|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
26-476 |
0e+00 |
|
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: 719.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEI 105
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 106 INAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASP 185
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 186 AELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDAD 265
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 266 LAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVS 345
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 346 KGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHAL 425
Cdd:cd07103 321 KGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 674257992 426 SQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFISQ 476
Cdd:cd07103 401 AEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
3-475 |
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: 596.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 3 SYPDIKLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQR 82
Cdd:COG1012 2 TTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 83 IDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRK 162
Cdd:COG1012 82 REELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 163 LSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAG 242
Cdd:COG1012 162 LAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 243 KHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADT 322
Cdd:COG1012 242 ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 323 TMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRI-GNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALE 401
Cdd:COG1012 322 DMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIA 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674257992 402 EANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN-HNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:COG1012 402 LANDTEYGLAASVFTRDLARARRVARRLEAGMVWINdGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
15-474 |
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: 559.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 15 WRDAlSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQ 94
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 95 GKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSII 174
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 175 VKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGG 254
Cdd:pfam00171 159 LKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 255 HAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIP 334
Cdd:pfam00171 239 KNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 335 AMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYA 414
Cdd:pfam00171 319 RVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674257992 415 FTGSVKTAHALSQRVEAGMLTVN-HNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:pfam00171 399 FTSDLERALRVARRLEAGMVWINdYTTGDADGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
10-474 |
1.34e-171 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 491.90 E-value: 1.34e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWL 89
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 90 MTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVAT 169
Cdd:PLN02278 108 MTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 170 GCSIIVKAPEETPAS---PAELIrafVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMK 246
Cdd:PLN02278 188 GCTVVVKPSELTPLTalaAAELA---LQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 247 RATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGP 326
Cdd:PLN02278 265 RVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 327 LANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRL 406
Cdd:PLN02278 345 LINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDT 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674257992 407 PFGLASYAFTGSVKTAHALSQRVEAGMLTVNhNGLAIPEV-PFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:PLN02278 425 EAGLAAYIFTRDLQRAWRVSEALEYGIVGVN-EGLISTEVaPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
55-472 |
1.86e-169 |
|
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: 484.02 E-value: 1.86e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 55 KGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGV 134
Cdd:cd07078 9 AAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 135 SNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISE 214
Cdd:cd07078 89 LAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 215 YLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQ 294
Cdd:cd07078 169 ALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVH 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 295 DSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGN-KGNFFEPTVLTDVP 373
Cdd:cd07078 249 ESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVPPTVLTDVD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 374 TSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN-HNGLAIPEVPFGGIK 452
Cdd:cd07078 329 PDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINdYSVGAEPSAPFGGVK 408
|
410 420
....*....|....*....|
gi 674257992 453 DSGYGTEGGSEAVEAYLETR 472
Cdd:cd07078 409 QSGIGREGGPYGLEEYTEPK 428
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
26-472 |
1.81e-159 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 459.20 E-value: 1.81e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEI 105
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 106 INAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASP 185
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 186 AELIRAFVDAGVPAGVVNLVYG-VPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDA 264
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 265 DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAV 344
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 345 SKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHA 424
Cdd:TIGR01780 321 EKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRIWR 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 674257992 425 LSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:TIGR01780 401 VAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
11-474 |
1.00e-144 |
|
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: 422.44 E-value: 1.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 11 INGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLM 90
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 91 TREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATG 170
Cdd:cd07088 82 VEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 171 CSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATM 250
Cdd:cd07088 162 NTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 251 ELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANE 330
Cdd:cd07088 242 ELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 331 RRIPAMEEMIQDAVSKGAVLKTGGKRI-GNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFG 409
Cdd:cd07088 322 AALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYG 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 674257992 410 LASYAFTGSVKTAHALSQRVEAGMLTVNHNGlaiPEVPFG---GIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07088 402 LTSYIYTENLNTAMRATNELEFGETYINREN---FEAMQGfhaGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
10-474 |
1.66e-143 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 420.08 E-value: 1.66e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWL 89
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 90 MTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVAT 169
Cdd:PRK11241 94 MTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 170 GCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRAT 249
Cdd:PRK11241 174 GCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 250 MELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLAN 329
Cdd:PRK11241 254 LELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLID 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 330 ERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFG 409
Cdd:PRK11241 334 EKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFG 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 674257992 410 LASYAFTGSVKTAHALSQRVEAGMLTVNhNGLAIPEV-PFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:PRK11241 414 LAAYFYARDLSRVFRVGEALEYGIVGIN-TGIISNEVaPFGGIKASGLGREGSKYGIEDYLEIKYM 478
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
26-472 |
1.79e-142 |
|
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: 416.18 E-value: 1.79e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFK--VWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM 103
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 104 EIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPA 183
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 184 SPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDD 263
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 264 ADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDA 343
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 344 VSKGAVLKTGGKRIG----NKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSV 419
Cdd:cd07114 321 REEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 674257992 420 KTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTK 453
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
8-472 |
1.87e-142 |
|
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: 417.00 E-value: 1.87e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKV--WRETSAFERSKIMRKAADLVRQRIDY 85
Cdd:cd07091 5 GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETgwWRKMDPRERGRLLNKLADLIERDRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 86 IAWLMTREQGKPLAQS-KMEIINAADTIDWFAEEARRTYGQVIPaRFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLS 164
Cdd:cd07091 85 LAALESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTIP-IDGNFLAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 165 AAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGK- 243
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAKs 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 244 HMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTT 323
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 324 MGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEA 403
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674257992 404 NRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07091 404 NDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVK 472
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
10-472 |
1.37e-138 |
|
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: 407.02 E-value: 1.37e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEWRDALSGKtiEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAW 88
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 89 LMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVA 168
Cdd:cd07097 82 LLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 169 TGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRA 248
Cdd:cd07097 162 YGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 249 TMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLA 328
Cdd:cd07097 242 QLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 329 NERRIPAMEEMIQDAVSKGAVLKTGGKRI--GNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRL 406
Cdd:cd07097 322 SERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDT 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674257992 407 PFGLASYAFTGSVKTAHALSQRVEAGMLTVN--HNGLAiPEVPFGGIKDSGYGT-EGGSEAVEAYLETR 472
Cdd:cd07097 402 EFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlpTAGVD-YHVPFGGRKGSSYGPrEQGEAALEFYTTIK 469
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
26-472 |
3.17e-136 |
|
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: 400.40 E-value: 3.17e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSK-ME 104
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLARtRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 105 IINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPAS 184
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 185 PAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDA 264
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 265 DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAV 344
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 345 SKGAVLKTGGKRIG----NKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVK 420
Cdd:cd07093 320 AEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 674257992 421 TAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07093 400 RAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELK 451
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
25-475 |
2.40e-135 |
|
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: 397.86 E-value: 2.40e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 25 EVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKME 104
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 105 IINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPAS 184
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 185 PAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDA 264
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 265 DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAV 344
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 345 SKGAVLKTGGKRignKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHA 424
Cdd:cd07150 322 AKGAKLLTGGKY---DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 674257992 425 LSQRVEAGMltVNHNGLAI---PEVPFGGIKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:cd07150 399 LAERLESGM--VHINDPTIldeAHVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
57-475 |
5.73e-135 |
|
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: 396.13 E-value: 5.73e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 57 FKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSN 136
Cdd:cd07104 13 QKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 137 LAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELI-RAFVDAGVPAGVVNLVYGVPSEISEY 215
Cdd:cd07104 93 MVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIaEIFEEAGLPKGVLNVVPGGGSEIGDA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 216 LIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQD 295
Cdd:cd07104 173 LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 296 SIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRignKGNFFEPTVLTDVPTS 375
Cdd:cd07104 253 SVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY---EGLFYQPTVLSDVTPD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 376 AKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGML-----TVNHNglaiPEVPFGG 450
Cdd:cd07104 330 MPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVhindqTVNDE----PHVPFGG 405
|
410 420
....*....|....*....|....*
gi 674257992 451 IKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:cd07104 406 VKASGGGRFGGPASLEEFTEWQWIT 430
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
55-459 |
7.81e-135 |
|
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: 395.68 E-value: 7.81e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 55 KGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGV 134
Cdd:cd07100 10 AAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLADEPIETDAGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 135 SNLAiKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYgVPSEISE 214
Cdd:cd07100 90 AYVR-YEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL-IDSDQVE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 215 YLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQ 294
Cdd:cd07100 168 AIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFIVH 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 295 DSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPT 374
Cdd:cd07100 248 EDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTVLTDVTP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 375 SAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDS 454
Cdd:cd07100 328 GMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPFGGVKRS 407
|
....*
gi 674257992 455 GYGTE 459
Cdd:cd07100 408 GYGRE 412
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
11-474 |
3.08e-134 |
|
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: 396.30 E-value: 3.08e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 11 INGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGF--KVWRETSAFERSKIMRKAADLVRQRIDYIAW 88
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFdsGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 89 LMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVA 168
Cdd:cd07119 82 LETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVP-PHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 169 TGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRA 248
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 249 TMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLA 328
Cdd:cd07119 241 ALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 329 NERRIPAMEEMIQDAVSKGAVLKTGGKRIGN----KGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEAN 404
Cdd:cd07119 321 SAEHREKVLSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLAN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 405 RLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07119 401 DTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
24-474 |
1.90e-133 |
|
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: 393.11 E-value: 1.90e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 24 IEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM 103
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 104 EIINAADTIDWFAEEARRTYGQVIP--ARFGGVSNLA--IKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPE 179
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPfdASPGGEGRIGftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 180 ETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGkhMKRATMELGGHAPVL 259
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 260 VFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEM 339
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 340 IQDAVSKGAVLKTGGKRIgnkGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSV 419
Cdd:cd07149 319 VEEAVEGGARLLTGGKRD---GAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDL 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 420 KTAHALSQRVEAGMLTVNHnglaIPEV-----PFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07149 396 QKALKAARELEVGGVMIND----SSTFrvdhmPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
9-474 |
3.69e-129 |
|
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: 382.62 E-value: 3.69e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 9 LLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAW 88
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 89 LMTREQGKPLAQSK--------MEIINAADTIDWFAEEARRTygqviparfggvSNLAIKFPVGPVAAFTPWNFPINQVV 160
Cdd:cd07138 81 AITLEMGAPITLARaaqvglgiGHLRAAADALKDFEFEERRG------------NSLVVREPIGVCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 161 RKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAAL 240
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 241 AGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDA 320
Cdd:cd07138 229 AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 321 DTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGG--KRIG-NKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLD 397
Cdd:cd07138 309 ATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgRPEGlERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDED 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 674257992 398 EALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAiPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07138 389 EAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINGAAFN-PGAPFGGYKQSGNGREWGRYGLEEFLEVKSI 464
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
24-475 |
8.56e-129 |
|
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: 381.31 E-value: 8.56e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 24 IEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM 103
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 104 EIINAADTIDWFAEEARRTYGQVIP--ARFGGVSNLAI--KFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPE 179
Cdd:cd07145 81 EVERTIRLFKLAAEEAKVLRGETIPvdAYEYNERRIAFtvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 180 ETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVL 259
Cdd:cd07145 161 NTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 260 VFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEM 339
Cdd:cd07145 241 VLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 340 IQDAVSKGAVLKTGGKRIGnkGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSV 419
Cdd:cd07145 321 VNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 674257992 420 KTAHALSQRVEAGMLTVNHNG-LAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:cd07145 399 NRALKVARELEAGGVVINDSTrFRWDNLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
9-474 |
2.14e-128 |
|
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: 380.77 E-value: 2.14e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 9 LLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGF--KVWRETSAFERSKIMRKAADLVRQRIDYI 86
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFdnGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 87 AWLMTREQGKPLAQSK-MEIINAADTIDWFAEEARR-TYGQVIPARFGGVSnLAIKFPVGPVAAFTPWNFPINQVVRKLS 164
Cdd:cd07139 81 ARLWTAENGMPISWSRrAQGPGPAALLRYYAALARDfPFEERRPGSGGGHV-LVRREPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 165 AAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKH 244
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 245 MKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTM 324
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 325 GPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIG--NKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEE 402
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674257992 403 ANRLPFGLASYAFTGSVKTAHALSQRVEAGmlTVNHNGLAI-PEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTG--TVGVNGFRLdFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
26-475 |
2.08e-126 |
|
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: 374.94 E-value: 2.08e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEI 105
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 106 INAAdtiDWFAEEARRTYGQ-VIPARFGGVSNLAIKfPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPAS 184
Cdd:cd07106 81 GGAV---AWLRYTASLDLPDeVIEDDDTRRVELRRK-PLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 185 PAELIRAFVDAgVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDA 264
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 265 DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAV 344
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 345 SKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHA 424
Cdd:cd07106 315 AKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 674257992 425 LSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:cd07106 395 VARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVIN 445
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
5-474 |
9.60e-126 |
|
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: 374.38 E-value: 9.60e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 5 PDI---KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFK---VWRETSAFERSKIMRKAADL 78
Cdd:cd07141 2 PEIkytKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKlgsPWRTMDASERGRLLNKLADL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 79 VRQRIDYIAWLMTREQGKPLA-QSKMEIINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPIN 157
Cdd:cd07141 82 IERDRAYLASLETLDNGKPFSkSYLVDLPGAIKVLRYYAGWADKIHGKTIPMD-GDFFTYTRHEPVGVCGQIIPWNFPLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 158 QVVRKLSAAVATGCSIIVKAPEETPASP---AELIRafvDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVG 234
Cdd:cd07141 161 MAAWKLAPALACGNTVVLKPAEQTPLTAlylASLIK---EAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 235 KHLAALAGK-HMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVK 313
Cdd:cd07141 238 KLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 314 VGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRF 393
Cdd:cd07141 318 VGNPFDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 394 STLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRF 473
Cdd:cd07141 398 KTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKT 477
|
.
gi 674257992 474 I 474
Cdd:cd07141 478 V 478
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-472 |
4.14e-125 |
|
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: 368.48 E-value: 4.14e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 55 KGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGV 134
Cdd:cd06534 5 AAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 135 SNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISE 214
Cdd:cd06534 85 EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 215 YLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQ 294
Cdd:cd06534 165 ALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVH 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 295 DSIADKFIDGIVkyaesvkvgngldadttmgplanerripameemiqdavskgavlktggkrignkgnffepTVLTDVPT 374
Cdd:cd06534 245 ESIYDEFVEKLV------------------------------------------------------------TVLVDVDP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 375 SAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN-HNGLAIPEVPFGGIKD 453
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINdSSIGVGPEAPFGGVKN 344
|
410
....*....|....*....
gi 674257992 454 SGYGTEGGSEAVEAYLETR 472
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTK 363
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
10-470 |
1.41e-124 |
|
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: 371.30 E-value: 1.41e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEWRDALSGKTIEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAW 88
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 89 LMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVA 168
Cdd:cd07131 82 LVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPALV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 169 TGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRA 248
Cdd:cd07131 162 CGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNKRV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 249 TMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLA 328
Cdd:cd07131 242 ALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 329 NERRIPAMEEMIQDAVSKGAVLKTGGKRI----GNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEAN 404
Cdd:cd07131 322 NEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIAN 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 674257992 405 RLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGL-AIPEVPFGGIKDSGYGT-EGGSEAVEAYLE 470
Cdd:cd07131 402 DTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGHrEAGTTALDAFTE 469
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
13-475 |
8.61e-124 |
|
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: 368.94 E-value: 8.61e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 13 GEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTR 92
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 93 EQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCS 172
Cdd:cd07151 81 ESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 173 IIVKAPEETPASPAELI-RAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATME 251
Cdd:cd07151 161 VVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 252 LGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANER 331
Cdd:cd07151 241 LGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 332 RIPAMEEMIQDAVSKGAVLKTGGKRignKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLA 411
Cdd:cd07151 321 QVDGLLDKIEQAVEEGATLLVGGEA---EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLS 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 674257992 412 SYAFTGSVKTAHALSQRVEAGMLTVNH---NGLaiPEVPFGGIKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:cd07151 398 GAVFTSDLERGVQFARRIDAGMTHINDqpvNDE--PHVPFGGEKNSGLGRFNGEWALEEFTTDKWIS 462
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
24-472 |
1.46e-123 |
|
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: 367.73 E-value: 1.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 24 IEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM 103
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 104 EIINAADTIDWFAEEARRTYGQVIP----ARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPE 179
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 180 ETPASPAELIRAFVDAGVPAGVVNlVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKhmKRATMELGGHAPVL 259
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFS-VLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 260 VFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEM 339
Cdd:cd07147 238 VDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 340 IQDAVSKGAVLKTGGKRignKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSV 419
Cdd:cd07147 318 VNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 674257992 420 KTAHALSQRVEAGMLTVNHnglaIPEV-----PFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07147 395 EKALRAWDELEVGGVVIND----VPTFrvdhmPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
24-474 |
2.06e-123 |
|
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: 367.53 E-value: 2.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 24 IEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM 103
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 104 EIINAADTIDWFAEEARRTYGQVIP----ARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPE 179
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEIPldatQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 180 ETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKhmKRATMELGGHAPVL 259
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 260 VFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEM 339
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 340 IQDAVSKGAVLKTGGKRignKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSV 419
Cdd:cd07094 319 VEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 674257992 420 KTAHALSQRVEAGMLTVN-HNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
26-474 |
7.45e-123 |
|
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: 365.99 E-value: 7.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSK-ME 104
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 105 IINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPAS 184
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEGEVIPVR-GPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 185 PAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDA 264
Cdd:cd07115 160 ALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 265 DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAV 344
Cdd:cd07115 240 DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 345 SKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHA 424
Cdd:cd07115 320 EEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 674257992 425 LSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07115 400 VAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
7-472 |
5.49e-122 |
|
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: 364.81 E-value: 5.49e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 7 IKLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFK-VWRETSAFERSKIMRKAADLVRQRIDY 85
Cdd:cd07144 8 TGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFEsWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 86 IAWLMTREQGKPLAQskmeiiNAADTID-------WFAEEARRTYGQVIPARFGGVSnLAIKFPVGPVAAFTPWNFPINQ 158
Cdd:cd07144 88 LAAIEALDSGKPYHS------NALGDLDeiiavirYYAGWADKIQGKTIPTSPNKLA-YTLHEPYGVCGQIIPWNYPLAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 159 VVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLA 238
Cdd:cd07144 161 AAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 239 ALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYA-ESVKVGNG 317
Cdd:cd07144 241 KAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 318 LDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGG---KRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFS 394
Cdd:cd07144 321 FDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFK 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 674257992 395 TLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07144 401 TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTK 478
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
26-475 |
2.02e-120 |
|
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: 360.01 E-value: 2.02e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFK-VWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKME 104
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFEsGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 105 IINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPAS 184
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 185 PAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDA 264
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 265 DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDaDTTMGPLANERRIPAMEEMIQDAV 344
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 345 SKGAVLKTGGKRIGN---KGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKT 421
Cdd:cd07109 319 ARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 674257992 422 AHALSQRVEAGMLTVNHNGLA--IpEVPFGGIKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:cd07109 399 ALRVARRLRAGQVFVNNYGAGggI-ELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
11-472 |
6.78e-119 |
|
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: 356.43 E-value: 6.78e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 11 INGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLM 90
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 91 TREQGKPLAQS-KMEIINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVAT 169
Cdd:TIGR01804 82 TLDTGKTLQETiVADMDSGADVFEFFAGLAPALNGEIIPLG-GPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 170 GCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRAT 249
Cdd:TIGR01804 161 GNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKHVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 250 MELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLAN 329
Cdd:TIGR01804 241 MELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPLIS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 330 ERRIPAMEEMIQDAVSKGAVLKTGGKRIGN----KGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANR 405
Cdd:TIGR01804 321 AAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARAND 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 674257992 406 LPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:TIGR01804 401 TEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
26-468 |
1.29e-118 |
|
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: 355.46 E-value: 1.29e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEI 105
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 106 INAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASP 185
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLP-GGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 186 AELIRAFVDAGVPAGVVNLVYGVpSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDAD 265
Cdd:cd07090 160 LLLAEILTEAGLPDGVFNVVQGG-GETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 266 LAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVS 345
Cdd:cd07090 239 LENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESAKQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 346 KGAVLKTGGKRIGNK-----GNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVK 420
Cdd:cd07090 319 EGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQ 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 674257992 421 TAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAY 468
Cdd:cd07090 399 RAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHY 446
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
21-474 |
2.43e-118 |
|
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: 354.99 E-value: 2.43e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 21 GKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFK--VWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPL 98
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFEsgVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 99 AQSKMEIIN-AADTIDWFAEEARRTYGQVIPARFGGVSnLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKA 177
Cdd:cd07112 81 SDALAVDVPsAANTFRWYAEAIDKVYGEVAPTGPDALA-LITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 178 PEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGK-HMKRATMELGGHA 256
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 257 PVLVFDDA-DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPA 335
Cdd:cd07112 240 PNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 336 MEEMIQDAVSKGAVLKTGGKR--IGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASY 413
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRvlTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674257992 414 AFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
26-472 |
2.49e-117 |
|
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: 351.63 E-value: 2.49e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSK-ME 104
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 105 IINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPAS 184
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 185 pAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDA 264
Cdd:cd07092 161 -TLLLAELAAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 265 DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAv 344
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 345 SKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHA 424
Cdd:cd07092 319 PAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMR 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 674257992 425 LSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07092 399 LSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIK 446
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
26-476 |
1.78e-116 |
|
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: 349.73 E-value: 1.78e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEI 105
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 106 INAADTIDWFAEEA---RRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETP 182
Cdd:cd07110 81 DDVAGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 183 ASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFD 262
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 263 DADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQD 342
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 343 AVSKGAVLKTGGKR--IGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVK 420
Cdd:cd07110 321 GKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 674257992 421 TAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFISQ 476
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQITR 456
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
55-475 |
2.76e-115 |
|
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: 346.10 E-value: 2.76e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 55 KGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGV 134
Cdd:cd07105 11 AAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 135 SNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPS---E 211
Cdd:cd07105 91 LAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPEdapE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 212 ISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRF 291
Cdd:cd07105 171 VVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 292 LIQDSIADKFIDGIVKYAESVKVGngldaDTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGK-RIGNKGNFFEPTVLT 370
Cdd:cd07105 251 IVHESIADEFVEKLKAAAEKLFAG-----PVVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLaDESPSGTSMPPTILD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 371 DVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMltVNHNGLAI---PEVP 447
Cdd:cd07105 326 NVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA--VHINGMTVhdePTLP 403
|
410 420
....*....|....*....|....*...
gi 674257992 448 FGGIKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:cd07105 404 HGGVKSSGYGRFNGKWGIDEFTETKWIT 431
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
6-474 |
4.44e-115 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 346.90 E-value: 4.44e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 6 DIKLLINGEWRDAlSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDY 85
Cdd:PRK13473 2 QTKLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 86 IAWLMTREQGKPLAQSKM-EIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLS 164
Cdd:PRK13473 81 FARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 165 AAVATGCSIIVKAPEETPASPAELIRAFVDAgVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKH 244
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 245 MKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTM 324
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 325 GPLANERRIPAMEEMIQDAVSKG-AVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEA 403
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674257992 404 NRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:PRK13473 400 NDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
60-474 |
6.07e-115 |
|
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: 345.86 E-value: 6.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 60 WRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQ----VIPARFGgvs 135
Cdd:cd07118 37 WPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADLWRYAASLARTLHGDsynnLGDDMLG--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 136 nLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEY 215
Cdd:cd07118 114 -LVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGATVGQA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 216 LIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQD 295
Cdd:cd07118 193 MTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 296 SIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRI-GNKGNFFEPTVLTDVPT 374
Cdd:cd07118 273 SIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLaSAAGLFYQPTIFTDVTP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 375 SAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDS 454
Cdd:cd07118 353 DMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPELPFGGFKQS 432
|
410 420
....*....|....*....|
gi 674257992 455 GYGTEGGSEAVEAYLETRFI 474
Cdd:cd07118 433 GIGRELGRYGVEEYTELKTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-472 |
1.52e-114 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 346.10 E-value: 1.52e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 1 MHSYPDIKLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVR 80
Cdd:PRK13252 1 MSRQPLQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 81 QRIDYIAWLMTREQGKPLAQ-SKMEIINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQV 159
Cdd:PRK13252 81 ERNDELAALETLDTGKPIQEtSVVDIVTGADVLEYYAGLAPALEGEQIPLR-GGSFVYTRREPLGVCAGIGAWNYPIQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 160 VRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAA 239
Cdd:PRK13252 160 CWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQG-DGRVGAWLTEHPDIAKVSFTGGVPTGKKVMA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 240 LAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLD 319
Cdd:PRK13252 239 AAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 320 ADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGN----KGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFST 395
Cdd:PRK13252 319 PATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDD 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 674257992 396 LDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:PRK13252 399 EDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIK 475
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
26-474 |
2.69e-114 |
|
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: 344.23 E-value: 2.69e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFK--VWReTSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKP--LAQS 101
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDtgDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 102 kMEIINAADTIDWFAEEARRTYGQVI----PARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKA 177
Cdd:cd07089 80 -MQVDGPIGHLRYFADLADSFPWEFDlpvpALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 178 PEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAP 257
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 258 VLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAME 337
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 338 EMIQDAVSKGAVLKTGGKRI--GNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAF 415
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 674257992 416 TGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07089 399 SADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
24-475 |
1.73e-113 |
|
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: 342.03 E-value: 1.73e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 24 IEVLDPATDETLGTIAhAEKADLDLALDAADKGFKvwRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM 103
Cdd:cd07146 1 LEVRNPYTGEVVGTVP-AGTEEALREALALAASYR--STLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 104 EIINAADTIDWFAEEARRTYGQVIP----ARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPE 179
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFScdltANGKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 180 ETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGkhMKRATMELGGHAPVL 259
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPLI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 260 VFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEM 339
Cdd:cd07146 236 VMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 340 IQDAVSKGAVLKTGGKRignKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSV 419
Cdd:cd07146 316 VEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDL 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 674257992 420 KTAHALSQRVEAGMLTVNHN-GLAIPEVPFGGIKDSGYGT-EGGSEAVEAYLETRFIS 475
Cdd:cd07146 393 DTIKRLVERLDVGTVNVNEVpGFRSELSPFGGVKDSGLGGkEGVREAMKEMTNVKTYS 450
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
10-470 |
1.83e-113 |
|
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: 343.01 E-value: 1.83e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEWRDAlSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWL 89
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 90 MTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVAT 169
Cdd:cd07086 81 VSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIALVC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 170 GCSIIVKAPEETPASP---AELI-RAFVDAGVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHM 245
Cdd:cd07086 161 GNTVVWKPSETTPLTAiavTKILaEVLEKNGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 246 KRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMG 325
Cdd:cd07086 240 GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 326 PLANERRIPAMEEMIQDAVSKGAVLKTGGKRI--GNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEA 403
Cdd:cd07086 320 PLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAIN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674257992 404 NRLPFGLASYAFTGSVKTA-HALSQR-VEAGMLTVNhnglaIP----EV--PFGGIKDSGYGTEGGSEAVEAYLE 470
Cdd:cd07086 400 NDVPQGLSSSIFTEDLREAfRWLGPKgSDCGIVNVN-----IPtsgaEIggAFGGEKETGGGRESGSDAWKQYMR 469
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
8-474 |
9.88e-112 |
|
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: 338.39 E-value: 9.88e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDAlSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRET-SAFERSKIMRKAADLVRQRIDYI 86
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 87 AWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPA-RFGGVSN-LAI--KFPVGPVAAFTPWNFPINQVVRK 162
Cdd:cd07082 82 ANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGdWFPGTKGkIAQvrREPLGVVLAIGPFNYPLNLTVSK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 163 LSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAG 242
Cdd:cd07082 162 LIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 243 khMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADT 322
Cdd:cd07082 242 --MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 323 TMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGnkGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEE 402
Cdd:cd07082 320 DITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIEL 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674257992 403 ANRLPFGLASYAFTGSVKTAHALSQRVEAGmlTVNHNGLAI--PEV-PFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07082 398 ANKSNYGLQASIFTKDINKARKLADALEVG--TVNINSKCQrgPDHfPFLGRKDSGIGTQGIGDALRSMTRRKGI 470
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
9-472 |
3.56e-111 |
|
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: 337.19 E-value: 3.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 9 LLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKV-W-RETSAFERSKIMRKAADLVRQRIDYI 86
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETdWgLKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 87 AWLMTREQGKP-LAQSKMEIINAADTIDWFAEEARRTYGQVI---PARFggvsNLAIKFPVGPVAAFTPWNFPINQVVRK 162
Cdd:cd07143 89 ASIEALDNGKTfGTAKRVDVQASADTFRYYGGWADKIHGQVIetdIKKL----TYTRHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 163 LSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVG-KHLAALA 241
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGrKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 242 GKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDAD 321
Cdd:cd07143 245 KSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 322 TTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALE 401
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIK 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674257992 402 EANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07143 405 RANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
8-472 |
2.33e-110 |
|
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: 334.85 E-value: 2.33e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKV--WRETSAFERSKIMRKAADLVRQRIDY 85
Cdd:cd07142 5 KLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEgpWPRMTGYERSRILLRFADLLEKHADE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 86 IAWLMTREQGKPLAQSKM-EIINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLS 164
Cdd:cd07142 85 LAALETWDNGKPYEQARYaEVPLAARLFRYYAGWADKIHGMTLPAD-GPHHVYTLHEPIGVVGQIIPWNFPLLMFAWKVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 165 AAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGK- 243
Cdd:cd07142 164 PALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAKs 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 244 HMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTT 323
Cdd:cd07142 244 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 324 MGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEA 403
Cdd:cd07142 324 QGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674257992 404 NRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07142 404 NNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVK 472
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
27-476 |
3.19e-110 |
|
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: 333.93 E-value: 3.19e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 27 LDPATDETLGTIAHAEKADLDLALDAADKGFK--VWReTSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKME 104
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDetDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 105 IINAADTIDWFAEEARRTYGQVIPARFGGVSnLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPAS 184
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIEPEPGSFS-LVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 185 PAELIRAFVDA-GVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDD 263
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 264 ADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDA 343
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 344 VSKGA-VLKTGGKRIG--NKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVK 420
Cdd:cd07120 320 IAAGAeVVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 674257992 421 TAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFISQ 476
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
5-472 |
1.56e-108 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 331.01 E-value: 1.56e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 5 PDI---KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFK--VWRETSAFERSKIMRKAADLV 79
Cdd:PLN02766 16 PEIkftKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 80 RQRIDYIAWLMTREQGKPLAQSK-MEIINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQ 158
Cdd:PLN02766 96 EEHIEELAALDTIDAGKLFALGKaVDIPAAAGLLRYYAGAADKIHGETLKMS-RQLQGYTLKEPIGVVGHIIPWNFPSTM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 159 VVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVG-KHL 237
Cdd:PLN02766 175 FFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGrKIM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 238 AALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNG 317
Cdd:PLN02766 255 QAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 318 LDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLD 397
Cdd:PLN02766 335 FDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVE 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674257992 398 EALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:PLN02766 415 EAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVK 489
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-474 |
3.18e-107 |
|
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: 326.99 E-value: 3.18e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIA 87
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 88 WLMTREQGKPLAQSKmeiinAAD---TIDWFaeearRTYGQVIPARFGGVSN-----LAIKF--PVGPVAAFTPWNFPIN 157
Cdd:cd07559 82 VAETLDNGKPIRETL-----AADiplAIDHF-----RYFAGVIRAQEGSLSEidedtLSYHFhePLGVVGQIIPWNFPLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 158 QVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAgVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHL 237
Cdd:cd07559 152 MAAWKLAPALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 238 AALAGKHMKRATMELGGHAPVLVFDDADLA------KAIEVSATAKFrNAGQVCVAPTRFLIQDSIADKFIDGIVKYAES 311
Cdd:cd07559 231 MQYAAENLIPVTLELGGKSPNIFFDDAMDAdddfddKAEEGQLGFAF-NQGEVCTCPSRALVQESIYDEFIERAVERFEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 312 VKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRI----GNKGNFFEPTVLTDVPTSAKMMNEEPFGPV 387
Cdd:cd07559 310 IKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 388 AIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN--HnglAIPE-VPFGGIKDSGYGTEGGSEA 464
Cdd:cd07559 390 LAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNcyH---QYPAhAPFGGYKKSGIGRETHKMM 466
|
490
....*....|
gi 674257992 465 VEAYLETRFI 474
Cdd:cd07559 467 LDHYQQTKNI 476
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-474 |
4.97e-106 |
|
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: 323.64 E-value: 4.97e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIA 87
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 88 WLMTREQGKPLAQSK-MEIINAADTIDWFAEEARRTYGQVIPARFGGVSnLAIKFPVGPVAAFTPWNFPINQVVRKLSAA 166
Cdd:cd07117 82 MVETLDNGKPIRETRaVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLS-IVLREPIGVVGQIIPWNFPFLMAAWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 167 VATGCSIIVKAPEETPASPAELIRAFVDAgVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMK 246
Cdd:cd07117 161 LAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 247 RATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGP 326
Cdd:cd07117 240 PATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 327 LANERRIPAMEEMIQDAVSKGAVLKTGGKRIG----NKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEE 402
Cdd:cd07117 320 QVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDM 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674257992 403 ANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN-HNglAIPE-VPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07117 400 ANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNtYN--QIPAgAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
5-475 |
5.72e-106 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 324.38 E-value: 5.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 5 PDIKLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGF-----KVWRETSAFERSKIMRKAADLV 79
Cdd:PLN02467 6 PRRQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnkgKDWARTTGAVRAKYLRAIAAKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 80 RQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYG-QVIPARFGGVS--NLAIKFPVGPVAAFTPWNFPI 156
Cdd:PLN02467 86 TERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAkQKAPVSLPMETfkGYVLKEPLGVVGLITPWNYPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 157 NQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKH 236
Cdd:PLN02467 166 LMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 237 LAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGN 316
Cdd:PLN02467 246 IMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 317 GLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIG--NKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFS 394
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 395 TLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLE---- 470
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSvkqv 485
|
....*
gi 674257992 471 TRFIS 475
Cdd:PLN02467 486 TKYIS 490
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
4-477 |
2.74e-105 |
|
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: 323.02 E-value: 2.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 4 YPdikLLINGEWRDalSGKTIEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQR 82
Cdd:cd07124 33 YP---LVIGGKEVR--TEEKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 83 IDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPaRFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRK 162
Cdd:cd07124 108 RFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVE-MVPGEDNRYVYRPLGVGAVISPWNFPLAILAGM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 163 LSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAG 242
Cdd:cd07124 187 TTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 243 K------HMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGN 316
Cdd:cd07124 267 KvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 317 GLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLkTGGKRIGN--KGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFS 394
Cdd:cd07124 347 PEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLL-LGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 395 TLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGL-AIPEV-PFGGIKDSGYGTE-GGSEAVEAYLET 471
Cdd:cd07124 426 DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITgALVGRqPFGGFKMSGTGSKaGGPDYLLQFMQP 505
|
....*.
gi 674257992 472 RFISQM 477
Cdd:cd07124 506 KTVTEN 511
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
27-474 |
1.93e-104 |
|
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: 318.78 E-value: 1.93e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 27 LDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEII 106
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 107 NAADTIDWFAEEARRTYGQviPARFGGVSNLAIKF-----PVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEET 181
Cdd:cd07099 81 LALEAIDWAARNAPRVLAP--RKVPTGLLMPNKKAtveyrPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 182 PASPAELIRAFVDAGVPAGVVNLVYGVpSEISEYLIPHpVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVF 261
Cdd:cd07099 159 PLVGELLAEAWAAAGPPQGVLQVVTGD-GATGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 262 DDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQ 341
Cdd:cd07099 237 ADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 342 DAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKT 421
Cdd:cd07099 317 DAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 674257992 422 AHALSQRVEAGMLTVNHNGL--AIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07099 397 AEAIARRLEAGAVSINDVLLtaGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
9-472 |
1.77e-103 |
|
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: 317.08 E-value: 1.77e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 9 LLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKV-WRETSAFERSKIMRKAADLVRQRIDYIA 87
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFVSaWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 88 WLMTREQGKPLAQSKM-EIINAADTIDWFAEEARRTYGQV----IPARFGG-VSNLAIKFPVGPVAAFTPWNFPINQVVR 161
Cdd:cd07113 82 QLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETlapsIPSMQGErYTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 162 KLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAALA 241
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNG-KGAVGAQLISHPDVAKVSFTGSVATGKKIGRQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 242 GKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDAD 321
Cdd:cd07113 241 ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 322 TTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALE 401
Cdd:cd07113 321 VMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQ 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674257992 402 EANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:cd07113 401 LINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELK 471
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
7-476 |
5.62e-101 |
|
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: 310.60 E-value: 5.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 7 IKLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYI 86
Cdd:cd07085 1 LKLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 87 AWLMTREQGKPLAQSKMEIINAADTIDwFAEEARRTY-GQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSA 165
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVE-FACSIPHLLkGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 166 AVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHM 245
Cdd:cd07085 160 AIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 246 KRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMG 325
Cdd:cd07085 239 KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 326 PLANERRIPAMEEMIQDAVSKGAVLKTGGKRI----GNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALE 401
Cdd:cd07085 319 PVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 402 EANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNhngLAIPeVP-----FGGIKDSGYGTEG--GSEAVEAYLETRFI 474
Cdd:cd07085 399 IINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN---VPIP-VPlaffsFGGWKGSFFGDLHfyGKDGVRFYTQTKTV 474
|
..
gi 674257992 475 SQ 476
Cdd:cd07085 475 TS 476
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
72-474 |
9.29e-99 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 302.81 E-value: 9.29e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 72 MRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTP 151
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 152 WNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGST 231
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 232 PVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAES 311
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 312 VKVGNGLDADT-TMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIV 390
Cdd:PRK10090 241 VQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVLPV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 391 NRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLE 470
Cdd:PRK10090 321 VAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEYLQ 400
|
....
gi 674257992 471 TRFI 474
Cdd:PRK10090 401 TQVV 404
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
9-470 |
2.28e-98 |
|
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: 304.32 E-value: 2.28e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 9 LLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAW 88
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 89 LMTREQGKPLAQSK-MEIINAADTIDWFAEEArrtygQVIPARFGGVSnlaikfPVGPVAAFTPWNFPINQVVRKLSAAV 167
Cdd:cd07111 104 LESLDNGKPIRESRdCDIPLVARHFYHHAGWA-----QLLDTELAGWK------PVGVVGQIVPWNFPLLMLAWKICPAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 168 ATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLA-ALAGKhMK 246
Cdd:cd07111 173 AMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRrATAGT-GK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 247 RATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGP 326
Cdd:cd07111 251 KLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 327 LANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRL 406
Cdd:cd07111 331 IVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNT 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674257992 407 PFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLE 470
Cdd:cd07111 411 PYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLR 474
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
26-470 |
4.77e-97 |
|
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: 300.05 E-value: 4.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPL-AQSKME 104
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 105 IINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPAS 184
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFG-PDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 185 P---AELIRAFVdagvPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVF 261
Cdd:cd07108 160 VlllAEILAQVL----PAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 262 DDADLAKAIE-VSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMI 340
Cdd:cd07108 236 PDADLDDAVDgAIAGMRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 341 QDAVS-KGAVLKTGGKR----IGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAF 415
Cdd:cd07108 316 DLGLStSGATVLRGGPLpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 674257992 416 TGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGgseAVEAYLE 470
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREA---SLEGMLE 447
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
24-459 |
5.23e-97 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 299.73 E-value: 5.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 24 IEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM 103
Cdd:PRK09406 3 IATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 104 EIINAADTIDWFAEEARRTYGQViPARFG--GVSNLAIKF-PVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEE 180
Cdd:PRK09406 83 EALKCAKGFRYYAEHAEALLADE-PADAAavGASRAYVRYqPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 181 TPASPAELIRAFVDAGVPAGVVNLVYgVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLV 260
Cdd:PRK09406 162 VPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 261 FDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMI 340
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 341 QDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVK 420
Cdd:PRK09406 321 DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 674257992 421 TAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTE 459
Cdd:PRK09406 401 EQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRE 439
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
26-474 |
2.35e-96 |
|
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: 298.13 E-value: 2.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 26 VLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEI 105
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 106 INAADTIDWFAEEARRTYGQVIPARFGGVsNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASP 185
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 186 ---AELIRAFVdagvPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFD 262
Cdd:cd07107 160 lrlAELAREVL----PPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 263 DADLAKAIEVSATA-KFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQ 341
Cdd:cd07107 236 DADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYID 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 342 DAVSKGAVLKTGGKR----IGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTG 417
Cdd:cd07107 316 SAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTN 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 674257992 418 SVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:cd07107 396 DISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
8-474 |
4.05e-96 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 298.73 E-value: 4.05e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFK--VWRETSAFERSKIMRKAADLVRQRIDY 85
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFErgDWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 86 IAWLMTREQGKPLAQS-KMEIINAADTIDWFAEEARRTYGQVIPArfgGVSNLA--IKFPVGPVAAFTPWNFPINQVVRK 162
Cdd:PRK09847 101 LALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATT---SSHELAmiVREPVGVIAAIVPWNFPLLLTCWK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 163 LSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAG 242
Cdd:PRK09847 178 LGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 243 K-HMKRATMELGGHAPVLVFDDA-DLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDA 320
Cdd:PRK09847 258 DsNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 321 DTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGgkRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEAL 400
Cdd:PRK09847 338 ATTMGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQAL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674257992 401 EEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:PRK09847 416 QLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
8-475 |
5.82e-96 |
|
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: 298.25 E-value: 5.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKV--WRETSAFERSKIMRKAADLVRQRIDY 85
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 86 IAWLMTREQGK--PLAQsKMEIINAADTIDWFAEEARRTYGQVIP---ARFGGVSNLAIKFPVGPVAAFTPWNFPINQVV 160
Cdd:cd07140 87 LATIESLDSGAvyTLAL-KTHVGMSIQTFRYFAGWCDKIQGKTIPinqARPNRNLTLTKREPIGVCGIVIPWNYPLMMLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 161 RKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKH-LAA 239
Cdd:cd07140 166 WKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHiMKS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 240 LAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLD 319
Cdd:cd07140 246 CAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 320 ADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRF--STLD 397
Cdd:cd07140 326 RSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFddGDVD 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 674257992 398 EALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFIS 475
Cdd:cd07140 406 GVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVT 483
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
8-472 |
6.10e-96 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 299.80 E-value: 6.10e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFK--VWRETSAFERSKIMRKAADLVRQRIDY 85
Cdd:PLN02466 59 QLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWPKMTAYERSRILLRFADLLEKHNDE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 86 IAWLMTREQGKPLAQS-KMEIINAADTIDWFAEEARRTYGQVIPARfGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLS 164
Cdd:PLN02466 139 LAALETWDNGKPYEQSaKAELPMFARLFRYYAGWADKIHGLTVPAD-GPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 165 AAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGK- 243
Cdd:PLN02466 218 PALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKs 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 244 HMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTT 323
Cdd:PLN02466 298 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 324 MGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEA 403
Cdd:PLN02466 378 QGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRA 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674257992 404 NRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETR 472
Cdd:PLN02466 458 NNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
60-475 |
2.52e-94 |
|
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: 292.66 E-value: 2.52e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 60 WRETSAFERSKIMRKAADLVRQRIDYIA-WLMtREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSnLA 138
Cdd:cd07152 29 WAATPPRERAAVLRRAADLLEEHADEIAdWIV-RESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLS-LA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 139 IKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELI-RAFVDAGVPAGVVNLVYGVPsEISEYLI 217
Cdd:cd07152 107 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIaRLFEEAGLPAGVLHVLPGGA-DAGEALV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 218 PHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSI 297
Cdd:cd07152 186 EDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 298 ADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRignKGNFFEPTVLTDVPTSAK 377
Cdd:cd07152 266 ADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY---DGLFYRPTVLSGVKPGMP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 378 MMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGML-----TVNHNglaiPEVPFGGIK 452
Cdd:cd07152 343 AFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLhindqTVNDE----PHNPFGGMG 418
|
410 420
....*....|....*....|....
gi 674257992 453 DSGYGTE-GGSEAVEAYLETRFIS 475
Cdd:cd07152 419 ASGNGSRfGGPANWEEFTQWQWVT 442
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-463 |
1.14e-90 |
|
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: 283.81 E-value: 1.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 28 DPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM-EII 106
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLgEIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 107 NAADTIDWFAEEARRTygqVIPARFGGVSNLAIK------FPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEE 180
Cdd:cd07098 82 VTCEKIRWTLKHGEKA---LRPESRPGGLLMFYKrarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 181 TPASPA---ELIR-AFVDAGVPAGVVNLVYGVPsEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHA 256
Cdd:cd07098 159 VAWSSGfflSIIReCLAACGHDPDLVQLVTCLP-ETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 257 PVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAM 336
Cdd:cd07098 238 PAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 337 EEMIQDAVSKGAVLKTGGKRIGN----KGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLAS 412
Cdd:cd07098 318 EELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 674257992 413 YAFTGSVKTAHALSQRVEAGMLTVNHNGLA--IPEVPFGGIKDSGYGTEGGSE 463
Cdd:cd07098 398 SVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEE 450
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
3-477 |
1.36e-90 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 285.22 E-value: 1.36e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 3 SYPdikLLINGEWRDalSGKTIEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQ 81
Cdd:TIGR01237 32 TYP---LVINGERVE--TENKIVSINPCdKSEVVGTVSKASQEHAEHALQAAAKAFEAWKKTDPEERAAILFKAAAIVRR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 82 RIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVR 161
Cdd:TIGR01237 107 RRHEFSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 162 KLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALA 241
Cdd:TIGR01237 187 MTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 242 GK------HMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVG 315
Cdd:TIGR01237 267 AKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 316 NGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLkTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFST 395
Cdd:TIGR01237 347 PPDSADVYVGPVIDQKSFNKIMEYIEIGKAEGRLV-SGGCGDDSKGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 396 LDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHN--GLAIPEVPFGGIKDSGYGTE-GGSEAVEAYLETR 472
Cdd:TIGR01237 426 FDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNitGAIVGYQPFGGFKMSGTDSKaGGPDYLALFMQAK 505
|
....*
gi 674257992 473 FISQM 477
Cdd:TIGR01237 506 TVTEM 510
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
20-477 |
1.81e-89 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 282.54 E-value: 1.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 20 SGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLA 99
Cdd:PRK09407 30 AGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 100 QSKMEIINAADTIDWFAEEARRTYGqviPARFGGVSNLAIK-----FPVGPVAAFTPWNFPINQVVRKLSAAVATGCSII 174
Cdd:PRK09407 110 HAFEEVLDVALTARYYARRAPKLLA---PRRRAGALPVLTKttelrQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 175 VKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHpvIRKISFTGSTPVGKHLAALAGKHMKRATMELGG 254
Cdd:PRK09407 187 LKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 255 HAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIP 334
Cdd:PRK09407 265 KNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 335 AMEEMIQDAVSKGAVLKTGGKRIGNKGN-FFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASY 413
Cdd:PRK09407 345 TVSAHVDDAVAKGATVLAGGKARPDLGPlFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNAS 424
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674257992 414 AFTGSVKTAHALSQRVEAGmlTVNHN-GLAIP----EVPFGGIKDSGYGTEGGSEAVEAYLETRFISQM 477
Cdd:PRK09407 425 VWTGDTARGRAIAARIRAG--TVNVNeGYAAAwgsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTIATQ 491
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
28-476 |
3.18e-89 |
|
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: 279.58 E-value: 3.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 28 DPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIIN 107
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 108 AADTIDWFAEEARRTYGqviPARFGGV-----SNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETP 182
Cdd:cd07101 82 VAIVARYYARRAERLLK---PRRRRGAipvltRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 183 ASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHpvIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFD 262
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 263 DADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQD 342
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 343 AVSKGAVLKTGGKRIGNKGN-FFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKT 421
Cdd:cd07101 317 AVAKGATVLAGGRARPDLGPyFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 674257992 422 AHALSQRVEAGMLTVNhNGLAIP----EVPFGGIKDSGYGTEGGSEAVEAYLETRFISQ 476
Cdd:cd07101 397 GRRIAARLRAGTVNVN-EGYAAAwasiDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
65-460 |
1.24e-87 |
|
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: 275.45 E-value: 1.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 65 AFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKF--- 141
Cdd:cd07148 43 AHERIAILERLADLMEERADELALLIAREGGKPLVDAKVEVTRAIDGVELAADELGQLGGREIPMGLTPASAGRIAFttr 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 142 -PVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYgVPSEISEYLIPHP 220
Cdd:cd07148 123 ePIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 221 VIRKISFTGSTPVGKHL-AALAGKhmKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIAD 299
Cdd:cd07148 202 RVAFFSFIGSARVGWMLrSKLAPG--TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIAD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 300 KFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNkgNFFEPTVLTDVPTSAKMM 379
Cdd:cd07148 280 DFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSD--TTYAPTVLLDPPRDAKVS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 380 NEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN-HNGLAIPEVPFGGIKDSGYGT 458
Cdd:cd07148 358 TQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNdHTAFRVDWMPFAGRRQSGYGT 437
|
..
gi 674257992 459 EG 460
Cdd:cd07148 438 GG 439
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-477 |
1.36e-86 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 274.89 E-value: 1.36e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 2 HSYPdikLLINGEWRDalSGKTIEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVR 80
Cdd:PRK03137 35 QDYP---LIIGGERIT--TEDKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 81 QR-IDYIAWlMTREQGKPLAQSKMEIINAADTIDWFAEEARRtYGQVIP-ARFGGVSNLAIKFPVGPVAAFTPWNFPINQ 158
Cdd:PRK03137 110 RRkHEFSAW-LVKEAGKPWAEADADTAEAIDFLEYYARQMLK-LADGKPvESRPGEHNRYFYIPLGVGVVISPWNFPFAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 159 VVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLA 238
Cdd:PRK03137 188 MAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 239 ALAGK------HMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESV 312
Cdd:PRK03137 268 ERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKEL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 313 KVGNGLDADtTMGPLANErripAMEEMIQDAVSKG---AVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAI 389
Cdd:PRK03137 348 TVGNPEDNA-YMGPVINQ----ASFDKIMSYIEIGkeeGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 390 VNRFSTLDEALEEANRLPFGLasyafTGSVKT---AHALSQRVE--AGMLTVNHN--GLAIPEVPFGGIKDSGYGTE-GG 461
Cdd:PRK03137 423 FIKAKDFDHALEIANNTEYGL-----TGAVISnnrEHLEKARREfhVGNLYFNRGctGAIVGYHPFGGFNMSGTDSKaGG 497
|
490
....*....|....*.
gi 674257992 462 SEAVEAYLETRFISQM 477
Cdd:PRK03137 498 PDYLLLFLQAKTVSEM 513
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
27-459 |
1.99e-84 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 267.50 E-value: 1.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 27 LDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEII 106
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 107 NAADTIDWFAEEArrtygqviPARFGGVSNLA------IKF-PVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVK-AP 178
Cdd:PRK13968 92 KSANLCDWYAEHG--------PAMLKAEPTLVenqqavIEYrPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKhAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 179 EETPAspAELI-RAFVDAGVPAGVVNLVYGVPSEISEyLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAP 257
Cdd:PRK13968 164 NVMGC--AQLIaQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 258 VLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAME 337
Cdd:PRK13968 241 FIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 338 EMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTG 417
Cdd:PRK13968 321 HQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTT 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 674257992 418 SVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTE 459
Cdd:PRK13968 401 DETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRE 442
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
55-467 |
1.27e-83 |
|
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: 265.26 E-value: 1.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 55 KGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGV 134
Cdd:cd07102 29 AAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIRGMLERARYMISIAEEALADIRVPEKDGF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 135 SNLAIKFPVGPVAAFTPWNFP----INQVVrklsAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGvPS 210
Cdd:cd07102 109 ERYIRREPLGVVLIIAPWNYPyltaVNAVI----PALLAGNAVILKHSPQTPLCGERFAAAFAEAGLPEGVFQVLHL-SH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 211 EISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTR 290
Cdd:cd07102 184 ETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAFFNSGQSCCSIER 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 291 FLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGN---KGNFFEPT 367
Cdd:cd07102 264 IYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPEdkaGGAYLAPT 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 368 VLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVP 447
Cdd:cd07102 344 VLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVFMNRCDYLDPALA 423
|
410 420
....*....|....*....|
gi 674257992 448 FGGIKDSGYGTEGGSEAVEA 467
Cdd:cd07102 424 WTGVKDSGRGVTLSRLGYDQ 443
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
11-472 |
4.23e-76 |
|
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: 246.59 E-value: 4.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 11 INGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLM 90
Cdd:cd07116 5 IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 91 TREQGKPLAQSKmeiinAAD---TIDWFaeearRTYGQVIPARFGGVSNL-----AIKF--PVGPVAAFTPWNFPINQVV 160
Cdd:cd07116 85 TWDNGKPVRETL-----AADiplAIDHF-----RYFAGCIRAQEGSISEIdentvAYHFhePLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 161 RKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAgVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAAL 240
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 241 AGKHMKRATMELGGHAPVLVF------DDADLAKAIEVSATAKFrNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKV 314
Cdd:cd07116 234 ASENIIPVTLELGGKSPNIFFadvmdaDDAFFDKALEGFVMFAL-NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 315 GNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKR----IGNKGNFFEPTVLTDvPTSAKMMNEEPFGPVAIV 390
Cdd:cd07116 313 GNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelgGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 391 NRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLE 470
Cdd:cd07116 392 TTFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQ 471
|
..
gi 674257992 471 TR 472
Cdd:cd07116 472 TK 473
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
12-468 |
6.41e-75 |
|
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: 243.27 E-value: 6.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 12 NGEWRDalSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMT 91
Cdd:cd07130 4 DGEWGG--GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 92 REQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPInqVVRKLSAAVATGC 171
Cdd:cd07130 82 LEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPV--AVWGWNAAIALVC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 172 --SIIVKAPEETP----ASPAELIRAFVDAGVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHM 245
Cdd:cd07130 160 gnVVVWKPSPTTPltaiAVTKIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 246 KRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMG 325
Cdd:cd07130 239 GRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 326 PLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLTdVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANR 405
Cdd:cd07130 319 PLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674257992 406 LPFGLASYAFTGSVKTA-HALSQR-VEAGMLTVNhnglaIP----EV--PFGGIKDSGYGTEGGSEAVEAY 468
Cdd:cd07130 398 VPQGLSSSIFTTDLRNAfRWLGPKgSDCGIVNVN-----IGtsgaEIggAFGGEKETGGGRESGSDAWKQY 463
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
8-460 |
1.29e-71 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 235.04 E-value: 1.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIA 87
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 88 WLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQ---VIPARFGGVSN----LAIKFPVGPVAAFTPWNFPINQVV 160
Cdd:PLN00412 97 ECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkfLVSDSFPGNERnkycLTSKIPLGVVLAIPPFNYPVNLAV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 161 RKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTpVGKHLAAL 240
Cdd:PLN00412 177 SKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGGD-TGIAISKK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 241 AGkhMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDa 320
Cdd:PLN00412 256 AG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPED- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 321 DTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRignKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEAL 400
Cdd:PLN00412 333 DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR---EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGI 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674257992 401 EEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPE-VPFGGIKDSGYGTEG 460
Cdd:PLN00412 410 HHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIGSQG 470
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
10-461 |
2.22e-70 |
|
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: 232.47 E-value: 2.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEwrDALSGKTIEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAW 88
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 89 LMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVI-PARFGGVSNLAIKfPVGPVAAFTPWNFPINQVVRKLSAAV 167
Cdd:cd07125 114 LAAAEAGKTLADADAEVREAIDFCRYYAAQARELFSDPElPGPTGELNGLELH-GRGVFVCISPWNFPLAIFTGQIAAAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 168 ATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLA-ALAGKHMK 246
Cdd:cd07125 193 AAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINrALAERDGP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 247 RATM--ELGGHAPVLVFDDADLAKAIE---VSAtakFRNAGQVCVApTRFLI-QDSIADKFIDGIVKYAESVKVGNGLDA 320
Cdd:cd07125 273 ILPLiaETGGKNAMIVDSTALPEQAVKdvvQSA---FGSAGQRCSA-LRLLYlQEEIAERFIEMLKGAMASLKVGDPWDL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 321 DTTMGPLANERRIPAMEEMIQDAVSKGAVLKTgGKRIGNKGNFFEPTVLTDVptSAKMMNEEPFGPVAIVNRF--STLDE 398
Cdd:cd07125 349 STDVGPLIDKPAGKLLRAHTELMRGEAWLIAP-APLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFkaEDLDE 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674257992 399 ALEEANRLPFGLasyafTGSV-----KTAHALSQRVEAGMLTVNHN--GlAIPEV-PFGGIKDSGYGTEGG 461
Cdd:cd07125 426 AIEDINATGYGL-----TLGIhsrdeREIEYWRERVEAGNLYINRNitG-AIVGRqPFGGWGLSGTGPKAG 490
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
7-475 |
2.58e-70 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 231.31 E-value: 2.58e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 7 IKLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYI 86
Cdd:TIGR01722 1 VNHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETFLTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 87 AWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAA 166
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 167 VATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMK 246
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 247 RATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSiADKFIDGIVKYAESVKVGNGLDADTTMGP 326
Cdd:TIGR01722 240 RVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGA-ADEWVPEIRERAEKIRIGPGDDPGAEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 327 LANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKG----NFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEE 402
Cdd:TIGR01722 319 LITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGyeegNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 403 ANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNhngLAIPeVP-----FGGIKDSGYGTEG--GSEAVEAYLETRFIS 475
Cdd:TIGR01722 399 INASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN---VPIP-VPlpyfsFTGWKDSFFGDHHiyGKQGTHFYTRGKTVT 474
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
1-461 |
1.46e-67 |
|
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: 224.77 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 1 MHSYPdikLLINGEWRDALSGKTIevLDP-ATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLV 79
Cdd:cd07083 16 GRAYP---LVIGGEWVDTKERMVS--VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 80 RQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARR-TYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQ 158
Cdd:cd07083 91 RRRRRELIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRlRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 159 VVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLA 238
Cdd:cd07083 171 FTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 239 ALAGKH------MKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESV 312
Cdd:cd07083 251 EAAARLapgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 313 KVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKtGGKRIGNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNR 392
Cdd:cd07083 331 SVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVL-GGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIR 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674257992 393 F--STLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHN--GLAIPEVPFGGIKDSGYGTEGG 461
Cdd:cd07083 410 YkdDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKitGALVGVQPFGGFKLSGTNAKTG 482
|
|
| aldehy_Rv0768 |
TIGR04284 |
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde ... |
8-475 |
8.18e-67 |
|
aldehyde dehydrogenase, Rv0768 family; This family describes a branch of the aldehyde dehydrogenase (NAD) family (see pfam00171) that includes Rv0768 from Mycobacterium tuberculosis. All members of this family belong to species predicted to synthesize mycofactocin, suggesting that this enzyme or another upstream or downstream in the same pathway might be mycofactocin-dependent. However, the taxonomic range of this family is not nearly broad enough to make that relationship conclusive. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 275104 Cd Length: 480 Bit Score: 221.95 E-value: 8.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 8 KLLINGEWRDALSGkTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKV--WRETSAFeRSKIMRKAADLVRQRIDY 85
Cdd:TIGR04284 2 RLLIDGKLVAGSAG-TFPTVNPATEEVLGVAADATAADMDAAIAAARRAFDEtdWSRDTAL-RVRCLRQLRDALRAHVEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 86 IAWLMTREQGKP-LAQSKMEIINAADTIDWFAEEA-----RRTYGQVIPArfgGVSN--LAIKFPVGPVAAFTPWNFPIN 157
Cdd:TIGR04284 80 LRELTIAEVGAPrMLTAGAQLEGPVDDLGFAADLAesyawTTDLGVASPM---GIPTrrTLRREAVGVVGAITPWNFPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 158 QVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVD-AGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKH 236
Cdd:TIGR04284 157 INLAKLGPALAAGNTVVLKPAPDTPWCAAVLGELIAEhTDFPPGVVNIVTSSDHRLGALLAKDPRVDMVSFTGSTATGRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 237 LAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGN 316
Cdd:TIGR04284 237 VMADAAATLKKVFLELGGKSAFIVLDDADLAAACSMAAFTVCMHAGQGCAITTRLVVPRARYDEAVAAAAATMGSIKPGD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 317 GLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNK--GNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFS 394
Cdd:TIGR04284 317 PADPGTVCGPVISARQRDRVQSYLDLAVAEGGRFACGGGRPADRdrGFFVEPTVIAGLDNNARVAREEIFGPVLTVIAHD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 395 TLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGLAIPEVPFGGIKDSGYGTEGGSEAVEAYLETRFI 474
Cdd:TIGR04284 397 GDDDAVRIANDSPYGLSGTVFGADPERAAAVAARVRTGTVNVNGGVWYSADAPFGGYKQSGIGREMGVAGFEEYLETKLI 476
|
.
gi 674257992 475 S 475
Cdd:TIGR04284 477 A 477
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
140-461 |
5.86e-64 |
|
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: 213.24 E-value: 5.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 140 KFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASpAELIRAFVDAGVPAGVVNLVYGVPSEISeYLIPH 219
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHT-AALLAELVPKYLDPDAFQVVQGGVPETT-ALLEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 220 PvIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIAD 299
Cdd:cd07135 184 K-FDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDPSVYD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 300 KFIDGIVKYAESVkVGNGLDADTTMGPLANERRIPAMEEMIQDavSKGAVLkTGGKRIGNKgNFFEPTVLTDVPTSAKMM 379
Cdd:cd07135 263 EFVEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLDT--TKGKVV-IGGEMDEAT-RFIPPTIVSDVSWDDSLM 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 380 NEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGL--AIPEVPFGGIKDSGYG 457
Cdd:cd07135 338 SEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIhvGVDNAPFGGVGDSGYG 417
|
....
gi 674257992 458 TEGG 461
Cdd:cd07135 418 AYHG 421
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
55-455 |
8.02e-62 |
|
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: 207.51 E-value: 8.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 55 KGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDwFAEEA--RRTYGQVIPARFG 132
Cdd:cd07095 11 AAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKID-ISIKAyhERTGERATPMAQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 133 gvsNLAIKF-PVGPVAAFTPWNFPIN----QVVRKLSAavatGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYG 207
Cdd:cd07095 90 ---RAVLRHrPHGVMAVFGPFNFPGHlpngHIVPALLA----GNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 208 VPsEISEYLIPHPVIRKISFTGSTPVGKHLA-ALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCV 286
Cdd:cd07095 163 GR-ETGEALAAHEGIDGLLFTGSAATGLLLHrQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 287 APTR-FLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFE 365
Cdd:cd07095 242 CARRlIVPDGAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFLS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 366 PTVLtDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNH--NGlAI 443
Cdd:cd07095 322 PGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNRptTG-AS 399
|
410
....*....|..
gi 674257992 444 PEVPFGGIKDSG 455
Cdd:cd07095 400 STAPFGGVGLSG 411
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
55-461 |
4.73e-61 |
|
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: 205.54 E-value: 4.73e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 55 KGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKM-EII----NAADTI----DWFAEEARRTygq 125
Cdd:cd07134 9 AHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLtEILpvlsEINHAIkhlkKWMKPKRVRT--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 126 viPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASpAELIRAFVDAGVPAGVVNLV 205
Cdd:cd07134 86 --PLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHT-SAVIAKIIREAFDEDEVAVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 206 YGVPsEISEYLIPHPViRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVC 285
Cdd:cd07134 163 EGDA-EVAQALLELPF-DHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 286 VAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTT-MGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNkGNFF 364
Cdd:cd07134 241 IAPDYVFVHESVKDAFVEHLKAEIEKFYGKDAARKASPdLARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAA-QRYI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 365 EPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGL--A 442
Cdd:cd07134 320 APTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhfL 399
|
410
....*....|....*....
gi 674257992 443 IPEVPFGGIKDSGYGTEGG 461
Cdd:cd07134 400 NPNLPFGGVNNSGIGSYHG 418
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
142-457 |
4.42e-60 |
|
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: 202.76 E-value: 4.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 142 PVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASpAELIRAFVDAGVPAGVVNLVYGVPSEISEyLIPHPv 221
Cdd:cd07087 100 PLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPAT-SALLAKLIPKYFDPEAVAVVEGGVEVATA-LLAEP- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 222 IRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKF 301
Cdd:cd07087 177 FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDEL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 302 IDGIVKYAESVkVGNGLDADTTMGPLANERRIPAMEEMIQDavskGAVLkTGGKRIGNKgNFFEPTVLTDVPTSAKMMNE 381
Cdd:cd07087 257 IEELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASLLDD----GKVV-IGGQVDKEE-RYIAPTILDDVSPDSPLMQE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 382 EPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN----HngLAIPEVPFGGIKDSGYG 457
Cdd:cd07087 330 EIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvllH--AAIPNLPFGGVGNSGMG 407
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
5-476 |
2.78e-59 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 205.37 E-value: 2.78e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 5 PDIKLLINGEWRDALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRID 84
Cdd:PLN02419 112 PRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 85 YIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLS 164
Cdd:PLN02419 192 KLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 165 AAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEyLIPHPVIRKISFTGSTPVGKHLAALAGKH 244
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 245 MKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVA-PTRFLIQDsiADKFIDGIVKYAESVKVGNGLDADTT 323
Cdd:PLN02419 351 GKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMAlSTVVFVGD--AKSWEDKLVERAKALKVTCGSEPDAD 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 324 MGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRI----GNKGNFFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEA 399
Cdd:PLN02419 429 LGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIvvpgYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEA 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 400 LEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHN-GLAIPEVPFGGIKDSGYGTEG--GSEAVEAYLETRFISQ 476
Cdd:PLN02419 509 ISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPiPVPLPFFSFTGNKASFAGDLNfyGKAGVDFFTQIKLVTQ 588
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
11-469 |
2.89e-53 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 186.96 E-value: 2.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 11 INGEWRDalSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLM 90
Cdd:PLN02315 25 VGGEWRA--NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 91 TREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATG 170
Cdd:PLN02315 103 SLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALVCG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 171 CSIIVKAPEETPASPAELIRAFVDA----GVPAGVVNLVYGvPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMK 246
Cdd:PLN02315 183 NCVVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 247 RATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTTMGP 326
Cdd:PLN02315 262 KCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 327 LANERRIPAMEEMIQDAVSKGAVLKTGGKRIGNKGNFFEPTVLtDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRL 406
Cdd:PLN02315 342 LHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSV 420
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 674257992 407 PFGLASYAFTGSVKTAHAL--SQRVEAGMLTVN--HNGLAIPEVpFGGIKDSGYGTEGGSEAVEAYL 469
Cdd:PLN02315 421 PQGLSSSIFTRNPETIFKWigPLGSDCGIVNVNipTNGAEIGGA-FGGEKATGGGREAGSDSWKQYM 486
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
64-457 |
1.86e-52 |
|
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: 182.68 E-value: 1.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 64 SAFERSKIMRKAADLVRQRIDYIAWLMTREQG-KPLAQSKM-EIINAADTID--------WFAEEARRTygqviPARFGG 133
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLLaEILPSIAGIKharkhlkkWMKPSRRHV-----GLLFLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 134 VSNLAIKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASpAELIRAFVDAGVPAGVVNLVYG---VPS 210
Cdd:cd07133 93 AKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRT-SALLAELLAEYFDEDEVAVVTGgadVAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 211 EISEYLIPHPVirkisFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTR 290
Cdd:cd07133 172 AFSSLPFDHLL-----FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 291 FLIQDSIADKFIDGIVKYAESVkVGNGLDADtTMGPLANER---RIpamEEMIQDAVSKGAVLKT--GGKRIGNKGNFFE 365
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAKM-YPTLADNP-DYTSIINERhyaRL---QGLLEDARAKGARVIElnPAGEDFAATRKLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 366 PTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGL--AI 443
Cdd:cd07133 322 PTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLhvAQ 401
|
410
....*....|....
gi 674257992 444 PEVPFGGIKDSGYG 457
Cdd:cd07133 402 DDLPFGGVGASGMG 415
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
139-461 |
7.90e-51 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 179.84 E-value: 7.90e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 139 IKFPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASpAELIRAFVDAGVPAGVVNLVYG---VPSEISEY 215
Cdd:PTZ00381 106 IPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHT-SKLMAKLLTKYLDPSYVRVIEGgveVTTELLKE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 216 LIPHpvirkISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQD 295
Cdd:PTZ00381 185 PFDH-----IFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 296 SIADKFIDgivKYAESVK--VGNGLDADTTMGPLANERRIPAMEEMIQDavSKGAVLKTGGKRIGNKgnFFEPTVLTDVP 373
Cdd:PTZ00381 260 SIKDKFIE---ALKEAIKefFGEDPKKSEDYSRIVNEFHTKRLAELIKD--HGGKVVYGGEVDIENK--YVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 374 TSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHN--GLAIPEVPFGGI 451
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCvfHLLNPNLPFGGV 412
|
330
....*....|
gi 674257992 452 KDSGYGTEGG 461
Cdd:PTZ00381 413 GNSGMGAYHG 422
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
151-457 |
5.16e-50 |
|
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: 176.54 E-value: 5.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 151 PWNFPINQVVRKLSAAVATGCSIIVKAPEETPASpAELIRAFVDAGVPAGVVNLVYGVPSEISEYLipHPVIRKISFTGS 230
Cdd:cd07136 109 PWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNT-SKVIAKIIEETFDEEYVAVVEGGVEENQELL--DQKFDYIFFTGS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 231 TPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAE 310
Cdd:cd07136 186 VRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHESVKEKFIKELKEEIK 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 311 SVKVGNGLDADTtMGPLANERRIPAMEEMIQDavskGAVLkTGGKriGNKG-NFFEPTVLTDVPTSAKMMNEEPFGPVAI 389
Cdd:cd07136 266 KFYGEDPLESPD-YGRIINEKHFDRLAGLLDN----GKIV-FGGN--TDREtLYIEPTILDNVTWDDPVMQEEIFGPILP 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 674257992 390 VNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN----HngLAIPEVPFGGIKDSGYG 457
Cdd:cd07136 338 VLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtimH--LANPYLPFGGVGNSGMG 407
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
9-455 |
5.17e-50 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 177.46 E-value: 5.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 9 LLINGEWRdALSGKTIEVLDPATDETL--GTIAHAEKADLDLALDAadKGFKVWRETSAFERSKIMRKAADLVRQRIDYI 86
Cdd:PRK09457 3 LWINGDWI-AGQGEAFESRNPVSGEVLwqGNDATAAQVDAAVRAAR--AAFPAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 87 AWLMTREQGKPLAQSKME---IINAAD-TIDWFAEearRTyGQVIPARFGGVSNLAIKfPVGPVAAFTPWNFPIN----Q 158
Cdd:PRK09457 80 AEVIARETGKPLWEAATEvtaMINKIAiSIQAYHE---RT-GEKRSEMADGAAVLRHR-PHGVVAVFGPYNFPGHlpngH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 159 VVRKLSAavatGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPsEISEYLIPHPVIRKISFTGSTPVGKHL- 237
Cdd:PRK09457 155 IVPALLA----GNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGR-ETGKALAAHPDIDGLLFTGSANTGYLLh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 238 AALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSI-ADKFIDGIVKYAESVKVGn 316
Cdd:PRK09457 230 RQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVG- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 317 GLDADTT--MGPLANERRIPAMEEMIQDAVSKGAV-LKTGGKRIGNKGnFFEPTVLtDVPTSAKMMNEEPFGPVAIVNRF 393
Cdd:PRK09457 309 RWDAEPQpfMGAVISEQAAQGLVAAQAQLLALGGKsLLEMTQLQAGTG-LLTPGII-DVTGVAELPDEEYFGPLLQVVRY 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674257992 394 STLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNH--NGlAIPEVPFGGIKDSG 455
Cdd:PRK09457 387 DDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNKplTG-ASSAAPFGGVGASG 449
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
10-461 |
2.17e-47 |
|
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: 170.86 E-value: 2.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEWRDalSGKTIEVLDPAT-DETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAW 88
Cdd:TIGR01238 41 IIGHSYKA--DGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 89 LMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPArfggvsnlaikfPVGPVAAFTPWNFPINQVVRKLSAAVA 168
Cdd:TIGR01238 119 LCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSVE------------SRGVFVCISPWNFPLAIFTGQISAALA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 169 TGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHL-AALAGKHMKR 247
Cdd:TIGR01238 187 AGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInQTLAQREDAP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 248 ATM--ELGGHAPVLVfDDADLAK--AIEVSATAkFRNAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTT 323
Cdd:TIGR01238 267 VPLiaETGGQNAMIV-DSTALPEqvVRDVLRSA-FDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 324 MGPLANERRIPAMEEMIQDAVSKG---AVLKTGGKRIGNKGNFFEPTVLTdvPTSAKMMNEEPFGPVAIVNRFST--LDE 398
Cdd:TIGR01238 345 VGPVIDAEAKQNLLAHIEHMSQTQkkiAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQ 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674257992 399 ALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHN--GLAIPEVPFGGIKDSGYGTEGG 461
Cdd:TIGR01238 423 IVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNqvGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
10-457 |
9.98e-46 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 171.15 E-value: 9.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGewrdalSGKTIEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAW 88
Cdd:PRK11904 556 IING------EGEARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIA 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 89 LMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPAR-FGGVSNLAIKFPVGPVAAFTPWNFP----INQVvrkl 163
Cdd:PRK11904 630 LCVREAGKTLQDAIAEVREAVDFCRYYAAQARRLFGAPEKLPgPTGESNELRLHGRGVFVCISPWNFPlaifLGQV---- 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 164 SAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLA-ALAG 242
Cdd:PRK11904 706 AAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINrTLAA 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 243 KHMKRATM--ELGGHAPVLVfdDA-----DLAKAIEVSAtakFRNAGQVCVApTRFL-IQDSIADKFIDGIVKYAESVKV 314
Cdd:PRK11904 786 RDGPIVPLiaETGGQNAMIV--DStalpeQVVDDVVTSA---FRSAGQRCSA-LRVLfVQEDIADRVIEMLKGAMAELKV 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 315 GNGLDADTTMGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIG-NKGNFFEPTVLtDVPtSAKMMNEEPFGPVAIVNRF 393
Cdd:PRK11904 860 GDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLPLPAGtENGHFVAPTAF-EID-SISQLEREVFGPILHVIRY 937
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 674257992 394 --STLDEALEEANRLPFGLasyafTGSV-----KTAHALSQRVEAGMLTVNHN--GlAIPEV-PFGGIKDSGYG 457
Cdd:PRK11904 938 kaSDLDKVIDAINATGYGL-----TLGIhsrieETADRIADRVRVGNVYVNRNqiG-AVVGVqPFGGQGLSGTG 1005
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
61-468 |
1.84e-44 |
|
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: 161.42 E-value: 1.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 61 RETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQS-KMEIINAADTI--------DWFAEEARRTYGQVIPARF 131
Cdd:cd07137 16 RTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkKWMAPEKVKTPLTTFPAKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 132 GGVSNlaikfPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASP---AELIRAFVDAGVpagvVNLVYGV 208
Cdd:cd07137 96 EIVSE-----PLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSallAKLIPEYLDTKA----IKVIEGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 209 PSEiSEYLIPHPvIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKF-RNAGQVCVA 287
Cdd:cd07137 167 VPE-TTALLEQK-WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 288 PTRFLIQDSIADKFIDGIVKYAESVKVGNGLDADTtMGPLANERRIPAMEEMIQDAVSKGAVLKtgGKRIGNKGNFFEPT 367
Cdd:cd07137 245 PDYVLVEESFAPTLIDALKNTLEKFFGENPKESKD-LSRIVNSHHFQRLSRLLDDPSVADKIVH--GGERDEKNLYIEPT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 368 VLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGL--AIPE 445
Cdd:cd07137 322 ILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVqyAIDT 401
|
410 420
....*....|....*....|...
gi 674257992 446 VPFGGIKDSGYGTEGGSEAVEAY 468
Cdd:cd07137 402 LPFGGVGESGFGAYHGKFSFDAF 424
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
6-475 |
2.18e-42 |
|
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: 157.36 E-value: 2.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 6 DIKLLINGEWRDalSGKTIEVLDPAT-DETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRid 84
Cdd:cd07123 32 EIPLVIGGKEVR--TGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGK-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 85 YIAWLMTRE---QGKPLAQSkmEIINAADTIDWF---AEEARRTYGQVIPARFGGVSNLAIKFPV-GPVAAFTPWNFpiN 157
Cdd:cd07123 108 YRYELNAATmlgQGKNVWQA--EIDAACELIDFLrfnVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNF--T 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 158 QVVRKLSAAVATGCSIIVKAPEETPASPAELI-RAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKH 236
Cdd:cd07123 184 AIGGNLAGAPALMGNVVLWKPSDTAVLSNYLVyKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 237 LAALAGKHMK------RATMELGGHAPVLVFDDADlakaIEVSATAKFRNA----GQVCVAPTRFLIQDSIADKFIDGIV 306
Cdd:cd07123 264 LWKQIGENLDryrtypRIVGETGGKNFHLVHPSAD----VDSLVTATVRGAfeyqGQKCSAASRAYVPESLWPEVKERLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 307 KYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQDA-VSKGAVLKTGGKRIGNKGNFFEPTV-LTDVPTSaKMMNEEPF 384
Cdd:cd07123 340 EELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAkSDPEAEIIAGGKCDDSVGYFVEPTViETTDPKH-KLMTEEIF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 385 GPVAIVNRFStlDEALEEANRLPFGLASYAFTGSV--------KTAH-ALsqRVEAGMLTVNH--NGLAIPEVPFGGIKD 453
Cdd:cd07123 419 GPVLTVYVYP--DSDFEETLELVDTTSPYALTGAIfaqdrkaiREATdAL--RNAAGNFYINDkpTGAVVGQQPFGGARA 494
|
490 500
....*....|....*....|..
gi 674257992 454 SGYGTEGGSeavEAYLeTRFIS 475
Cdd:cd07123 495 SGTNDKAGS---PLNL-LRWVS 512
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
10-450 |
5.22e-41 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 157.02 E-value: 5.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEwrdALSGKTIEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLV-RQRIDYIA 87
Cdd:COG4230 561 LIAGE---AASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLeAHRAELMA 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 88 wLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARfggvsnlaikfPVGPVAAFTPWNFP----INQVvrkl 163
Cdd:COG4230 638 -LLVREAGKTLPDAIAEVREAVDFCRYYAAQARRLFAAPTVLR-----------GRGVFVCISPWNFPlaifTGQV---- 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 164 SAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLA-ALAG 242
Cdd:COG4230 702 AAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINrTLAA 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 243 KHmkratmelGGHAPVL-------------------VFDDAdLAkaievSAtakFRNAGQVCVApTRFL-IQDSIADKFI 302
Cdd:COG4230 782 RD--------GPIVPLIaetggqnamivdssalpeqVVDDV-LA-----SA---FDSAGQRCSA-LRVLcVQEDIADRVL 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 303 DGIVKYAESVKVGNGLDADTTMGPL--ANERripameEMIQDAVSKgavLKTGGKRI--------GNKGNFFEPTVLtDV 372
Cdd:COG4230 844 EMLKGAMAELRVGDPADLSTDVGPVidAEAR------ANLEAHIER---MRAEGRLVhqlplpeeCANGTFVAPTLI-EI 913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 373 PtSAKMMNEEPFGPVAIVNRF--STLDEALEEANRLPFGLasyafTGSV-----KTAHALSQRVEAGMLTVNHN--GlAI 443
Cdd:COG4230 914 D-SISDLEREVFGPVLHVVRYkaDELDKVIDAINATGYGL-----TLGVhsridETIDRVAARARVGNVYVNRNiiG-AV 986
|
....*...
gi 674257992 444 PEV-PFGG 450
Cdd:COG4230 987 VGVqPFGG 994
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
17-457 |
3.33e-40 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 154.64 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 17 DALSGKTIEVLDPA-TDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQG 95
Cdd:PRK11905 562 GDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAG 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 96 KPLAQSKMEIINAADTIDWFAEEARRTygqviparFGGVSNLaikfPVGPVAAFTPWNFP----INQVvrklSAAVATGC 171
Cdd:PRK11905 642 KTLANAIAEVREAVDFLRYYAAQARRL--------LNGPGHK----PLGPVVCISPWNFPlaifTGQI----AAALVAGN 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 172 SIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGKHMKRATM- 250
Cdd:PRK11905 706 TVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPl 785
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 251 --ELGGHAPVLVfDDADLA----KAIEVSAtakFRNAGQVCVApTRFL-IQDSIADKFIDGIVKYAESVKVGNGLDADTT 323
Cdd:PRK11905 786 iaETGGQNAMIV-DSSALPeqvvADVIASA---FDSAGQRCSA-LRVLcLQEDVADRVLTMLKGAMDELRIGDPWRLSTD 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 324 MGPLANERRIPAMEEMIQDAVSKGAVLKTGGKRIG-NKGNFFEPTV-----LTDvptsakmMNEEPFGPVAIVNRF--ST 395
Cdd:PRK11905 861 VGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAEtEKGTFVAPTLieidsISD-------LEREVFGPVLHVVRFkaDE 933
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 674257992 396 LDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHN--GlAIPEV-PFGGIKDSGYG 457
Cdd:PRK11905 934 LDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNRNiiG-AVVGVqPFGGEGLSGTG 997
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
142-457 |
2.55e-39 |
|
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: 147.37 E-value: 2.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 142 PVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASP---AELIRAFVDAGVPAgvvnLVYGVPSEISEYLip 218
Cdd:cd07132 100 PLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAkllAELIPKYLDKECYP----VVLGGVEETTELL-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 219 HPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIA 298
Cdd:cd07132 174 KQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLCTPEVQ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 299 DKFIDGIVK-----YAESVKVGNGLdadttmGPLANERRIPAMEEMIQDavSKGAVlktgGKRIGNKGNFFEPTVLTDVP 373
Cdd:cd07132 254 EKFVEALKKtlkefYGEDPKESPDY------GRIINDRHFQRLKKLLSG--GKVAI----GGQTDEKERYIAPTVLTDVK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 374 TSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVN----HngLAIPEVPFG 449
Cdd:cd07132 322 PSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtimH--YTLDSLPFG 399
|
....*...
gi 674257992 450 GIKDSGYG 457
Cdd:cd07132 400 GVGNSGMG 407
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
59-461 |
2.17e-37 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 146.27 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 59 VWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYgqviparfggvSNLA 138
Cdd:PRK11809 697 IWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDF-----------DNDT 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 139 IKfPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIP 218
Cdd:PRK11809 766 HR-PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVA 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 219 HPVIRKISFTGSTPVGKHLA-ALAGK--HMKRAT---MELGGHAPVLVfDDADLAK--AIEVSATAkFRNAGQVCVApTR 290
Cdd:PRK11809 845 DARVRGVMFTGSTEVARLLQrNLAGRldPQGRPIpliAETGGQNAMIV-DSSALTEqvVADVLASA-FDSAGQRCSA-LR 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 291 FL-IQDSIADKFIDGIVKYAESVKVGNGLDADTTMGPL------AN-ERRIPAMEE----MIQDAVSKGAVLKTggkrig 358
Cdd:PRK11809 922 VLcLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVidaeakANiERHIQAMRAkgrpVFQAARENSEDWQS------ 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 359 nkGNFFEPTVLT-DvptSAKMMNEEPFGPVAIVNRF--STLDEALEEANRLPFGLasyafTGSVKT------AHaLSQRV 429
Cdd:PRK11809 996 --GTFVPPTLIElD---SFDELKREVFGPVLHVVRYnrNQLDELIEQINASGYGL-----TLGVHTridetiAQ-VTGSA 1064
|
410 420 430
....*....|....*....|....*....|....
gi 674257992 430 EAGMLTVNHN--GLAIPEVPFGGIKDSGYGTEGG 461
Cdd:PRK11809 1065 HVGNLYVNRNmvGAVVGVQPFGGEGLSGTGPKAG 1098
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
113-468 |
2.98e-36 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 139.80 E-value: 2.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 113 DWFAEEARRTYGQVIPARFGGVSNlaikfPVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAeLIRAF 192
Cdd:PLN02174 88 NWMAPEKAKTSLTTFPASAEIVSE-----PLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSA-LLAKL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 193 VDAGVPAGVVNLVYGVPSEISEYLipHPVIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEV 272
Cdd:PLN02174 162 LEQYLDSSAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 273 SATAKFR-NAGQVCVAPTRFLIQDSIADKFIDGIVKYAESVKVGNGLDAdTTMGPLANERRIPAMEEMIQDAVSKGAVLK 351
Cdd:PLN02174 240 IIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMES-KDMSRIVNSTHFDRLSKLLDEKEVSDKIVY 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 352 TGGKRIGNKGnfFEPTVLTDVPTSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEA 431
Cdd:PLN02174 319 GGEKDRENLK--IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSA 396
|
330 340 350
....*....|....*....|....*....|....*....
gi 674257992 432 GMLTVNHNG--LAIPEVPFGGIKDSGYGTEGGSEAVEAY 468
Cdd:PLN02174 397 GGIVVNDIAvhLALHTLPFGGVGESGMGAYHGKFSFDAF 435
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
142-457 |
6.40e-34 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 133.31 E-value: 6.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 142 PVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAEL---IRAFVDAGVpagvVNLVYGVPsEISEYLIP 218
Cdd:PLN02203 108 PLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLaanIPKYLDSKA----VKVIEGGP-AVGEQLLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 219 HPvIRKISFTGSTPVGKHLAALAGKHMKRATMELGGHAPVlVFDDADLAKAIEVSAT----AKFRN-AGQVCVAPTRFLI 293
Cdd:PLN02203 183 HK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPC-IVDSLSSSRDTKVAVNrivgGKWGScAGQACIAIDYVLV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 294 QDSIADKFIDGIVKYAESVKVGNGLDADTtMGPLANERRIPAMEEMIQDAVSKGAVLKTGGkrIGNKGNFFEPTVLTDVP 373
Cdd:PLN02203 261 EERFAPILIELLKSTIKKFFGENPRESKS-MARILNKKHFQRLSNLLKDPRVAASIVHGGS--IDEKKLFIEPTILLNPP 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 374 TSAKMMNEEPFGPVAIVNRFSTLDEALEEANRLPFGLASYAFTGSVKTAHALSQRVEAGMLTVNHNGL--AIPEVPFGGI 451
Cdd:PLN02203 338 LDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAIIqyACDSLPFGGV 417
|
....*.
gi 674257992 452 KDSGYG 457
Cdd:PLN02203 418 GESGFG 423
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
57-437 |
2.57e-28 |
|
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: 116.87 E-value: 2.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 57 FKVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARR-TYGQVI-----PAR 130
Cdd:cd07129 12 FESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgSWLDARidpadPDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 131 F-GGVSNL-AIKFPVGPVAAFTPWNFPInqvvrKLS-------AAVATGCSIIVKApeeTPASP------AELIRAFVDA 195
Cdd:cd07129 92 QpLPRPDLrRMLVPLGPVAVFGASNFPL-----AFSvaggdtaSALAAGCPVVVKA---HPAHPgtselvARAIRAALRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 196 -GVPAGVVNLVYGVPSEISEYLIPHPVIRKISFTGSTPVGKHLAALAGkhmKRAT-----MELGGHAPVLVFDDA----- 264
Cdd:cd07129 164 tGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAA---ARPEpipfyAELGSVNPVFILPGAlaerg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 265 -DLAKAIEVSATAkfrNAGQVCVAP-TRFLIQDSIADKFIDGIVKYAESVKVgngldadttmGPLANERRIPAMEEMIQD 342
Cdd:cd07129 241 eAIAQGFVGSLTL---GAGQFCTNPgLVLVPAGPAGDAFIAALAEALAAAPA----------QTMLTPGIAEAYRQGVEA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 343 AVSKGAVLKTGGKRIGNKGNFFEPTVLtdVPTSAKMMN-----EEPFGPVAIVNRFSTLDEALEEANRLPFGL-AS-YAF 415
Cdd:cd07129 308 LAAAPGVRVLAGGAAAEGGNQAAPTLF--KVDAAAFLAdpalqEEVFGPASLVVRYDDAAELLAVAEALEGQLtATiHGE 385
|
410 420
....*....|....*....|....
gi 674257992 416 TGSVKTAHALSQRVE--AGMLTVN 437
Cdd:cd07129 386 EDDLALARELLPVLErkAGRLLFN 409
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
58-472 |
6.92e-26 |
|
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: 109.63 E-value: 6.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 58 KVWRETSAFERSKIMRKAADLVRQRIDYIAWLMTREQGKPlaqsKMEIINAADTIDWFAEEARRTYGQVIPARFGGVSNL 137
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG----WMFAENICGDQVQLRARAFVIYSYRIPHEPGNHLGQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 138 AIKF-------PVGPVAAFTPWNFPINQVVRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAG-VPAGVVNLVYGvP 209
Cdd:cd07084 89 GLKQqshgyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLING-D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 210 SEISEYLIPHPVIRKISFTGSTPVGKHLAALAgkHMKRATMELGGHAPVLVFDDAD----LAKAIEVSATAKfrnAGQVC 285
Cdd:cd07084 168 GKTMQALLLHPNPKMVLFTGSSRVAEKLALDA--KQARIYLELAGFNWKVLGPDAQavdyVAWQCVQDMTAC---SGQKC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 286 VAPTR-FLIQDSIADKFIDGIVKYAESVKVGngldaDTTMGPLANERRIPAMEEMIQDAvskGAVLKTGGKRIGNKG--N 362
Cdd:cd07084 243 TAQSMlFVPENWSKTPLVEKLKALLARRKLE-----DLLLGPVQTFTTLAMIAHMENLL---GSVLLFSGKELKNHSipS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 363 FFEPTVLTD--VPTSA-----KMMNEEPFGPVAIVNRF-----STLDEALE-EANRLPFGLAS--YAFTGSVKTAHALSQ 427
Cdd:cd07084 315 IYGACVASAlfVPIDEilktyELVTEEIFGPFAIVVEYkkdqlALVLELLErMHGSLTAAIYSndPIFLQELIGNLWVAG 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 674257992 428 RVEAGMLtvNHNGLAIPEVPFGGIKDSGYGTE-GGSEAVEAYLETR 472
Cdd:cd07084 395 RTYAILR--GRTGVAPNQNHGGGPAADPRGAGiGGPEAIKLVWRCH 438
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
11-405 |
1.33e-21 |
|
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: 97.34 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 11 INGEWRdALSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRK-AADLVRQRIDYIAwl 89
Cdd:cd07128 5 VAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKAlAKYLMERKEDLYA-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 90 MTREQGKPLAQSKMEIINAADTIDWFAEEARR--------TYGQVIP-ARFGGVSNLAIKFPVGPVA----AFtpwNFPI 156
Cdd:cd07128 82 LSAATGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPlSKDGTFVGQHILTPRRGVAvhinAF---NFPV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 157 NQVVRKLSAAVATGCSIIVKapeetPASPA-----ELIRAFVDAGV-PAGVVNLVYGVPSEISEYLIPHPVIrkiSFTGS 230
Cdd:cd07128 159 WGMLEKFAPALLAGVPVIVK-----PATATaylteAVVKDIVESGLlPEGALQLICGSVGDLLDHLGEQDVV---AFTGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 231 TPVGKHLAALAG--KHMKRATME--------LGghaPVLVFDDADLAKAI-EVSA--TAKfrnAGQVCVAPTRFLIQDSI 297
Cdd:cd07128 231 AATAAKLRAHPNivARSIRFNAEadslnaaiLG---PDATPGTPEFDLFVkEVARemTVK---AGQKCTAIRRAFVPEAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 298 ADKFIDGIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIqDAVSKGAVLKTGGK-------RIGNKGNFFEPTVLT 370
Cdd:cd07128 305 VDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAV-ATLLAEAEVVFGGPdrfevvgADAEKGAFFPPTLLL 383
|
410 420 430
....*....|....*....|....*....|....*..
gi 674257992 371 -DVPTSAKMMNE-EPFGPVAIVNRFSTLDEALEEANR 405
Cdd:cd07128 384 cDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAAR 420
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
10-437 |
5.68e-15 |
|
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: 77.15 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 10 LINGEWRDAlsGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFK--VWRETSAFER----SKIMRKAADLVR--Q 81
Cdd:cd07126 2 LVAGKWKGA--SNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLRQCPKsgLHNPLKNPERyllyGDVSHRVAHELRkpE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 82 RIDYIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARR--TYGQVIPARFGGVSNLAIKFPVGPVAAFTPWNFPINQV 159
Cdd:cd07126 80 VEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRflARSFNVPGDHQGQQSSGYRWPYGPVAIITPFNFPLEIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 160 VRKLSAAVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEyLIPHPVIRKISFTGSTPVGKHLAA 239
Cdd:cd07126 160 ALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNK-ILLEANPRMTLFTGSSKVAERLAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 240 LAgkHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADK-FIDGIVKYAESVKVgngl 318
Cdd:cd07126 239 EL--HGKVKLEDAGFDWKILGPDVSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKALAEQRKL---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 319 dADTTMGP---LANERRIPAMEEMIQdavSKGAVLKTGGKRIGNKG-----NFFEPTVLTdVPTSAKMMNE-------EP 383
Cdd:cd07126 313 -EDLTIGPvltWTTERILDHVDKLLA---IPGAKVLFGGKPLTNHSipsiyGAYEPTAVF-VPLEEIAIEEnfelvttEV 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 674257992 384 FGPVAIVNRF--STLDEALEEANRLPFGLASYAFTGSVKtahaLSQRVEAGmlTVN 437
Cdd:cd07126 388 FGPFQVVTEYkdEQLPLVLEALERMHAHLTAAVVSNDIR----FLQEVLAN--TVN 437
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
11-405 |
6.58e-14 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 73.97 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 11 INGEWRDAlSGKTIEVLDPATDETLGTIAHAEKADLDLALDAADKGFKVWRETSAFERSKIMRKAADLVR-QRIDYIAwL 89
Cdd:PRK11903 9 VAGRWQAG-SGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQaNRDAYYD-I 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 90 MTREQGKPLAQSKMEIINAADTIDWFAEeARRTYGQVIPARFGGVSNLA---------IKFPVGPVAAF-TPWNFPINQV 159
Cdd:PRK11903 87 ATANSGTTRNDSAVDIDGGIFTLGYYAK-LGAALGDARLLRDGEAVQLGkdpafqgqhVLVPTRGVALFiNAFNFPAWGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 160 VRKLSAAVATGCSIIVKapeetPASPA-----ELIRAFVDAGV-PAGVVNLVYGVPSEISEYLIPHPVIrkiSFTGSTPV 233
Cdd:PRK11903 166 WEKAAPALLAGVPVIVK-----PATATawltqRMVKDVVAAGIlPAGALSVVCGSSAGLLDHLQPFDVV---SFTGSAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 234 GKHLAALAG--KHMKRATMELGGHAPVLVFDDAD--------LAKAIEVSATAKfrnAGQVCVAPTRFLIQDSIADKFID 303
Cdd:PRK11903 238 AAVLRSHPAvvQRSVRVNVEADSLNSALLGPDAApgseafdlFVKEVVREMTVK---SGQKCTAIRRIFVPEALYDAVAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 304 GIVKYAESVKVGNGLDADTTMGPLANERRIPAMEEMIQdAVSKGAVLKTGGKRIG------NKGNFFEPTVL-TDVPTSA 376
Cdd:PRK11903 315 ALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGFAlvdadpAVAACVGPTLLgASDPDAA 393
|
410 420 430
....*....|....*....|....*....|
gi 674257992 377 KMMNE-EPFGPVAIVNRFSTLDEALEEANR 405
Cdd:PRK11903 394 TAVHDvEVFGPVATLLPYRDAAHALALARR 423
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
68-303 |
1.65e-10 |
|
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: 63.05 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 68 RSKIMRKAADL-VRQRIDyIAWLMTREQGKPLAQSKMEIINAADTIDWFAEEARRTYGQVIPARFGGVsnLAIKFPVGPV 146
Cdd:cd07081 23 VDLIFRAAAEAaEDARID-LAKLAVSETGMGRVEDKVIKNHFAAEYIYNVYKDEKTCGVLTGDENGGT--LIIAEPIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 147 AAFTPWNFPINQVVRKLSAAVATGCSIIV----KAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPSEISEYLIPHPVI 222
Cdd:cd07081 100 ASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSIELAQRLMKFPGI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 223 RKISFTGstpvGKHLAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLIQDSIADKFI 302
Cdd:cd07081 180 GLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDSVYDEVM 255
|
.
gi 674257992 303 D 303
Cdd:cd07081 256 R 256
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
87-406 |
4.63e-09 |
|
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: 58.64 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 87 AWLMTREQGKPLAQSK-MEIINAAdtidwfAEEARRTYGQVIPAR-FGGVSNLAIK--FPVGP--------VAAFTPWN- 153
Cdd:cd07127 137 AFMMAFQAGGPHAQDRgLEAVAYA------WREMSRIPPTAEWEKpQGKHDPLAMEktFTVVPrgvalvigCSTFPTWNg 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 154 FPinqvvrKLSAAVATGCSIIVKaPEETPASPAELI-----RAFVDAGVPAGVVNLVYGVPSE-ISEYLIPHPVIRKISF 227
Cdd:cd07127 211 YP------GLFASLATGNPVIVK-PHPAAILPLAITvqvarEVLAEAGFDPNLVTLAADTPEEpIAQTLATRPEVRIIDF 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 228 TGSTPVGKHLAALAGKhmKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNAGQVCVAPTRFLI-QDSIADKfiDGIV 306
Cdd:cd07127 284 TGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVDSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVpRDGIQTD--DGRK 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 307 KYAEsvkVGNGLdADTTMGPLANERRI---------PAMEEMIQDAVSKGAVLKTgGKRIGN----KGNFFEPTVLTDVP 373
Cdd:cd07127 360 SFDE---VAADL-AAAIDGLLADPARAaallgaiqsPDTLARIAEARQLGEVLLA-SEAVAHpefpDARVRTPLLLKLDA 434
|
330 340 350
....*....|....*....|....*....|...
gi 674257992 374 TSAKMMNEEPFGPVAIVNRFSTLDEALEEANRL 406
Cdd:cd07127 435 SDEAAYAEERFGPIAFVVATDSTDHSIELARES 467
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
68-303 |
5.49e-07 |
|
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: 51.84 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 68 RSKIMRKAADLV---RQRIDYIAWLMTREQGKPLAQ--------SKMEIINAADTIDWFAEEARRTYGQVIPARFGgvsN 136
Cdd:cd07077 18 RDLIINAIANALydtRQRLASEAVSERGAYIRSLIAnwiammgcSESKLYKNIDTERGITASVGHIQDVLLPDNGE---T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 137 LAIKFPVGPVAAFTPWNFPINQVVRKLSAaVATGCSIIVKAPEETPASPAELIRAFVDAGVPAGVVNLVYGVPS---EIS 213
Cdd:cd07077 95 YVRAFPIGVTMHILPSTNPLSGITSALRG-IATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLYVPHpsdELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 214 EYLIPHPVIRKISFTGSTPVGKhlAALAGKHMKRATMELGGHAPVLVFDDADLAKAIEVSATAKFRNaGQVCVAPTRFLI 293
Cdd:cd07077 174 EELLSHPKIDLIVATGGRDAVD--AAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYV 250
|
250
....*....|
gi 674257992 294 QDSIADKFID 303
Cdd:cd07077 251 VDDVLDPLYE 260
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
142-303 |
3.55e-06 |
|
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: 49.03 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 142 PVGPVAAFTPWNFPINQVVRKLSAAVATGCSII-------VKAPEETpaspAELIR-AFVDAGVPAGVVNLVYGVPSEIS 213
Cdd:cd07122 95 PVGVIAALIPSTNPTSTAIFKALIALKTRNAIIfsphpraKKCSIEA----AKIMReAAVAAGAPEGLIQWIEEPSIELT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674257992 214 EYLIPHPVIRKISFTGSTPVGKhLAALAGKHmkratmELG---GHAPVLVFDDADLAKAIEVSATAK-FRNaGQVCVAPT 289
Cdd:cd07122 171 QELMKHPDVDLILATGGPGMVK-AAYSSGKP------AIGvgpGNVPAYIDETADIKRAVKDIILSKtFDN-GTICASEQ 242
|
170
....*....|....
gi 674257992 290 RFLIQDSIADKFID 303
Cdd:cd07122 243 SVIVDDEIYDEVRA 256
|
|
| |
