGVAE----LPDEEY 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613258995 393 FGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRI-WINTYNQVPEGAPFGGYKKSG 464
Cdd:PRK09457 377 FGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
10-486 |
5.98e-72 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 236.58 E-value: 5.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 10 AENYGLFINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQK 89
Cdd:PLN00412 13 GDVYKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 90 DKIAMIETLNNGKPIRETTAiDIPFAARHFHYFAsvietEEGT---------VNDI----DKDTMSIVRHEPIGVVGAVV 156
Cdd:PLN00412 93 APIAECLVKEIAKPAKDAVT-EVVRSGDLISYTA-----EEGVrilgegkflVSDSfpgnERNKYCLTSKIPLGVVLAIP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 157 AWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGS 235
Cdd:PLN00412 167 PFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAgFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 236 tDVGYQVAEAAAkhLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFS 315
Cdd:PLN00412 247 -DTGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 316 NIKVGNPQDEA--TQMGSQTGKDqldKIQSYIDAAKESDAQILAGGHRltengldKGFFFEPTLI--AVPDnhHKLAQEE 391
Cdd:PLN00412 324 KLTVGPPEDDCdiTPVVSESSAN---FIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLdnVRPD--MRIAWEE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 392 IFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTY-NQVPEGAPFGGYKKSGIGRETY 470
Cdd:PLN00412 392 PFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGSQGI 471
|
490
....*....|....*.
gi 613258995 471 KGALSNYQQVKNIYID 486
Cdd:PLN00412 472 TNSINMMTKVKSTVIN 487
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
49-472 |
6.15e-71 |
|
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: 232.11 E-value: 6.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 49 DKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAIDIPFAARHFHYFASVIET 128
Cdd:cd07135 4 LDEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 129 ----EEGTVNDIDKDTMSI-VRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLP 203
Cdd:cd07135 84 wakdEKVKDGPLAFMFGKPrIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 204 KGVVNILTGkGSESGNAIFNHdGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGIL 283
Cdd:cd07135 164 PDAFQVVQG-GVPETTALLEQ-KFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 284 FNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFsNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKesdAQILAGGhrlT 363
Cdd:cd07135 242 GNAGQICVAPDYVLVDPSVYDEFVEELKKVL-DEFYPGGANASPDYTRIVNPRHFNRLKSLLDTTK---GKVVIGG---E 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 364 ENGLDKgfFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRI 443
Cdd:cd07135 315 MDEATR--FIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGV 392
|
410 420 430
....*....|....*....|....*....|.
gi 613258995 444 WIN-TYNQVP-EGAPFGGYKKSGIGRetYKG 472
Cdd:cd07135 393 VINdTLIHVGvDNAPFGGVGDSGYGA--YHG 421
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
142-472 |
1.71e-68 |
|
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: 225.48 E-value: 1.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 142 SIVRHEPIGVVGAVVAWNFPMLLAawkIAP---AIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGKGSESg 218
Cdd:cd07087 94 AYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVAVVEGGVEVA- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 219 NAIFNHdGVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLV 298
Cdd:cd07087 170 TALLAE-PFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 299 HEKIYDQLVPRLQEAFSNiKVGNPQDEATQMGSQTGKDQLDKIQSYIDaakesDAQILAGGHRLTENgldkgFFFEPTLI 378
Cdd:cd07087 249 HESIKDELIEELKKAIKE-FYGEDPKESPDYGRIINERHFDRLASLLD-----DGKVVIGGQVDKEE-----RYIAPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 379 AVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIwinTYNQV-----PE 453
Cdd:cd07087 318 DDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGV---CVNDVllhaaIP 394
|
330
....*....|....*....
gi 613258995 454 GAPFGGYKKSGIGRetYKG 472
Cdd:cd07087 395 NLPFGGVGNSGMGA--YHG 411
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
144-472 |
4.56e-65 |
|
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: 216.58 E-value: 4.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 144 VRHEPIGVVGAVVAWNFPMLLAawkIAP---AIAAGNTIVIQPSSSTP-LSLLeVAKIFQEVLPKGVVNILTGkGSESGN 219
Cdd:cd07133 97 VEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPrTSAL-LAELLAEYFDEDEVAVVTG-GADVAA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 220 AI----FNHdgvdkLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSR 295
Cdd:cd07133 172 AFsslpFDH-----LLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 296 LLVHEKIYDQLVPRLQEAFSNI---KVGNPQDeaTQMGSQtgkDQLDKIQSYIDAAKESDAQIlaggHRLTENG--LDKG 370
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKMyptLADNPDY--TSIINE---RHYARLQGLLEDARAKGARV----IELNPAGedFAAT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 371 FFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN--TY 448
Cdd:cd07133 318 RKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtLL 397
|
330 340
....*....|....*....|....
gi 613258995 449 NQVPEGAPFGGYKKSGIGRetYKG 472
Cdd:cd07133 398 HVAQDDLPFGGVGASGMGA--YHG 419
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
15-464 |
7.56e-62 |
|
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: 210.52 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 15 LFINGEFVKgsSDETIEVTNPAT-GETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDkLMAQK--DK 91
Cdd:cd07123 35 LVIGGKEVR--TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAAD-LLSGKyrYE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 92 IAMIETLNNGKPIRETTaID-----IPFAarHFH-YFASVIETEEGTVNDidKDTMSIVRHEPI-GVVGAVVAWNFPMLL 164
Cdd:cd07123 112 LNAATMLGQGKNVWQAE-IDaacelIDFL--RFNvKYAEELYAQQPLSSP--AGVWNRLEYRPLeGFVYAVSPFNFTAIG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 165 AAWKIAPAIAaGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDV----G 239
Cdd:cd07123 187 GNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAgLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTfkslW 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 240 YQVAEAAAKHLVPATL--ELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNI 317
Cdd:cd07123 266 KQIGENLDRYRTYPRIvgETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEI 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 318 KVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESD-AQILAGGhrlteNGLD-KGFFFEPTLIAVPDNHHKLAQEEIFGP 395
Cdd:cd07123 346 KMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDPeAEIIAGG-----KCDDsVGYFVEPTVIETTDPKHKLMTEEIFGP 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 396 VLTVIKVKDDQ--EAIDIAND-SEYGLAGGVFSQNiTRALNIA-KAVR--TGRIWINTYnqvPEGA-----PFGGYKKSG 464
Cdd:cd07123 421 VLTVYVYPDSDfeETLELVDTtSPYALTGAIFAQD-RKAIREAtDALRnaAGNFYINDK---PTGAvvgqqPFGGARASG 496
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
142-466 |
1.00e-59 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 204.11 E-value: 1.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 142 SIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGkGSESGNAI 221
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVIEG-GVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 222 FNHDgVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEK 301
Cdd:PTZ00381 182 LKEP-FDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHRS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 302 IYDQLVPRLQEAFSNIKVGNPQdEATQMGSQTGKDQLDKIQSYIDAAKesdAQILAGGHRLTENGldkgfFFEPTLIAVP 381
Cdd:PTZ00381 261 IKDKFIEALKEAIKEFFGEDPK-KSEDYSRIVNEFHTKRLAELIKDHG---GKVVYGGEVDIENK-----YVAPTIIVNP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 382 DNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN--TYNQVPEGAPFGG 459
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGG 411
|
....*..
gi 613258995 460 YKKSGIG 466
Cdd:PTZ00381 412 VGNSGMG 418
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
30-466 |
5.48e-58 |
|
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: 198.80 E-value: 5.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 30 IEVTNPATGETLSHITRAKDKDVDHAVEVAQEAF---ESWslTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKP--- 103
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFldrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPlvd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 104 -IRETT-AID-IPFAARHFHYFASViE-----TEEGTvndidkDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAA 175
Cdd:cd07148 79 aKVEVTrAIDgVELAADELGQLGGR-EipmglTPASA------GRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 176 GNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKgSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAkhlvPAT 254
Cdd:cd07148 152 GCPVIVKPALATPLSCLAFVDLLHEAgLPEGWCQAVPCE-NAVAEKLVTDPRVAFFSFIGSARVGWMLRSKLA----PGT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 255 ---LELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGS 331
Cdd:cd07148 227 rcaLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 332 QTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENgldkgfFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDI 411
Cdd:cd07148 307 LIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDT------TYAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQ 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 613258995 412 ANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN--TYNQVpEGAPFGGYKKSGIG 466
Cdd:cd07148 381 ANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNdhTAFRV-DWMPFAGRRQSGYG 436
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
10-491 |
5.12e-57 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 197.36 E-value: 5.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 10 AENYGLFINGEFvkGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQK 89
Cdd:PLN02315 18 SRNLGCYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 90 DKIAMIETLNNGKPIRETTA-----IDI-PFA---ARHFHyfASVIETEEgtvndidKDTMSIVRHEPIGVVGAVVAWNF 160
Cdd:PLN02315 96 DYLGRLVSLEMGKILAEGIGevqeiIDMcDFAvglSRQLN--GSIIPSER-------PNHMMMEVWNPLGIVGVITAFNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 161 PMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVL-----PKGVVNILTGkGSESGNAIFNHDGVDKLSFTGS 235
Cdd:PLN02315 167 PCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLeknnlPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 236 TDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFS 315
Cdd:PLN02315 246 SKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 316 NIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGhRLTENGldkGFFFEPTLIAVPDNhHKLAQEEIFGP 395
Cdd:PLN02315 326 QVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGG-SAIESE---GNFVQPTIVEISPD-ADVVKEELFGP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 396 VLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITralNIAKAV-----RTGRIWINTYNQVPE-GAPFGGYKKSGIGRET 469
Cdd:PLN02315 401 VLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPE---TIFKWIgplgsDCGIVNVNIPTNGAEiGGAFGGEKATGGGREA 477
|
490 500
....*....|....*....|..
gi 613258995 470 YKGALSNYQQVKNIYIDTSNAL 491
Cdd:PLN02315 478 GSDSWKQYMRRSTCTINYGNEL 499
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
25-466 |
5.84e-57 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 204.71 E-value: 5.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 25 SSDETIEVTNPA-TGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDK---IAMIE---T 97
Cdd:PRK11905 564 VDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPElfaLAVREagkT 643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 98 LNNG-KPIREttAIDipfaarhF--HYFASVIETEEGTvndidkdtmsivRHEPIGVVGAVVAWNFPmlLAAW--KIAPA 172
Cdd:PRK11905 644 LANAiAEVRE--AVD-------FlrYYAAQARRLLNGP------------GHKPLGPVVCISPWNFP--LAIFtgQIAAA 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 173 IAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHL- 250
Cdd:PRK11905 701 LVAGNTVLAKPAEQTPLIAARAVRLLHEAgVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSg 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 251 --VPATLELGGKSAnIILDDANL------DLAVEGIQlgilfNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNP 322
Cdd:PRK11905 781 ppVPLIAETGGQNA-MIVDSSALpeqvvaDVIASAFD-----SAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDP 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 323 QDEATQMGSQTGKDQLDKIQSYIDAAKesdaqilAGGHRLTENGL----DKGFFFEPTLIAVpDNHHKLaQEEIFGPVLT 398
Cdd:PRK11905 855 WRLSTDVGPVIDAEAQANIEAHIEAMR-------AAGRLVHQLPLpaetEKGTFVAPTLIEI-DSISDL-EREVFGPVLH 925
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613258995 399 VIKVKDDQ--EAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTyNQVpeGA-----PFGGYKKSGIG 466
Cdd:PRK11905 926 VVRFKADEldRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNR-NII--GAvvgvqPFGGEGLSGTG 997
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
60-472 |
1.70e-56 |
|
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: 193.98 E-value: 1.70e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 60 QEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRET--TAI-----DIPFAARHFHYFASVIE----- 127
Cdd:cd07134 8 QAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVdlTEIlpvlsEINHAIKHLKKWMKPKRvrtpl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 128 TEEGTVndidkdtmSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVV 207
Cdd:cd07134 88 LLFGTK--------SKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 208 NILTGkGSESGNAI----FNHdgvdkLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGIL 283
Cdd:cd07134 160 AVFEG-DAEVAQALlelpFDH-----IFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 284 FNQGEVCSAGSRLLVHEKIYDQLVPRLQEAfsnIKVGNPQDEATQMGSQTG----KDQLDKIQSYIDAAKESDAQILAGG 359
Cdd:cd07134 234 LNAGQTCIAPDYVFVHESVKDAFVEHLKAE---IEKFYGKDAARKASPDLArivnDRHFDRLKGLLDDAVAKGAKVEFGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 360 -HRLTENgldkgfFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAV 438
Cdd:cd07134 311 qFDAAQR------YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLART 384
|
410 420 430
....*....|....*....|....*....|....*.
gi 613258995 439 RTGRIWINT--YNQVPEGAPFGGYKKSGIGRetYKG 472
Cdd:cd07134 385 SSGGVVVNDvvLHFLNPNLPFGGVNNSGIGS--YHG 418
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
142-472 |
6.22e-56 |
|
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: 193.10 E-value: 6.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 142 SIVRHEPIGVVGAVVAWNFPMLLAawkIAP---AIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGkGSESG 218
Cdd:cd07136 94 SYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVAVVEG-GVEEN 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 219 NAIFNHDgVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLV 298
Cdd:cd07136 170 QELLDQK-FDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 299 HEKIYDQLVPRLQEAFSNIKVGNPQDEATqMGSQTGKDQLDKIQSYIDAAKesdaqILAGGhrlteNGLDKGFFFEPTLI 378
Cdd:cd07136 249 HESVKEKFIKELKEEIKKFYGEDPLESPD-YGRIINEKHFDRLAGLLDNGK-----IVFGG-----NTDRETLYIEPTIL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 379 AVPDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN-TYNQVpegA-- 455
Cdd:cd07136 318 DNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdTIMHL---Anp 394
|
330
....*....|....*....
gi 613258995 456 --PFGGYKKSGIGRetYKG 472
Cdd:cd07136 395 ylPFGGVGNSGMGS--YHG 411
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
17-466 |
8.60e-54 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 195.16 E-value: 8.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 17 INGEfvkGSSDETIEVTNPA-TGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDK-IAM 94
Cdd:COG4230 562 IAGE---AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAElMAL 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 95 I--E---TLNNG-KPIREttAIDipfaarhF-HYFASVIETEEGTVndidkdtmsiVRHEPIGVVGAVVAWNFPmlLAAW 167
Cdd:COG4230 639 LvrEagkTLPDAiAEVRE--AVD-------FcRYYAAQARRLFAAP----------TVLRGRGVFVCISPWNFP--LAIF 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 168 --KIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAE 244
Cdd:COG4230 698 tgQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAgVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINR 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 245 A-AAKHLVPATL--ELGGKSANI-------------ILDDAnldlavegiqlgilFNqgevcSAGSR------LLVHEKI 302
Cdd:COG4230 778 TlAARDGPIVPLiaETGGQNAMIvdssalpeqvvddVLASA--------------FD-----SAGQRcsalrvLCVQEDI 838
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 303 YDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKesdaqilAGGHRLTE----NGLDKGFFFEPTLI 378
Cdd:COG4230 839 ADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMR-------AEGRLVHQlplpEECANGTFVAPTLI 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 379 AVPDnhhkLAQ--EEIFGPVLTVIKVKDDQ--EAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTyNQVpeG 454
Cdd:COG4230 912 EIDS----ISDleREVFGPVLHVVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVNR-NII--G 984
|
490
....*....|....*..
gi 613258995 455 A-----PFGGYKKSGIG 466
Cdd:COG4230 985 AvvgvqPFGGEGLSGTG 1001
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
32-466 |
9.31e-53 |
|
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: 185.88 E-value: 9.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 32 VTNPAT-GETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAi 110
Cdd:TIGR01238 55 VTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIA- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 111 DIPFAARHFHYFASVIEteegtvNDIDKDTmsivrHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLS 190
Cdd:TIGR01238 134 EVREAVDFCRYYAKQVR------DVLGEFS-----VESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 191 LLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHL---VPATLELGGKSANIIL 266
Cdd:TIGR01238 203 AYRAVELMQEAgFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREdapVPLIAETGGQNAMIVD 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 267 DDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYID 346
Cdd:TIGR01238 283 STALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 347 AAKESDAQIlaggHRLT-ENGLD--KGFFFEPTLIAVpDNHHKLaQEEIFGPVLTVIKVKDDQ--EAIDIANDSEYGLAG 421
Cdd:TIGR01238 363 HMSQTQKKI----AQLTlDDSRAcqHGTFVAPTLFEL-DDIAEL-SEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTM 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 613258995 422 GVFSQNITRALNIAKAVRTGRIWINTyNQVpeGA-----PFGGYKKSGIG 466
Cdd:TIGR01238 437 GVHSRIETTYRWIEKHARVGNCYVNR-NQV--GAvvgvqPFGGQGLSGTG 483
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
14-466 |
7.32e-50 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 183.48 E-value: 7.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 14 GLFINGefvkgsSDETIEVTNPA-TGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKI 92
Cdd:PRK11904 554 GPIING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAEL 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKPI-------REttAIDipF-------AARHFhyfaSVIETEEGTVNDidkdtMSIVRHEPIGVVGAVVAW 158
Cdd:PRK11904 628 IALCVREAGKTLqdaiaevRE--AVD--FcryyaaqARRLF----GAPEKLPGPTGE-----SNELRLHGRGVFVCISPW 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 159 NFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTD 237
Cdd:PRK11904 695 NFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAgIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTE 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 238 VGYQVAEA-AAKH--LVPATLELGGKSANI---------ILDDAnldlavegiqLGILFNQ-GEVCSAGSRLLVHEKIYD 304
Cdd:PRK11904 775 TARIINRTlAARDgpIVPLIAETGGQNAMIvdstalpeqVVDDV----------VTSAFRSaGQRCSALRVLFVQEDIAD 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 305 QLVPRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKeSDAQILAGGHRltENGLDKGFFFEPTLIAVPDnh 384
Cdd:PRK11904 845 RVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMK-REARLLAQLPL--PAGTENGHFVAPTAFEIDS-- 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 385 hkLAQ--EEIFGPVLTVIKVKDDQ--EAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTyNQVpeGA----- 455
Cdd:PRK11904 920 --ISQleREVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVNR-NQI--GAvvgvq 994
|
490
....*....|.
gi 613258995 456 PFGGYKKSGIG 466
Cdd:PRK11904 995 PFGGQGLSGTG 1005
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
147-475 |
1.76e-48 |
|
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: 172.60 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 147 EPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGkGSESGNAIFNHDG 226
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKVIEG-GVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 227 vDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGIL-FNQGEVCSAGSRLLVHE----K 301
Cdd:cd07137 179 -DKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEEsfapT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 302 IYDQLVPRLQEAFSNikvgNPQdEATQMGSQTGKDQLDKIQSYIDAAKESDaQILAGGHRlTENGLdkgfFFEPTLIAVP 381
Cdd:cd07137 258 LIDALKNTLEKFFGE----NPK-ESKDLSRIVNSHHFQRLSRLLDDPSVAD-KIVHGGER-DEKNL----YIEPTILLDP 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 382 DNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN-TYNQVP-EGAPFGG 459
Cdd:cd07137 327 PLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAiDTLPFGG 406
|
330
....*....|....*.
gi 613258995 460 YKKSGIGRetYKGALS 475
Cdd:cd07137 407 VGESGFGA--YHGKFS 420
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
16-483 |
4.97e-48 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 174.93 E-value: 4.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSSDETIEVTNPATGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMI 95
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMN 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 96 ETLNNGKPIRETTAiDIPFAARHFHYFASVIETEEG-----TVNDIDkdTMSIvrHEPIGVVGAVVAWNFPMLLAAWKIA 170
Cdd:PLN02419 197 ITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGeylpnVSNGVD--TYSI--REPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 171 PAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKgSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKH 249
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAgLPDGVLNIVHGT-NDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 250 LVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLV---HEKIYDQLVPRLQEafsnIKVGNPQDEA 326
Cdd:PLN02419 351 GKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSWEDKLVERAKA----LKVTCGSEPD 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 327 TQMGSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQ 406
Cdd:PLN02419 427 ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFD 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 407 EAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTynQVPEGAP---FGGYKKSGIGRETY--KGALSNYQQVK 481
Cdd:PLN02419 507 EAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPffsFTGNKASFAGDLNFygKAGVDFFTQIK 584
|
..
gi 613258995 482 NI 483
Cdd:PLN02419 585 LV 586
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
55-475 |
1.21e-47 |
|
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: 170.48 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 55 AVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKI--AMIETLNngKPIRETTAIDIPFAARHFHYFASVIET---- 128
Cdd:cd07132 3 AVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIveALAKDLR--KPKFEAVLSEILLVKNEIKYAISNLPEwmkp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 129 ---EEGTVNDIDkDTMsiVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPlsllEVAKIFQEVLPKG 205
Cdd:cd07132 81 epvKKNLATLLD-DVY--IYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP----ATAKLLAELIPKY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 206 VVN----ILTGkGSESGNAIFNHDgVDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLG 281
Cdd:cd07132 154 LDKecypVVLG-GVEETTELLKQR-FDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 282 ILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQdEATQMGSQTGKDQLDKIQSYIDAAKesdaqILAGGhr 361
Cdd:cd07132 232 KFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPK-ESPDYGRIINDRHFQRLKKLLSGGK-----VAIGG-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 362 lteNGLDKGFFFEPT-LIAVPDNhHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQN---ITRALNiaka 437
Cdd:cd07132 304 ---QTDEKERYIAPTvLTDVKPS-DPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNkkvINKILS---- 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 613258995 438 vRT--GRIWIN-TYNQ-VPEGAPFGGYKKSGIGRetYKGALS 475
Cdd:cd07132 376 -NTssGGVCVNdTIMHyTLDSLPFGGVGNSGMGA--YHGKYS 414
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
25-466 |
8.12e-46 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 172.08 E-value: 8.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 25 SSDETIEVTNPA-TGETLSHITRAKDKDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMI------ET 97
Cdd:PRK11809 656 AAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLlvreagKT 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 98 LNNG-KPIREttAIDIpfaarhFHYFASVIEteegtvNDIDKDTmsivrHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAG 176
Cdd:PRK11809 736 FSNAiAEVRE--AVDF------LRYYAGQVR------DDFDNDT-----HRPLGPVVCISPWNFPLAIFTGQVAAALAAG 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 177 NTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAKHL----- 250
Cdd:PRK11809 797 NSVLAKPAEQTPLIAAQAVRILLEAgVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRNLAGRLdpqgr 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 251 -VPATLELGGKSAnIILDDANLDLAVEGIQLGILFNQ-GEVCSAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQ 328
Cdd:PRK11809 877 pIPLIAETGGQNA-MIVDSSALTEQVVADVLASAFDSaGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTD 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 329 MGSQTGKDQLDKIQSYIDAAKESdaqilagGHRLT----ENGLD--KGFFFEPTLIAVpDNHHKLaQEEIFGPVLTVIKV 402
Cdd:PRK11809 956 IGPVIDAEAKANIERHIQAMRAK-------GRPVFqaarENSEDwqSGTFVPPTLIEL-DSFDEL-KREVFGPVLHVVRY 1026
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613258995 403 KDDQ--EAIDIANDSEYGLAGGVFS---QNITRALNIAKAvrtGRIWINTyNQVpeGA-----PFGGYKKSGIG 466
Cdd:PRK11809 1027 NRNQldELIEQINASGYGLTLGVHTridETIAQVTGSAHV---GNLYVNR-NMV--GAvvgvqPFGGEGLSGTG 1094
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
16-446 |
8.94e-41 |
|
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: 153.19 E-value: 8.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSsDETIEVTNPATGETLSHITRAK---DKDVDHAVEVAQEAFESWSLtskSERAQMLRDIGDKLMAQKDKI 92
Cdd:cd07128 4 YVAGQWHAGT-GDGRTLHDAVTGEVVARVSSEGldfAAAVAYAREKGGPALRALTF---HERAAMLKALAKYLMERKEDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 93 AMIETLNNGKpiRETTAIDIPFAARHFHYFASVIETE--------EGTVNDIDKDTMSIVRH--EPI-GVVGAVVAWNFP 161
Cdd:cd07128 80 YALSAATGAT--RRDSWIDIDGGIGTLFAYASLGRRElpnahflvEGDVEPLSKDGTFVGQHilTPRrGVAVHINAFNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 162 mllaAW----KIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQE--VLPKGVVNILTGkgseSGNAIFNH-DGVDKLSFTG 234
Cdd:cd07128 158 ----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVEsgLLPEGALQLICG----SVGDLLDHlGEQDVVAFTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 235 STDVGYQ--VAEAAAKHLVPATLELGGKSANIILDDAN-----LDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLV 307
Cdd:cd07128 230 SAATAAKlrAHPNIVARSIRFNAEADSLNAAILGPDATpgtpeFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 308 PRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKEsDAQILAGG-HRLTENGLD--KGFFFEPTLIAV--PD 382
Cdd:cd07128 310 EALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLA-EAEVVFGGpDRFEVVGADaeKGAFFPPTLLLCddPD 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 383 NHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQN--ITRALNIAKAVRTGRIWIN 446
Cdd:cd07128 389 AATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDpaFARELVLGAAPYHGRLLVL 454
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
16-425 |
4.58e-37 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 142.92 E-value: 4.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 16 FINGEFVKGSSDETIeVTNPATGETLSHiTRAKDKDVDHAVEVAQE----AFESWSLtskSERAQMLRDIGDKLMAQKDK 91
Cdd:PRK11903 8 YVAGRWQAGSGAGTP-LFDPVTGEELVR-VSATGLDLAAAFAFAREqggaALRALTY---AQRAALLAAIVKVLQANRDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 92 IAMIETLNNGKpIRETTAIDIPFAARHFHYFASVIET-------EEGTVNDIDKDTMSIVRHEPI---GVVGAVVAWNFP 161
Cdd:PRK11903 83 YYDIATANSGT-TRNDSAVDIDGGIFTLGYYAKLGAAlgdarllRDGEAVQLGKDPAFQGQHVLVptrGVALFINAFNFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 162 mllaAW----KIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQE--VLPKGVVNILTGkgseSGNAIFNH-DGVDKLSFTG 234
Cdd:PRK11903 162 ----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAagILPAGALSVVCG----SSAGLLDHlQPFDVVSFTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 235 STDVGYQVAE--AAAKHLVPATLELGGKSANIILDDAN-----LDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLV 307
Cdd:PRK11903 234 SAETAAVLRShpAVVQRSVRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 308 PRLQEAFSNIKVGNPQDEATQMGSQTGKDQLDKIQSYIDAAKEsDAQILAGG--HRLTENGLDKGFFFEPTLIAV--PDN 383
Cdd:PRK11903 314 EALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRA-QAEVLFDGggFALVDADPAVAACVGPTLLGAsdPDA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 613258995 384 HHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFS 425
Cdd:PRK11903 393 ATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
147-475 |
1.82e-35 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 137.87 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 147 EPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGKGSESgNAIFNHDG 226
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAVTET-TALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 227 vDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGIL-FNQGEVCSAGSRLLVHEKIYDQ 305
Cdd:PLN02174 190 -DKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYILTTKEYAPK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 306 LVPRLQEAFSNIKVGNPQdEATQMGSQTGKDQLDKIQSYIDAAKESDaQILAGGHRLTENgldkgFFFEPT-LIAVPDNh 384
Cdd:PLN02174 269 VIDAMKKELETFYGKNPM-ESKDMSRIVNSTHFDRLSKLLDEKEVSD-KIVYGGEKDREN-----LKIAPTiLLDVPLD- 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 385 HKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWIN--TYNQVPEGAPFGGYKK 462
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiAVHLALHTLPFGGVGE 420
|
330
....*....|...
gi 613258995 463 SGIGreTYKGALS 475
Cdd:PLN02174 421 SGMG--AYHGKFS 431
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
52-408 |
7.63e-35 |
|
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: 135.44 E-value: 7.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 52 VDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAIDIPFAarHFHYFASVIET--- 128
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQV--QLRARAFVIYSyri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 129 EEGTVNDIDKDTMSIVRHE--PIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV--LPK 204
Cdd:cd07084 79 PHEPGNHLGQGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAglLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 205 GVVNILTGKGsESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAakHLVPATLELGGKSANIILDDAN-LDLAVEGIQLGIL 283
Cdd:cd07084 159 EDVTLINGDG-KTMQALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 284 FNQGEVCSAGSRLLVHEKiyDQLVPRLQEAFSNIKVGNPQDeatqmgSQTGKDQLDKIQSYIDAAKESDAQILAGGHRLT 363
Cdd:cd07084 236 ACSGQKCTAQSMLFVPEN--WSKTPLVEKLKALLARRKLED------LLLGPVQTFTTLAMIAHMENLLGSVLLFSGKEL 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 613258995 364 ENGLDKGFF--FEPTLIAVP----DNHHKLAQEEIFGPVLTVIKVKDDQEA 408
Cdd:cd07084 308 KNHSIPSIYgaCVASALFVPideiLKTYELVTEEIFGPFAIVVEYKKDQLA 358
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
147-475 |
1.89e-34 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 135.24 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 147 EPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTGkGSESGNAIFNHDG 226
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVKVIEG-GPAVGEQLLQHKW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 227 vDKLSFTGSTDVGYQVAEAAAKHLVPATLELGGKSANII--LDDA-NLDLAVEGIqLGILFN--QGEVCSAGSRLLVHEK 301
Cdd:PLN02203 186 -DKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdsLSSSrDTKVAVNRI-VGGKWGscAGQACIAIDYVLVEER 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 302 IYDQLVPRLQEAFSNIKVGNPQdEATQMGSQTGKDQLDKIQSYIDaAKESDAQILAGGHrltengLD-KGFFFEPTLIAV 380
Cdd:PLN02203 264 FAPILIELLKSTIKKFFGENPR-ESKSMARILNKKHFQRLSNLLK-DPRVAASIVHGGS------IDeKKLFIEPTILLN 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 381 PDNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIwinTYNQ-----VPEGA 455
Cdd:PLN02203 336 PPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDaiiqyACDSL 412
|
330 340
....*....|....*....|
gi 613258995 456 PFGGYKKSGIGRetYKGALS 475
Cdd:PLN02203 413 PFGGVGESGFGR--YHGKYS 430
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
52-454 |
7.48e-27 |
|
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: 112.63 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 52 VDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKI---AMIETlnnGKPIRETTAiDIPFAARHFHYFASVIEt 128
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELvarAHAET---GLPEARLQG-ELGRTTGQLRLFADLVR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 129 eEGTVNDIDKDTMSIVRHE-----------PIGVVGAVVAWNFPMllaAWKI-----APAIAAGNTIVIQPSSSTP-LSL 191
Cdd:cd07129 76 -EGSWLDARIDPADPDRQPlprpdlrrmlvPLGPVAVFGASNFPL---AFSVaggdtASALAAGCPVVVKAHPAHPgTSE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LeVAKIFQEV-----LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGSTDVGYQVAEAAAK--HLVPATLELGgkSAN- 263
Cdd:cd07129 152 L-VARAIRAAlratgLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELG--SVNp 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 264 -IILDDAnldLAVEGIQLG------ILFNQGEVC-SAGSRLLVHEKIYDQLVPRLQEAFSNIKVGNPQDEATQMGSQTGK 335
Cdd:cd07129 229 vFILPGA---LAERGEAIAqgfvgsLTLGAGQFCtNPGLVLVPAGPAGDAFIAALAEALAAAPAQTMLTPGIAEAYRQGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 336 DQLdkiqsyidaAKESDAQILAGGHrltenGLDKGFFFEPTLIAVPD----NHHKLaQEEIFGPVLTVIKVKDDQEAIDI 411
Cdd:cd07129 306 EAL---------AAAPGVRVLAGGA-----AAEGGNQAAPTLFKVDAaaflADPAL-QEEVFGPASLVVRYDDAAELLAV 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 613258995 412 AN-------------DSEYGLAggvfsQNITRALniakAVRTGRIwinTYNQVPEG 454
Cdd:cd07129 371 AEalegqltatihgeEDDLALA-----RELLPVL----ERKAGRL---LFNGWPTG 414
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
52-447 |
6.51e-18 |
|
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: 85.78 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 52 VDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAIDIPFAARHFhYFASVIETEEG 131
Cdd:cd07081 1 LDDAVAAAKVAQQGLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKVIKNHFAAEYI-YNVYKDEKTCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 132 TVNDiDKDTMSIVRHEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVL-----PKGV 206
Cdd:cd07081 80 VLTG-DENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAAvaagaPENL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 207 VNILTGKGSESGNAIFNHDGVDKLSFTGstdvGYQVAEAAAKHLVPATLELGGKSANIILDDANLDLAVEGIQLGILFNQ 286
Cdd:cd07081 159 IGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 287 GEVCSAGSRLLVHEKIYDQLVPRLQEafsnikvgnpqdeatQMGSQTGKDQLDKIQSYIDAAKESDAQIL---------A 357
Cdd:cd07081 235 GVICASEQSVIVVDSVYDEVMRLFEG---------------QGAYKLTAEELQQVQPVILKNGDVNRDIVgqdaykiaaA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 358 GGHRLTENglDKGFFFEPTLIAvpdnHHKLAQEEIFGPVLTVIKVKDDQEAIDIA----NDSEYGLAGGVFSQNITRALN 433
Cdd:cd07081 300 AGLKVPQE--TRILIGEVTSLA----EHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIEN 373
|
410
....*....|....*..
gi 613258995 434 I---AKAVRTGRIWINT 447
Cdd:cd07081 374 MnqfANAMKTSRFVKNG 390
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
74-473 |
2.19e-17 |
|
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: 83.81 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 74 RAQMLRDIGDKLMAQKDKIAMIETLNNGKPIRETTAIDIPFAARHFHYFASVIETEEGTVNDIDK--------DTMSIVR 145
Cdd:cd07077 18 RDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSESKLYKNIDTERGITASVGHiqdvllpdNGETYVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 146 HEPIGVVGAVVAWNFPmLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVVNILTG----KGSESGNAI 221
Cdd:cd07077 98 AFPIGVTMHILPSTNP-LSGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLyvphPSDELAEEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 222 FNHDGVDKLSFTGstdvGYQVAEAAAKH--LVPAtLELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVH 299
Cdd:cd07077 177 LSHPKIDLIVATG----GRDAVDAAVKHspHIPV-IGFGAGNSPVVVDETADEERASGSVHDSKFFDQNACASEQNLYVV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 300 EKIYDQLVPRLQEAFSNIKVGNPQDEatqmgsqtgkdqldKIQSYidaakesdaqilagghrltengldkgfffeptliA 379
Cdd:cd07077 252 DDVLDPLYEEFKLKLVVEGLKVPQET--------------KPLSK----------------------------------E 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 380 VPDNHHKLAQEEiFGPVLTVIKVKD----DQEAIDIANDSEYGLAGGVFSQNITRALNIAKAVRTGRIWINTYNQVPEGA 455
Cdd:cd07077 284 TTPSFDDEALES-MTPLECQFRVLDvisaVENAWMIIESGGGPHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGA 362
|
410 420
....*....|....*....|
gi 613258995 456 PFGGYKKSGI--GRETYKGA 473
Cdd:cd07077 363 FAGKGVERIVtsGMNNIFGA 382
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
121-459 |
8.80e-17 |
|
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: 82.54 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 121 YFASvieteEGTVNDI-DKDTMSIVRH----------EPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPL 189
Cdd:cd07122 62 HFAS-----EYVYNDIkDMKTVGVIEEdeekgiveiaEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 190 SLLEVAKIFQEV-----LPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGstdvGYQVAEAAAKHLVPAtleLGGKSAN- 263
Cdd:cd07122 137 CSIEAAKIMREAavaagAPEGLIQWIEEPSIELTQELMKHPDVDLILATG----GPGMVKAAYSSGKPA---IGVGPGNv 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 264 --IILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEA---FSNikvgnpqdeatqmgsqtgKDQL 338
Cdd:cd07122 210 paYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEIYDEVRAELKRRgayFLN------------------EEEK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 339 DKIQSYI---------DAAKESDAQI--LAGghrltengldkgffFE-P---TLIAVPDNH----HKLAQEEIFgPVLTV 399
Cdd:cd07122 272 EKLEKALfddggtlnpDIVGKSAQKIaeLAG--------------IEvPedtKVLVAEETGvgpeEPLSREKLS-PVLAF 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613258995 400 IKVKDDQEAIDIAND-SEYGLAG---GVFSQNITRALNIAKAVRTGRIWINTynqvpeGAPFGG 459
Cdd:cd07122 337 YRAEDFEEALEKARElLEYGGAGhtaVIHSNDEEVIEEFALRMPVSRILVNT------PSSLGG 394
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
50-440 |
1.10e-16 |
|
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: 81.90 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 50 KDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIEtlnngkpiRETTAIdipfaARHFHYFASVIETE 129
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMA--------VEETGM-----GRVEDKIAKNHLAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 130 EGT--VNDIDKDT------MSIVRHEPIGVVGAV---------VAWNFPMLLAAwkiapaiaaGNTIVIQP-SSSTPLSL 191
Cdd:cd07121 71 EKTpgTEDLTTTAwsgdngLTLVEYAPFGVIGAItpstnptetIINNSISMLAA---------GNAVVFNPhPGAKKVSA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 192 LEV----AKIFQEVLPKGVVNILTGKGSESGNAIFNHDGVDKLSFTGstdvGYQVAEAAAKHlvpatlelgGKSA----- 262
Cdd:cd07121 142 YAVelinKAIAEAGGPDNLVVTVEEPTIETTNELMAHPDINLLVVTG----GPAVVKAALSS---------GKKAigaga 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 263 -N--IILDD-ANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQE--AFsniKVGNPQDEA-------TQM 329
Cdd:cd07121 209 gNppVVVDEtADIEKAARDIVQGASFDNNLPCIAEKEVIAVDSVADYLIAAMQRngAY---VLNDEQAEQllevvllTNK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 330 GSQTGKDQLDKIQSYIDAAK--ESDAQIlagghRLtengldkgfffeptLIAVPDNHHKLAQEEIFGPVLTVIKVKDDQE 407
Cdd:cd07121 286 GATPNKKWVGKDASKILKAAgiEVPADI-----RL--------------IIVETDKDHPFVVEEQMMPILPVVRVKNFDE 346
|
410 420 430
....*....|....*....|....*....|....*
gi 613258995 408 AIDIANDSEYGL--AGGVFSQNITRALNIAKAVRT 440
Cdd:cd07121 347 AIELAVELEHGNrhTAIIHSKNVENLTKMARAMQT 381
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
50-440 |
2.86e-15 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 78.02 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 50 KDVDHAVEVAQEAFESWSLTSKSERAQMLRDIGDKLMAQKDKIAMIEtlnngkpirettaidipfaarhfhyfasVIETE 129
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELA----------------------------VEETG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 130 EGTVND--------IDK---------------DTMSIVRHEPIGVVGAVVAWNFPmllAAWKIAPAI---AAGNTIVIQP 183
Cdd:PRK15398 88 MGRVEDkiaknvaaAEKtpgvedlttealtgdNGLTLIEYAPFGVIGAVTPSTNP---TETIINNAIsmlAAGNSVVFSP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 184 -SSSTPLSLLEVAKIFQEVL----PKGVVNILTGKGSESGNAIFNHDGVDKLSFTGstdvGYQVAEAAAKhlvpatlelG 258
Cdd:PRK15398 165 hPGAKKVSLRAIELLNEAIVaaggPENLVVTVAEPTIETAQRLMKHPGIALLVVTG----GPAVVKAAMK---------S 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 259 GKSA------N--IILDD-ANLDLAVEGIQLGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQE--AFsnikvgnpqdeat 327
Cdd:PRK15398 232 GKKAigagagNppVVVDEtADIEKAARDIVKGASFDNNLPCIAEKEVIVVDSVADELMRLMEKngAV------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 328 qmgsQTGKDQLDKIQsyidaakesdAQILAGGHRLTEN--GLDKGFFFEPTLIAVPDN----------HHKLAQEEIFGP 395
Cdd:PRK15398 299 ----LLTAEQAEKLQ----------KVVLKNGGTVNKKwvGKDAAKILEAAGINVPKDtrllivetdaNHPFVVTELMMP 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 613258995 396 VLTVIKVKDDQEAIDIANDSEYGL--AGGVFSQNITRALNIAKAVRT 440
Cdd:PRK15398 365 VLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSRNVDNLNKMARAIQT 411
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
130-447 |
1.87e-11 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 66.75 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 130 EGTVNDIDKD-TMSIVR-HEPIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-----L 202
Cdd:PRK13805 88 EKTVGVIEEDdEFGIIEiAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVLDAavaagA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 203 PKGVVNILTGKGSESGNAIFNHDGVDKLSFTGstdvGYQVAEAAAKHLVPAtleLG---GKSANIILDDANLDLAVEGIQ 279
Cdd:PRK13805 168 PKDIIQWIEEPSVELTNALMNHPGIALILATG----GPGMVKAAYSSGKPA---LGvgaGNVPAYIDKTADIKRAVNDIL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 280 LGILFNQGEVCSAGSRLLVHEKIYDQLVPRLQEA---FSNikvgnpqdeatqmgsqtgKDQLDKIQSYI----------D 346
Cdd:PRK13805 241 LSKTFDNGMICASEQAVIVDDEIYDEVKEEFASHgayFLN------------------KKELKKLEKFIfgkengalnaD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 347 AAKESDAQI--LAGghrltengldkgfffeptlIAVPDN-------------HHKLAQEEIFgPVLTVIKVKDDQEAIDI 411
Cdd:PRK13805 303 IVGQSAYKIaeMAG-------------------FKVPEDtkiliaevkgvgeSEPLSHEKLS-PVLAMYKAKDFEDAVEK 362
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 613258995 412 AND-SEYGLAG---GVFSQNITRALNIAKAVRTGRIWINT 447
Cdd:PRK13805 363 AEKlVEFGGLGhtaVIYTNDDELIKEFGLRMKACRILVNT 402
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
148-428 |
2.45e-08 |
|
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: 56.35 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 148 PIGVVGAVVAWNFPMLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEV-LPKGVVNILTGKGSESgNAIFNHDG 226
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCgMPATDVDLIHSDGPTM-NKILLEAN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 227 VDKLSFTGSTDVgyqvaeaaAKHLvpaTLELGGKsanIILDDANLDLAVEGIQLGIL------FNQ------GEVCSAGS 294
Cdd:cd07126 221 PRMTLFTGSSKV--------AERL---ALELHGK---VKLEDAGFDWKILGPDVSDVdyvawqCDQdayacsGQKCSAQS 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 295 RLLVHEKIYDQ-LVPRLQEA-----FSNIKVGnpqdEATQMGSQTGKDQLDKIQSyIDAAKesdaqILAGGHRLTENGLD 368
Cdd:cd07126 287 ILFAHENWVQAgILDKLKALaeqrkLEDLTIG----PVLTWTTERILDHVDKLLA-IPGAK-----VLFGGKPLTNHSIP 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613258995 369 KGF-FFEPTLIAVP------DNHHKLAQEEIFGPVLTVIKVKDDQE--AIDIANDSEYGLAGGVFSQNI 428
Cdd:cd07126 357 SIYgAYEPTAVFVPleeiaiEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDI 425
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
158-446 |
1.73e-07 |
|
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: 53.64 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 158 WN-FPMLLAAwkiapaIAAGNTIVIQPSSSTPLSLLEVAKIFQEVL------PKGVVNILTGKGSESGNAIFNHDGVDKL 230
Cdd:cd07127 208 WNgYPGLFAS------LATGNPVIVKPHPAAILPLAITVQVAREVLaeagfdPNLVTLAADTPEEPIAQTLATRPEVRII 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 231 SFTGSTDVGYQVAEAAAKHLVPAtlELGGKSANIILDDANLDLAVEGIQLGILFNQGEVCSAGSRLLV---------HEK 301
Cdd:cd07127 282 DFTGSNAFGDWLEANARQAQVYT--EKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVprdgiqtddGRK 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613258995 302 IYDQLVPRLQEAFSNIkVGNPQDEATQMGSQTGKDQLDKIqsyidAAKESDAQILAGGHRLTENGLDKGFFFEPTLIAVP 381
Cdd:cd07127 360 SFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARI-----AEARQLGEVLLASEAVAHPEFPDARVRTPLLLKLD 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613258995 382 DNHHKLAQEEIFGPVLTVIKVKDDQEAIDIANDS--EYG-LAGGVFS---------QNITRALNIAKAVR-TGRIWIN 446
Cdd:cd07127 434 ASDEAAYAEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYStdpevvervQEAALDAGVALSINlTGGVFVN 511
|
|
| ALDH_Acyl-CoA-Red_LuxC |
cd07080 |
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase ... |
144-207 |
7.84e-03 |
|
Acyl-CoA reductase LuxC; Acyl-CoA reductase, LuxC, (EC=1.2.1.50) is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase. The fatty acid reductase, a luminescence-specific, multienzyme complex (LuxCDE), reduces myristic acid to generate the long chain fatty aldehyde required for the luciferase-catalyzed reaction resulting in the emission of blue-green light. Mutational studies of conserved cysteines of LuxC revealed that the cysteine which aligns with the catalytic cysteine conserved throughout the ALDH superfamily is the LuxC acylation site. This CD is composed of mainly bacterial sequences but also includes a few archaeal sequences similar to the Methanospirillum hungateiacyl acyl-CoA reductase RfbN.
Pssm-ID: 143399 Cd Length: 422 Bit Score: 38.80 E-value: 7.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613258995 144 VRHEPIGVVGAVVAWNFPmLLAAWKIAPAIAAGNTIVIQPSSSTPLSLLEVAKIFQEVLPKGVV 207
Cdd:cd07080 108 IRAQPRGLVVHIIAGNVP-LLPVWSIVRGLLVKNVNLLKMSSSDPLTATALLRSLADVDPNHPL 170
|
|
| |
