|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
27-477 |
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: 626.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVM 186
Cdd:cd07103 81 DYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 187 IAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVP 266
Cdd:cd07103 161 LALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 267 AERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVK 346
Cdd:cd07103 241 LDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDAVA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 347 SGARLLCgGGEPVGLGdGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQ 426
Cdd:cd07103 321 KGAKVLT-GGKRLGLG-GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 736049070 427 RLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07103 399 RVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-480 |
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: 562.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 1 MTYPELKLLVDGQWLGAEKNqrDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAI 80
Cdd:COG1012 1 MTTPEYPLFIGGEWVAAASG--ETFDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 81 REQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLA 160
Cdd:COG1012 79 EERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 161 ARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLG 240
Cdd:COG1012 159 AWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 241 LASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMD 320
Cdd:COG1012 239 AAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 321 ETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCgGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLE 400
Cdd:COG1012 319 PGTDMGPLISEAQLERVLAYIEDAVAEGAELLT-GGRRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 401 QAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINT-FAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:COG1012 398 EAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDgTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTI 477
|
.
gi 736049070 480 S 480
Cdd:COG1012 478 R 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
23-477 |
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: 520.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 23 DTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEA 102
Cdd:pfam00171 7 ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 103 LGEVTATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEET 182
Cdd:pfam00171 87 RGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 183 PGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVD 262
Cdd:pfam00171 166 PLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 263 RDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTD 342
Cdd:pfam00171 246 EDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 343 EAVKSGARLLCGGGEpvGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSV 422
Cdd:pfam00171 326 DAKEEGAKLLTGGEA--GLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDL 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 736049070 423 ESMQRLQGSLQAGSVSINTFAVTPPE-LPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:pfam00171 404 ERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
48-478 |
1.08e-162 |
|
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: 467.07 E-value: 1.08e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 48 EQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRV 127
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 128 VPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLY 207
Cdd:cd07078 81 IPSPDPGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 208 GVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICH 287
Cdd:cd07078 161 GDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 288 APTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGlGDGFFW 367
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEG-GKGYFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 368 QATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAV-TP 446
Cdd:cd07078 320 PPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAE 399
|
410 420 430
....*....|....*....|....*....|..
gi 736049070 447 PELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07078 400 PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVT 431
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
9-477 |
1.19e-156 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 454.15 E-value: 1.19e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 9 LVDGQWLGAEKNqrDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLA 88
Cdd:PLN02278 28 LIGGKWTDAYDG--KTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 89 QILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATAL 168
Cdd:PLN02278 106 QLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 169 AAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKK 248
Cdd:PLN02278 186 AAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 249 ITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPL 328
Cdd:PLN02278 266 VSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 329 VNRRRQAAMQELTDEAVKSGARLLCgGGEPVGLGdGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANN 408
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLL-GGKRHSLG-GTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736049070 409 VEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
27-475 |
1.91e-150 |
|
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: 436.48 E-value: 1.91e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:TIGR01780 1 VYNPATGEIIGSVPDQGVDETEAAIRAAYEAFKTWRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVM 186
Cdd:TIGR01780 81 LYAASFLEWFAEEAKRVYGDTIPSPQSDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPLSA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 187 IAIARICMDEGLPSGTLNVLYG-VPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:TIGR01780 161 LALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSASTVKKVSMELGGNAPFIVFDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAV 345
Cdd:TIGR01780 241 DLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIADAV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCgGGEPVGLGdGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESM 425
Cdd:TIGR01780 321 EKGAKVVT-GGKRHELG-GNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSRI 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 736049070 426 QRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIK 475
Cdd:TIGR01780 399 WRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
10-478 |
1.99e-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: 421.67 E-value: 1.99e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 10 VDGQWLGAEKNqrDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQ 89
Cdd:cd07088 2 INGEFVPSSSG--ETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 90 ILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALA 169
Cdd:cd07088 80 LIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 170 AGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKI 249
Cdd:cd07088 160 TGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 250 TLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLV 329
Cdd:cd07088 240 SLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 330 NRRRQAAMQELTDEAVKSGARLLCGGGEPvGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNV 409
Cdd:cd07088 320 NEAALDKVEEMVERAVEAGATLLTGGKRP-EGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736049070 410 EFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07088 399 EYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
27-478 |
6.36e-144 |
|
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: 420.03 E-value: 6.36e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAF--AAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALG 104
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFegGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 105 EVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPG 184
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 185 VMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRD 264
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 265 VPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEA 344
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 345 VKSGARLLCGGGEP--VGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSV 422
Cdd:cd07114 321 REEGARVLTGGERPsgADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 736049070 423 ESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
27-479 |
5.69e-141 |
|
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: 412.51 E-value: 5.69e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRV---YGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETP 183
Cdd:cd07110 81 DDVAGCFEYYADLAEQLdakAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 184 GVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDR 263
Cdd:cd07110 161 LTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 264 DVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDE 343
Cdd:cd07110 241 DADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFIAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 344 AVKSGARLLCGGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVE 423
Cdd:cd07110 321 GKEEGARLLCGGRRPAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 736049070 424 SMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07110 401 RCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQITR 456
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
10-477 |
4.01e-137 |
|
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: 403.62 E-value: 4.01e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 10 VDGQWLGAEKnqRDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAA--WKTWTALERGRLLLRIASAIREQARSL 87
Cdd:cd07119 2 IDGEWVEAAS--GKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 88 AQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATA 167
Cdd:cd07119 80 ARLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVP-PHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 168 LAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMK 247
Cdd:cd07119 159 LAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 248 KITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGP 327
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 328 LVNRRRQAAMQELTDEAVKSGARLLCGGGEPVG--LGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIET 405
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGdeLAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049070 406 ANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
7-478 |
1.32e-136 |
|
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: 402.36 E-value: 1.32e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEknQRDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAF--AAWKTWTALERGRLLLRIASAIREQA 84
Cdd:cd07091 5 GLFINNEFVDSV--SGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFetGWWRKMDPRERGRLLNKLADLIERDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 85 RSLAQILTLEQGKTLPEAL-GEVTATADTFEWMAEQGKRVYGRVVPsrfTGVEQLVV--HEPVGVIGAFSPWNYPMVLAA 161
Cdd:cd07091 83 DELAALESLDNGKPLEESAkGDVALSIKCLRYYAGWADKIQGKTIP---IDGNFLAYtrREPIGVCGQIIPWNFPLLMLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 162 RKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGL 241
Cdd:cd07091 160 WKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 242 ASAA-MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMD 320
Cdd:cd07091 240 AAKSnLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 321 ETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGgEPVGlGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLE 400
Cdd:cd07091 320 PDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGG-ERHG-SKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 401 QAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
26-472 |
2.67e-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: 2.67e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 26 PVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGE 105
Cdd:cd07150 2 DDLNPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGV 185
Cdd:cd07150 82 TTFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:cd07150 162 GLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAV 345
Cdd:cd07150 242 DLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCGGGEpvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESM 425
Cdd:cd07150 322 AKGAKLLTGGKY-----DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 736049070 426 QRLQGSLQAGSVSINtfAVT---PPELPFAGIKLSGMGVEMGEEGlMDHF 472
Cdd:cd07150 397 FKLAERLESGMVHIN--DPTildEAHVPFGGVKASGFGREGGEWS-MEEF 443
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
9-477 |
9.02e-134 |
|
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: 394.69 E-value: 9.02e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 9 LVDGQWLGAeknqRDTQPVHNPA-TGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSL 87
Cdd:cd07097 4 YIDGEWVAG----GDGEENRNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 88 AQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATA 167
Cdd:cd07097 80 ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 168 LAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMK 247
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 248 KITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGP 327
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 328 LVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETAN 407
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIAN 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049070 408 NVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN-TFAVTPPELPFAGIKLSGMGV-EMGEEGLMDHFHIKAV 477
Cdd:cd07097 400 DTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGPrEQGEAALEFYTTIKTV 471
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
27-477 |
2.72e-132 |
|
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: 389.97 E-value: 2.72e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVygRVVPSRFTG-VEqlVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGV 185
Cdd:cd07106 81 GGAVAWLRYTASLDLPD--EVIEDDDTRrVE--LRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARICMDEgLPSGTLNVLYGvPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAV 345
Cdd:cd07106 235 DIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCgGGEPVGlGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESM 425
Cdd:cd07106 315 AKGAKVLA-GGEPLD-GPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 736049070 426 QRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
29-477 |
7.98e-132 |
|
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: 389.11 E-value: 7.98e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 29 NPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALG-EVT 107
Cdd:cd07115 3 NPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARRlDVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 108 ATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMI 187
Cdd:cd07115 83 RAADTFRYYAGWADKIEGEVIPVR-GPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 188 AIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPA 267
Cdd:cd07115 162 RIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 268 ERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKS 347
Cdd:cd07115 242 DAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDVGREE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 348 GARLLCGGGEPVglGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQR 427
Cdd:cd07115 322 GARLLTGGKRPG--ARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 736049070 428 LQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07115 400 VAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
9-475 |
2.93e-131 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 388.88 E-value: 2.93e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 9 LVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLA 88
Cdd:PRK11241 14 LINGEWLDANNGE--VIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 89 QILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATAL 168
Cdd:PRK11241 92 RLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 169 AAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKK 248
Cdd:PRK11241 172 AAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 249 ITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPL 328
Cdd:PRK11241 252 VSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 329 VNRRRQAAMQELTDEAVKSGARLLCgGGEPVGLGDGFFwQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANN 408
Cdd:PRK11241 332 IDEKAVAKVEEHIADALEKGARVVC-GGKAHELGGNFF-QPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAND 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736049070 409 VEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIK 475
Cdd:PRK11241 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
25-462 |
1.21e-130 |
|
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: 386.18 E-value: 1.21e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 25 QPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALG 104
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 105 EVTATADTFEWMAEQGKRVYGRVVP-SRFTGVEQLV---VHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAE 180
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETIPfDASPGGEGRIgftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 181 ETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLlgLASAAMKKITLELGGHSPVI 260
Cdd:cd07149 161 QTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAI--ARKAGLKKVTLELGSNAAVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 261 VDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQEL 340
Cdd:cd07149 239 VDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEEW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 341 TDEAVKSGARLLCGGGEpvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTR 420
Cdd:cd07149 319 VEEAVEGGARLLTGGKR-----DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTN 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 736049070 421 SVESMQRLQGSLQAGSVSIN---TFAVTppELPFAGIKLSGMGVE 462
Cdd:cd07149 394 DLQKALKAARELEVGGVMINdssTFRVD--HMPYGGVKESGTGRE 436
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
47-478 |
7.54e-130 |
|
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: 383.35 E-value: 7.54e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 47 VEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRvYGR 126
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEA-FLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 127 VVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVL 206
Cdd:cd07100 80 DEPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 207 YGVPDMISRrLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQIC 286
Cdd:cd07100 160 LIDSDQVEA-IIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 287 HAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVnrrRQAAMQELT---DEAVKSGARLLCGGGEPVglGD 363
Cdd:cd07100 239 IAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLA---RKDLRDELHeqvEEAVAAGATLLLGGKRPD--GP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 364 GFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFA 443
Cdd:cd07100 314 GAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMV 393
|
410 420 430
....*....|....*....|....*....|....*
gi 736049070 444 VTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07100 394 KSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
10-475 |
9.76e-128 |
|
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: 379.15 E-value: 9.76e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 10 VDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQ 89
Cdd:TIGR01804 2 IDGEYVEDSAGT--TREIINPANGEVIATVHAATPEDVERAIAAARRAQGEWAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 90 ILTLEQGKTLPEAL-GEVTATADTFEWMAEQGKRVYGRVVPSRFTGvEQLVVHEPVGVIGAFSPWNYPMVLAARKVATAL 168
Cdd:TIGR01804 80 LETLDTGKTLQETIvADMDSGADVFEFFAGLAPALNGEIIPLGGPS-FAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 169 AAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKK 248
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 249 ITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPL 328
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 329 VNRRRQAAMQELTDEAVKSGARLLCGGGEP--VGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETA 406
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPenVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736049070 407 NNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIK 475
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
46-465 |
1.48e-127 |
|
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: 377.26 E-value: 1.48e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 46 DVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYG 125
Cdd:cd07104 1 DVDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 126 RVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETP---GVMIAiaRICMDEGLPSGT 202
Cdd:cd07104 81 EILPSDVPGKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPvtgGLLIA--EIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 203 LNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNA 282
Cdd:cd07104 159 LNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 283 GQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEpvglg 362
Cdd:cd07104 239 GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 363 DGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTF 442
Cdd:cd07104 314 EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINDQ 393
|
410 420
....*....|....*....|....
gi 736049070 443 AVT-PPELPFAGIKLSGMGVEMGE 465
Cdd:cd07104 394 TVNdEPHVPFGGVKASGGGRFGGP 417
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
27-478 |
2.26e-126 |
|
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: 375.42 E-value: 2.26e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAA-WKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGE 105
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGV 185
Cdd:cd07109 81 VEAAARYFEYYGGAADKLHGETIPLG-PGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDEtVQMGPLVNRRRQAAMQELTDEAV 345
Cdd:cd07109 240 DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGFVARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCGGGEPVG-LGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVES 424
Cdd:cd07109 319 ARGARIVAGGRIAEGaPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDR 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 736049070 425 MQRLQGSLQAGSVSINT-FAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07109 399 ALRVARRLRAGQVFVNNyGAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
27-479 |
7.37e-126 |
|
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: 374.27 E-value: 7.37e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWkTW--TALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALG 104
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTG-DWstDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 105 -EVTATADTFEWMAEQGKRVYGRVV----PSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPA 179
Cdd:cd07089 80 mQVDGPIGHLRYFADLADSFPWEFDlpvpALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 180 EETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPV 259
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 260 IVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQE 339
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 340 LTDEAVKSGARLLCGGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFT 419
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPAGLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 420 RSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
8-479 |
1.58e-124 |
|
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: 371.14 E-value: 1.58e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 8 LLVDGQWlgAEKNQRDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAA--WKTWTALERGRLLLRIASAIREQAR 85
Cdd:cd07139 1 LFIGGRW--VAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 86 SLAQILTLEQGKTLP-EALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKV 164
Cdd:cd07139 79 ELARLWTAENGMPISwSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 165 ATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPVGRHLLGLASA 244
Cdd:cd07139 159 APALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPADRE-VGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 245 AMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIV----HDSVADAFerefAKRAGQLRLGNGMD 320
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVprsrYDEVVEAL----AAAVAALKVGDPLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 321 ETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLE 400
Cdd:cd07139 314 PATQIGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDED 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736049070 401 QAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTpPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07139 394 DAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLD-FGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
8-479 |
1.78e-124 |
|
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: 370.68 E-value: 1.78e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 8 LLVDGQWLGAEKnqRDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSL 87
Cdd:cd07138 1 FYIDGAWVAPAG--TETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 88 AQILTLEQGKTLPEALG-EVTATADTFEWMAEQGKRvygrvvpsrFTGVEQ----LVVHEPVGVIGAFSPWNYPMVLAAR 162
Cdd:cd07138 79 AQAITLEMGAPITLARAaQVGLGIGHLRAAADALKD---------FEFEERrgnsLVVREPIGVCGLITPWNWPLNQIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 163 KVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLA 242
Cdd:cd07138 150 KVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 243 SAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDET 322
Cdd:cd07138 230 ADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 323 VQMGPLVNRRRQAAMQELTDEAVKSGARLLCGG-GEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQ 401
Cdd:cd07138 310 TTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpGRPEGLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDE 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 402 AIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTfAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07138 390 AIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQG 466
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
23-460 |
5.30e-124 |
|
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: 369.62 E-value: 5.30e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 23 DTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWkTWTAL---ERGRLLLRIASAIREQARSLAQILTLEQGKTL 99
Cdd:cd07112 2 ETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESG-VWSRLspaERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 100 PEAL-GEVTATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKP 178
Cdd:cd07112 81 SDALaVDVPSAANTFRWYAEAIDKVYGEVAPTG-PDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 179 AEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAA-MKKITLELGGHS 257
Cdd:cd07112 160 AEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWLECGGKS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 258 PVIVDRDVP-AERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAA 336
Cdd:cd07112 240 PNIVFADAPdLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 337 MQELTDEAVKSGARLLCGGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAY 416
Cdd:cd07112 320 VLGYIESGKAEGARLVAGGKRVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAAS 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 736049070 417 AFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMG 460
Cdd:cd07112 400 VWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNG 443
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
27-477 |
1.10e-123 |
|
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: 368.19 E-value: 1.10e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEAL-GE 105
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRdDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGV 185
Cdd:cd07092 81 LPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARIcMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:cd07092 161 TLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAv 345
Cdd:cd07092 240 DLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERA- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCGGGEPVglGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESM 425
Cdd:cd07092 319 PAHARVLTGGRRAE--GPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 736049070 426 QRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07092 397 MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
27-477 |
1.90e-123 |
|
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: 367.78 E-value: 1.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVYGRVVP---SRFTGVEQlvvhEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETP 183
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPlpgGSFAYTRR----EPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 184 GVMIAIARICMDEGLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDR 263
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGE-TGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 264 DVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDE 343
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 344 AVKSGARLLCGGGEPV---GLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTR 420
Cdd:cd07090 316 AKQEGAKVLCGGERVVpedGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 736049070 421 SVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
7-477 |
2.85e-122 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 365.39 E-value: 2.85e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEKnqrDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARS 86
Cdd:PRK13473 4 KLLINGELVAGEG---EKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 87 LAQILTLEQGKTLPEALG-EVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVA 165
Cdd:PRK13473 81 FARLESLNCGKPLHLALNdEIPAIVDVFRFFAGAARCLEGKAAGEYLEGHTSMIRRDPVGVVASIAPWNYPLMMAAWKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 166 TALAAGCTIVIKPAEETPGVMIAIARICMdEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAA 245
Cdd:PRK13473 161 PALAAGNTVVLKPSEITPLTALKLAELAA-DILPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAADS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 246 MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQM 325
Cdd:PRK13473 240 VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 326 GPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGlGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIET 405
Cdd:PRK13473 320 GPLISAAHRDRVAGFVERAKALGHIRVVTGGEAPD-GKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRW 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049070 406 ANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:PRK13473 399 ANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
26-462 |
6.16e-122 |
|
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: 363.98 E-value: 6.16e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 26 PVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGE 105
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVPSR-FTGVEQLVV---HEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEE 181
Cdd:cd07145 82 VERTIRLFKLAAEEAKVLRGETIPVDaYEYNERRIAftvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 182 TPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIV 261
Cdd:cd07145 162 TPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 262 DRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELT 341
Cdd:cd07145 242 LKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMENLV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 342 DEAVKSGARLLCGGGEPvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRS 421
Cdd:cd07145 322 NDAVEKGGKILYGGKRD----EGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTND 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 736049070 422 VESMQRLQGSLQAGSVSIN-TFAVTPPELPFAGIKLSGMGVE 462
Cdd:cd07145 398 INRALKVARELEAGGVVINdSTRFRWDNLPFGGFKKSGIGRE 439
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
27-468 |
1.06e-121 |
|
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: 363.42 E-value: 1.06e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEA-LGE 105
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLArTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGV 185
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:cd07093 160 AWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAV 345
Cdd:cd07093 240 DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVELAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCGGGEPV--GLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVE 423
Cdd:cd07093 320 AEGATILTGGGRPElpDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLG 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 736049070 424 SMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGL 468
Cdd:cd07093 400 RAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSL 444
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
28-477 |
2.49e-121 |
|
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: 362.43 E-value: 2.49e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 28 HNPATGELLGRLPMALEDDVEQAIEAAHRAFAA--WKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGE 105
Cdd:cd07118 2 RSPAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGV 185
Cdd:cd07118 82 IEGAADLWRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAV 345
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCGGGEpVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESM 425
Cdd:cd07118 322 AEGATLLLGGER-LASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 736049070 426 QRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
27-478 |
5.96e-120 |
|
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: 358.98 E-value: 5.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTL-PEALGE 105
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGV 185
Cdd:cd07108 81 AAVLADLFRYFGGLAGELKGETLPFG-PDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARICMDEgLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:cd07108 160 VLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAA-KFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEA 344
Cdd:cd07108 239 DLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYIDLG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 345 VK-SGARLLCGGGEPVG--LGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRS 421
Cdd:cd07108 319 LStSGATVLRGGPLPGEgpLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRD 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 422 VESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHF-HIKAVV 478
Cdd:cd07108 399 LGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEHFtQKKTVN 456
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
52-479 |
2.93e-119 |
|
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: 353.84 E-value: 2.93e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 52 EAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSR 131
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 132 FTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPD 211
Cdd:cd06534 81 DPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 212 MISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTR 291
Cdd:cd06534 161 EVGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 292 FIVHDSVADAFEREFakragqlrlgngmdetvqmgplvnrrrqaamqeltdeavksgarllcgggepvglgdgffwqATV 371
Cdd:cd06534 241 LLVHESIYDEFVEKL--------------------------------------------------------------VTV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 372 LADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAV-TPPELP 450
Cdd:cd06534 259 LVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAP 338
|
410 420 430
....*....|....*....|....*....|
gi 736049070 451 FAGIKLSGMGVEMGEEGLmDHF-HIKAVVR 479
Cdd:cd06534 339 FGGVKNSGIGREGGPYGL-EEYtRTKTVVI 367
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
4-479 |
6.59e-118 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 355.19 E-value: 6.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 4 PELKLLVDGQWLGAEKNQRdtQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAA-----WKTWTALERGRLLLRIAS 78
Cdd:PLN02467 6 PRRQLFIGGEWREPVLGKR--IPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 79 AIREQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQL---VVHEPVGVIGAFSPWNY 155
Cdd:PLN02467 84 KITERKSELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAEALDAKQKAPVSLPMETFkgyVLKEPLGVVGLITPWNY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 156 PMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVG 235
Cdd:PLN02467 164 PLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 236 RHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRL 315
Cdd:PLN02467 244 RKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 316 GNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSR 395
Cdd:PLN02467 324 SDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 396 FDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIK 475
Cdd:PLN02467 404 FSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVK 483
|
....
gi 736049070 476 AVVR 479
Cdd:PLN02467 484 QVTK 487
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
7-478 |
6.91e-118 |
|
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: 354.35 E-value: 6.91e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAF---AAWKTWTALERGRLLLRIASAIREQ 83
Cdd:cd07141 8 KIFINNEWHDSVSGK--TFPTINPATGEKICEVQEGDKADVDKAVKAARAAFklgSPWRTMDASERGRLLNKLADLIERD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 84 ARSLAQILTLEQGKTLPEA-LGEVTATADTFEWMAEQGKRVYGRVVPSR---FTgveqLVVHEPVGVIGAFSPWNYPMVL 159
Cdd:cd07141 86 RAYLASLETLDNGKPFSKSyLVDLPGAIKVLRYYAGWADKIHGKTIPMDgdfFT----YTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 160 AARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLL 239
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 240 GLASAA-MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNG 318
Cdd:cd07141 242 QAAGKSnLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 319 MDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPvglGD-GFFWQATVLADVGAGARAMHEEVFGPIALVSRFD 397
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRH---GDkGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 398 TLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07141 399 TIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
.
gi 736049070 478 V 478
Cdd:cd07141 479 T 479
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
6-477 |
8.28e-118 |
|
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: 354.41 E-value: 8.28e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 6 LKLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKT-WTALERGRLLLRIASAIREQA 84
Cdd:cd07144 8 TGLFINNEFVKSSDGE--TIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSkVTGEERGELLDKLADLVEKNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 85 RSLAQILTLEQGKTL-PEALGEVTATADTFEWMAEQGKRVYGRVVPsrfTGVEQL--VVHEPVGVIGAFSPWNYPMVLAA 161
Cdd:cd07144 86 DLLAAIEALDSGKPYhSNALGDLDEIIAVIRYYAGWADKIQGKTIP---TSPNKLayTLHEPYGVCGQIIPWNYPLAMAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 162 RKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGL 241
Cdd:cd07144 163 WKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 242 ASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQ-LRLGNGMD 320
Cdd:cd07144 243 AAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKVGSPFD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 321 ETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGG-GEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTL 399
Cdd:cd07144 323 DDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGeKAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTY 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 400 EQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07144 403 EEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
27-462 |
9.04e-117 |
|
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: 350.58 E-value: 9.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVYGRVVPS----RFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEET 182
Cdd:cd07094 83 DRAIDTLRLAAEEAERIRGEEIPLdatqGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 183 PGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLlgLASAAMKKITLELGGHSPVIVD 262
Cdd:cd07094 163 PLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEAL--RANAGGKRIALELGGNAPVIVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 263 RDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTD 342
Cdd:cd07094 241 RDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERWVE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 343 EAVKSGARLLCGGGEpvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSV 422
Cdd:cd07094 321 EAVEAGARLLCGGER-----DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 736049070 423 ESMQRLQGSLQAGSVSIN-TFAVTPPELPFAGIKLSGMGVE 462
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNdSSAFRTDWMPFGGVKESGVGRE 436
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
29-478 |
3.59e-116 |
|
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: 349.33 E-value: 3.59e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 29 NPATGELLGRLPMALEDDVEQAIEAAHRAF--AAWKTWTALeRGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:cd07120 3 DPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVM 186
Cdd:cd07120 82 SGAISELRYYAGLARTEAGRMIEPE-PGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 187 IAIARiCMDE--GLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRD 264
Cdd:cd07120 161 AAIIR-ILAEipSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 265 VPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEA 344
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 345 VKSGARLLCGGGEPV-GLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVE 423
Cdd:cd07120 320 IAAGAEVVLRGGPVTeGLAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 736049070 424 SMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07120 400 RAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
1-477 |
6.49e-116 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 349.56 E-value: 6.49e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 1 MTYPELKLLVDGQWLGAEKNqrDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAI 80
Cdd:PRK13252 2 SRQPLQSLYIDGAYVEATSG--ETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 81 REQARSLAQILTLEQGKTLPEAL-GEVTATADTFEWMAEQGKRVYGRVVPSR-----FTgveqlvVHEPVGVIGAFSPWN 154
Cdd:PRK13252 80 RERNDELAALETLDTGKPIQETSvVDIVTGADVLEYYAGLAPALEGEQIPLRggsfvYT------RREPLGVCAGIGAWN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 155 YPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPV 234
Cdd:PRK13252 154 YPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 235 GRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLR 314
Cdd:PRK13252 233 GKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 315 LGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGG--EPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIAL 392
Cdd:PRK13252 313 IGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGErlTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 393 VSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHF 472
Cdd:PRK13252 393 VLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYT 472
|
....*
gi 736049070 473 HIKAV 477
Cdd:PRK13252 473 QIKSV 477
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
9-477 |
8.43e-115 |
|
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: 346.64 E-value: 8.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 9 LVDGQWLGAEKNQRDTQpvHNPATG-ELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSL 87
Cdd:cd07131 2 YIGGEWVDSASGETFDS--RNPADLeEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 88 AQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATA 167
Cdd:cd07131 80 ARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 168 LAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMK 247
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 248 KITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGP 327
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 328 LVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGLG--DGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIET 405
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 736049070 406 ANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAV-TPPELPFAGIKLSGMGVEMGEEGLMDHF-HIKAV 477
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNAPTIgAEVHLPFGGVKKSGNGHREAGTTALDAFtEWKAV 473
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
26-469 |
1.12e-114 |
|
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: 345.38 E-value: 1.12e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 26 PVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGE 105
Cdd:cd07147 2 EVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVP----SRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEE 181
Cdd:cd07147 82 VARAIDTFRIAAEEATRIYGEVLPldisARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 182 TPGVMIAIARICMDEGLPSGTLNVLyGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAamKKITLELGGHSPVIV 261
Cdd:cd07147 162 TPLSALILGEVLAETGLPKGAFSVL-PCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 262 DRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELT 341
Cdd:cd07147 239 DSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 342 DEAVKSGARLLCGGGEpvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRS 421
Cdd:cd07147 319 NEAVDAGAKLLTGGKR-----DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 736049070 422 VESMQRLQGSLQAGSVSIN---TFAVTPpeLPFAGIKLSGMGVE--------MGEEGLM 469
Cdd:cd07147 394 LEKALRAWDELEVGGVVINdvpTFRVDH--MPYGGVKDSGIGREgvryaieeMTEPRLL 450
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
7-478 |
1.51e-114 |
|
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: 345.63 E-value: 1.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAF--AAWKTWTALERGRLLLRIASAIREQA 84
Cdd:cd07142 5 KLFINGQFVDAASGK--TFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFdeGPWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 85 RSLAQILTLEQGKTLPEA-LGEVTATADTFEWMAEQGKRVYGRVVPSrfTGVEQL-VVHEPVGVIGAFSPWNYPMVLAAR 162
Cdd:cd07142 83 DELAALETWDNGKPYEQArYAEVPLAARLFRYYAGWADKIHGMTLPA--DGPHHVyTLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 163 KVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLA 242
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 243 SAA-MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDE 321
Cdd:cd07142 241 AKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 322 TVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEpvgLGD-GFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLE 400
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDR---IGSkGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 401 QAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07142 398 EVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
12-460 |
9.36e-109 |
|
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: 330.42 E-value: 9.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 12 GQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQIL 91
Cdd:cd07151 1 GEWRDGTSER--TIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 92 TLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAG 171
Cdd:cd07151 79 IRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 172 CTIVIKPAEETP---GVMIAiaRICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKK 248
Cdd:cd07151 159 NAVVLKPASDTPitgGLLLA--KIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 249 ITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPL 328
Cdd:cd07151 237 VALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 329 VNRRRQAAMQELTDEAVKSGARLLCGGGEpvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANN 408
Cdd:cd07151 317 INESQVDGLLDKIEQAVEEGATLLVGGEA-----EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 736049070 409 VEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVT-PPELPFAGIKLSGMG 460
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNdEPHVPFGGEKNSGLG 444
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
8-477 |
1.12e-108 |
|
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: 331.03 E-value: 1.12e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 8 LLVDGQWLGAEKNQRDTqpVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAwkTW----TALERGRLLLRIASAIREQ 83
Cdd:cd07143 9 LFINGEFVDSVHGGTVK--VYNPSTGKLITKIAEATEADVDIAVEVAHAAFET--DWglkvSGSKRGRCLSKLADLMERN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 84 ARSLAQILTLEQGKTLPEALG-EVTATADTFEWMAEQGKRVYGRVV---PSRFTgveqLVVHEPVGVIGAFSPWNYPMVL 159
Cdd:cd07143 85 LDYLASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIetdIKKLT----YTRHEPIGVCGQIIPWNFPLLM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 160 AARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLL 239
Cdd:cd07143 161 CAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 240 GLASAA-MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNG 318
Cdd:cd07143 241 EAAAKSnLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 319 MDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPvglGD-GFFWQATVLADVGAGARAMHEEVFGPIALVSRFD 397
Cdd:cd07143 321 FAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRH---GNeGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 398 TLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07143 398 TEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
5-462 |
7.52e-108 |
|
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: 328.38 E-value: 7.52e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 5 ELKLLVDGQWlgaEKNQRDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAF-AAWKTWTALERGRLLLRIASAIREQ 83
Cdd:cd07082 1 QFKYLINGEW---KESSGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAGrGWWPTMPLEERIDCLHKFADLLKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 84 ARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFT----GVEQLVVHEPVGVIGAFSPWNYPMVL 159
Cdd:cd07082 78 KEEVANLLMWEIGKTLKDALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFpgtkGKIAQVRREPLGVVLAIGPFNYPLNL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 160 AARKVATALAAGCTIVIKPAeeTPGVMIAI--ARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRH 237
Cdd:cd07082 158 TVSKLIPALIMGNTVVFKPA--TQGVLLGIplAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 238 LlgLASAAMKKITLELGGHSPVIVDRDvpaervAELATAAK------FRNAGQICHAPTRFIVHDSVADAFEREFAKRAG 311
Cdd:cd07082 236 L--KKQHPMKRLVLELGGKDPAIVLPD------ADLELAAKeivkgaLSYSGQRCTAIKRVLVHESVADELVELLKEEVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 312 QLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGepvGLGDGFFWqATVLADVGAGARAMHEEVFGPIA 391
Cdd:cd07082 308 KLKVGMPWDNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG---REGGNLIY-PTLLDPVTPDMRLAWEEPFGPVL 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049070 392 LVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTF-AVTPPELPFAGIKLSGMGVE 462
Cdd:cd07082 384 PIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcQRGPDHFPFLGRKDSGIGTQ 455
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
8-477 |
1.40e-107 |
|
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: 327.86 E-value: 1.40e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 8 LLVDGQWLGAEKNQRDTqpVHNPATGELLGRLPMALEDDVEQAIEAAHRAF-AAWKTWTALERGRLLLRIASAIREQARS 86
Cdd:cd07113 2 HFIDGRPVAGQSEKRLD--ITNPATEQVIASVASATEADVDAAVASAWRAFvSAWAKTTPAERGRILLRLADLIEQHGEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 87 LAQILTLEQGKT--LPEALgEVTATADTFEWMAEQGKRVYGRV----VPS----RFTGVEQlvvHEPVGVIGAFSPWNYP 156
Cdd:cd07113 80 LAQLETLCSGKSihLSRAF-EVGQSANFLRYFAGWATKINGETlapsIPSmqgeRYTAFTR---REPVGVVAGIVPWNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 157 MVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPVGR 236
Cdd:cd07113 156 VMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 237 HLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLG 316
Cdd:cd07113 235 KIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 317 NGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVglGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRF 396
Cdd:cd07113 315 SPMDESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA--GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 397 DTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKA 476
Cdd:cd07113 393 EDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKS 472
|
.
gi 736049070 477 V 477
Cdd:cd07113 473 V 473
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
7-472 |
1.81e-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: 327.76 E-value: 1.81e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARS 86
Cdd:cd07559 2 DNFINGEWVAPSKGE--YFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 87 LAQILTLEQGKTLPEALG-EVTATADTFewmaeqgkRVYGRVVPSRFTGVEQL-------VVHEPVGVIGAFSPWNYPMV 158
Cdd:cd07559 80 LAVAETLDNGKPIRETLAaDIPLAIDHF--------RYFAGVIRAQEGSLSEIdedtlsyHFHEPLGVVGQIIPWNFPLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 159 LAARKVATALAAGCTIVIKPAEETPGVMIAIARIcMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHL 238
Cdd:cd07559 152 MAAWKLAPALAAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 239 LGLASAAMKKITLELGGHSPVIVDRDVPAE-----RVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQL 313
Cdd:cd07559 231 MQYAAENLIPVTLELGGKSPNIFFDDAMDAdddfdDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 314 RLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPV--GLGDGFFWQATVLADVGAGARAMHEEVFGPIA 391
Cdd:cd07559 311 KVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTlgGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 392 LVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEmGEEGLMDH 471
Cdd:cd07559 391 AVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRE-THKMMLDH 469
|
.
gi 736049070 472 F 472
Cdd:cd07559 470 Y 470
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
28-479 |
6.40e-107 |
|
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: 325.33 E-value: 6.40e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 28 HNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVT 107
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 108 ATADTFEWMAEQGKRVYG-RVVPSR--FTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPG 184
Cdd:cd07099 81 LALEAIDWAARNAPRVLApRKVPTGllMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 185 VMIAIARICMDEGLPSGTLNVLYGVPDmISRRLIASpKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRD 264
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGA-TGAALIDA-GVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 265 VPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEA 344
Cdd:cd07099 239 ADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 345 VKSGARLLCGGgePVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVES 424
Cdd:cd07099 319 VAKGAKALTGG--ARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 736049070 425 MQRLQGSLQAGSVSINTFAVTP--PELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07099 397 AEAIARRLEAGAVSINDVLLTAgiPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
27-477 |
1.54e-106 |
|
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: 324.71 E-value: 1.54e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVYGRVVPSRFTGVeQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVM 186
Cdd:cd07107 81 MVAAALLDYFAGLVTELKGETIPVGGRNL-HYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 187 IAIARIcMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVP 266
Cdd:cd07107 160 LRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 267 AERVAELATAA-KFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAV 345
Cdd:cd07107 239 PEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDSAK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCGGGEPVG--LGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVE 423
Cdd:cd07107 319 REGARLVTGGGRPEGpaLEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDIS 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 736049070 424 SMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07107 399 QAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
9-464 |
1.69e-106 |
|
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: 325.29 E-value: 1.69e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 9 LVDGQWLGaekNQRDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLA 88
Cdd:cd07086 2 VIGGEWVG---SGGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 89 QILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATAL 168
Cdd:cd07086 79 RLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 169 AAGCTIVIKPAEETPGVMIAIARICMD----EGLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPVGRHLLGLASA 244
Cdd:cd07086 159 VCGNTVVWKPSETTPLTAIAVTKILAEvlekNGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 245 AMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQ 324
Cdd:cd07086 238 RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 325 MGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIE 404
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736049070 405 TANNVEFGLAAYAFTRSVESMQRLQG--SLQAGSVSINtfavTPPE-----LPFAGIKLSGMGVEMG 464
Cdd:cd07086 398 INNDVPQGLSSSIFTEDLREAFRWLGpkGSDCGIVNVN----IPTSgaeigGAFGGEKETGGGRESG 460
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
27-464 |
3.35e-106 |
|
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: 323.54 E-value: 3.35e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAhraFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEV 106
Cdd:cd07146 3 VRNPYTGEVVGTVPAGTEEALREALALA---ASYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTRYEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVYGRVVPSRFTGVEQ----LVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEET 182
Cdd:cd07146 80 GRAADVLRFAAAEALRDDGESFSCDLTANGKarkiFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 183 PGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLglASAAMKKITLELGGHSPVIVD 262
Cdd:cd07146 160 PLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAIA--ATAGYKRQLLELGGNDPLIVM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 263 RDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTD 342
Cdd:cd07146 238 DDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 343 EAVKSGARLLCGGGEpvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSV 422
Cdd:cd07146 318 EAIAQGARVLLGNQR-----QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDL 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 736049070 423 ESMQRLQGSLQAGSVSINTfavTP----PELPFAGIKLSGMGVEMG 464
Cdd:cd07146 393 DTIKRLVERLDVGTVNVNE---VPgfrsELSPFGGVKDSGLGGKEG 435
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-460 |
2.02e-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: 323.41 E-value: 2.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 2 TYPelkLLVDGQWLGAEknqrDTQPVHNPA-TGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAI 80
Cdd:cd07124 32 EYP---LVIGGKEVRTE----EKIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 81 REQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLA 160
Cdd:cd07124 105 RRRRFELAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFPVEMV-PGEDNRYVYRPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 161 ARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLG 240
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 241 LAS------AAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLR 314
Cdd:cd07124 264 RAAkvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 315 LGNGMDETVQMGPLVNrrrQAAMQELTD--EAVKSGARLLCGGGEPVGLGDGFFWQATVLADVGAGARAMHEEVFGPIAL 392
Cdd:cd07124 344 VGDPEDPEVYMGPVID---KGARDRIRRyiEIGKSEGRLLLGGEVLELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLA 420
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049070 393 VSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAVtPPELPFAGIKLSGMG 460
Cdd:cd07124 421 VIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkiTGAL-VGRQPFGGFKMSGTG 490
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
7-472 |
2.53e-104 |
|
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: 319.40 E-value: 2.53e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEKNqrDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARS 86
Cdd:cd07117 2 GLFINGEWVKGSSG--ETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 87 LAQILTLEQGKTLPEALG-EVTATADTFEWMA-----EQGKRVygrVVPSRFTgveQLVVHEPVGVIGAFSPWNYPMVLA 160
Cdd:cd07117 80 LAMVETLDNGKPIRETRAvDIPLAADHFRYFAgviraEEGSAN---MIDEDTL---SIVLREPIGVVGQIIPWNFPFLMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 161 ARKVATALAAGCTIVIKPAEETPGVMIAIARIcMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHllg 240
Cdd:cd07117 154 AWKLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRD--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 241 LASAAMKKI---TLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGN 317
Cdd:cd07117 230 VAIAAAKKLipaTLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 318 GMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPV--GLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSR 395
Cdd:cd07117 310 PLDPDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIK 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736049070 396 FDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMgEEGLMDHF 472
Cdd:cd07117 390 FKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRET-HKSMLDAY 465
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
6-479 |
2.08e-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: 312.14 E-value: 2.08e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 6 LKLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQAR 85
Cdd:cd07085 1 LKLFINGEWVESKTTE--WLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 86 SLAQILTLEQGKTLPEALGEV--------TATADTFEWMAEqgkrvYGRVVPsrfTGVEQLVVHEPVGVIGAFSPWNYPM 157
Cdd:cd07085 79 ELARLITLEHGKTLADARGDVlrglevveFACSIPHLLKGE-----YLENVA---RGIDTYSYRQPLGVVAGITPFNFPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 158 VLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISrRLIASPKVAQLSFTGSVPVGRH 237
Cdd:cd07085 151 MIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVN-ALLDHPDIKAVSFVGSTPVGEY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 238 LLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGN 317
Cdd:cd07085 230 IYERAAANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 318 GMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPV--GLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSR 395
Cdd:cd07085 310 GDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKvpGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 396 FDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINT-FAVTPPELPFAGIKLSGMGVemgeeglmDHFHI 474
Cdd:cd07085 390 VDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVpIPVPLAFFSFGGWKGSFFGD--------LHFYG 461
|
....*
gi 736049070 475 KAVVR 479
Cdd:cd07085 462 KDGVR 466
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
46-468 |
2.62e-100 |
|
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: 307.58 E-value: 2.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 46 DVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYG 125
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 126 RVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNV 205
Cdd:cd07105 81 GSIPSDKPGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 206 LYGVPD---MISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNA 282
Cdd:cd07105 161 VTHSPEdapEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 283 GQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNgmdetVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGLG 362
Cdd:cd07105 241 GQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESPS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 363 DGFFwQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTF 442
Cdd:cd07105 316 GTSM-PPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINGM 394
|
410 420
....*....|....*....|....*..
gi 736049070 443 AV-TPPELPFAGIKLSGMGVEMGEEGL 468
Cdd:cd07105 395 TVhDEPTLPHGGVKSSGYGRFNGKWGI 421
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
4-468 |
3.08e-100 |
|
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: 309.33 E-value: 3.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 4 PELKLLVDGQWLGAEknQRDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQ 83
Cdd:cd07111 20 RSFGHFINGKWVKPE--NRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 84 ARSLAQILTLEQGKTLPEAL-GEVTATADTFEWMAEQGKrvygrvvpsrfTGVEQLVVHEPVGVIGAFSPWNYPMVLAAR 162
Cdd:cd07111 98 QRLFAVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQ-----------LLDTELAGWKPVGVVGQIVPWNFPLLMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 163 KVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRrLIASPKVAQLSFTGSVPVGRHLLGLA 242
Cdd:cd07111 167 KICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSFGSA-LANHPGVDKVAFTGSTEVGRALRRAT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 243 SAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDET 322
Cdd:cd07111 246 AGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 323 VQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVglGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQA 402
Cdd:cd07111 326 IDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP--SKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEA 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736049070 403 IETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGL 468
Cdd:cd07111 404 VALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGL 469
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
7-478 |
7.08e-100 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 310.20 E-value: 7.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAF--AAWKTWTALERGRLLLRIASAIREQA 84
Cdd:PLN02466 59 QLLINGQFVDAASGK--TFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFdeGPWPKMTAYERSRILLRFADLLEKHN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 85 RSLAQILTLEQGKTLPEALG-EVTATADTFEWMAEQGKRVYGRVVPSrfTGVEQL-VVHEPVGVIGAFSPWNYPMVLAAR 162
Cdd:PLN02466 137 DELAALETWDNGKPYEQSAKaELPMFARLFRYYAGWADKIHGLTVPA--DGPHHVqTLHEPIGVAGQIIPWNFPLLMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 163 KVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLA 242
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 243 SAA-MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDE 321
Cdd:PLN02466 295 AKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 322 TVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEpvgLGD-GFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLE 400
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDR---FGSkGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLD 451
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 401 QAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:PLN02466 452 EVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVV 529
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
29-477 |
2.34e-99 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 306.28 E-value: 2.34e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 29 NPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTA 108
Cdd:PRK09406 7 NPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAEALK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 109 TADTFEWMAEQGKRVYGRVvPSRFTGV---EQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGV 185
Cdd:PRK09406 87 CAKGFRYYAEHAEALLADE-PADAAAVgasRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARICMDEGLPSGTLNVLYgVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDV 265
Cdd:PRK09406 166 ALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 266 PAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAV 345
Cdd:PRK09406 245 DLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQVDDAV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 346 KSGARLLCGGGEPVglGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESM 425
Cdd:PRK09406 325 AAGATILCGGKRPD--GPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQ 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 736049070 426 QRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:PRK09406 403 ERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
7-477 |
2.73e-99 |
|
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: 306.73 E-value: 2.73e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEKNqrDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAF--AAWKTWTALERGRLLLRIASAIREQA 84
Cdd:cd07140 7 QLFINGEFVDAEGG--KTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFenGEWGKMNARDRGRLMYRLADLMEEHQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 85 RSLAQILTLEQGKTLPEALG-EVTATADTFEWMAEQGKRVYGRVVP---SRFTGVEQLVVHEPVGVIGAFSPWNYPMVLA 160
Cdd:cd07140 85 EELATIESLDSGAVYTLALKtHVGMSIQTFRYFAGWCDKIQGKTIPinqARPNRNLTLTKREPIGVCGIVIPWNYPLMML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 161 ARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLL- 239
Cdd:cd07140 165 AWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMk 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 240 GLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGM 319
Cdd:cd07140 245 SCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 320 DETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGE---PvglgdGFFWQATVLADVGAGARAMHEEVFGPIALVSRF 396
Cdd:cd07140 325 DRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQvdrP-----GFFFEPTVFTDVEDHMFIAKEESFGPIMIISKF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 397 DT--LEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHI 474
Cdd:cd07140 400 DDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKT 479
|
...
gi 736049070 475 KAV 477
Cdd:cd07140 480 KTV 482
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
73-477 |
4.96e-98 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 301.27 E-value: 4.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 73 LLRIASAIREQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSP 152
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 153 WNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSV 232
Cdd:PRK10090 81 WNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 233 PVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQ 312
Cdd:PRK10090 161 SAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 313 LRLGNGMD-ETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCgGGEPVGlGDGFFWQATVLADVGAGARAMHEEVFGPIA 391
Cdd:PRK10090 241 VQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVAL-GGKAVE-GKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 392 LVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDH 471
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEY 398
|
....*.
gi 736049070 472 FHIKAV 477
Cdd:PRK10090 399 LQTQVV 404
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
28-478 |
6.82e-97 |
|
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: 299.99 E-value: 6.82e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 28 HNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEA-LGEV 106
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDAsLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 107 TATADTFEWMAEQGKRVygrVVP-SRFTGVEQL-----VVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAE 180
Cdd:cd07098 81 LVTCEKIRWTLKHGEKA---LRPeSRPGGLLMFykrarVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 181 ET---PGVMIAIARICMDE-GLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGH 256
Cdd:cd07098 158 QVawsSGFFLSIIRECLAAcGHDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 257 SPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAA 336
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 337 MQELTDEAVKSGARLLCGGGEPVGLGD--GFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLA 414
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKRYPHPEYpqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736049070 415 AYAFTRSVESMQRLQGSLQAGSVSINTFAVT--PPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:cd07098 397 ASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
33-464 |
7.27e-97 |
|
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: 299.21 E-value: 7.27e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 33 GELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTATADT 112
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 113 FEWMAEQGKRVYGRVVPSRfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETP---GVMIAi 189
Cdd:cd07152 81 LHEAAGLPTQPQGEILPSA-PGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPvsgGVVIA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 190 aRICMDEGLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAER 269
Cdd:cd07152 159 -RLFEEAGLPAGVLHVLPGGAD-AGEALVEDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 270 VAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGA 349
Cdd:cd07152 237 AASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 350 RLLCGGGEpvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQ 429
Cdd:cd07152 317 RLEAGGTY-----DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 736049070 430 GSLQAGSVSINTFAVT-PPELPFAGIKLSGMGVEMG 464
Cdd:cd07152 392 DRLRTGMLHINDQTVNdEPHNPFGGMGASGNGSRFG 427
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
4-478 |
7.64e-95 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 295.96 E-value: 7.64e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 4 PEL---KLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAF--AAWKTWTALERGRLLLRIAS 78
Cdd:PLN02766 16 PEIkftKLFINGEFVDAASGK--TFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFdhGPWPRMSGFERGRIMMKFAD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 79 AIREQARSLAQILTLEQGKTLpeALG---EVTATADTFEWMAEQGKRVYGRVVpsRFTGVEQ-LVVHEPVGVIGAFSPWN 154
Cdd:PLN02766 94 LIEEHIEELAALDTIDAGKLF--ALGkavDIPAAAGLLRYYAGAADKIHGETL--KMSRQLQgYTLKEPIGVVGHIIPWN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 155 YPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPV 234
Cdd:PLN02766 170 FPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 235 GRHLLGLASAA-MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQL 313
Cdd:PLN02766 250 GRKIMQAAATSnLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDW 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 314 RLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGgEPVGlGDGFFWQATVLADVGAGARAMHEEVFGPIALV 393
Cdd:PLN02766 330 VVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGG-KPCG-DKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 394 SRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFH 473
Cdd:PLN02766 408 MKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQ 487
|
....*
gi 736049070 474 IKAVV 478
Cdd:PLN02766 488 VKSVV 492
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
28-472 |
2.37e-92 |
|
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: 287.99 E-value: 2.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 28 HNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVT 107
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 108 ATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMI 187
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 188 AIARICMDEGLPSGTLNVLYGvPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPA 267
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHL-SHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 268 ERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKS 347
Cdd:cd07102 240 DAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 348 GARLLCGGGE-PVGLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQ 426
Cdd:cd07102 320 GARALIDGALfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAE 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 736049070 427 RLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLmDHF 472
Cdd:cd07102 400 ALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGY-DQL 444
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
22-468 |
3.37e-92 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 289.86 E-value: 3.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 22 RDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPE 101
Cdd:PRK09407 31 GPTREVTAPFTGEPLATVPVSTAADVEAAFARARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 102 ALGEVTATADTFEWMAEQGKRVYGrvvPSRFTGVEQL-----VVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVI 176
Cdd:PRK09407 111 AFEEVLDVALTARYYARRAPKLLA---PRRRAGALPVltkttELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 177 KPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASpkVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGH 256
Cdd:PRK09407 188 KPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 257 SPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAA 336
Cdd:PRK09407 266 NPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLET 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 337 MQELTDEAVKSGARLLCGGGEPVGLGDgFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAY 416
Cdd:PRK09407 346 VSAHVDDAVAKGATVLAGGKARPDLGP-LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNAS 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 736049070 417 AFTRSVESMQRLQGSLQAGSVSIN-----TFAVTppELPFAGIKLSGMGVEMGEEGL 468
Cdd:PRK09407 425 VWTGDTARGRAIAARIRAGTVNVNegyaaAWGSV--DAPMGGMKDSGLGRRHGAEGL 479
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
28-477 |
2.79e-90 |
|
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: 282.66 E-value: 2.79e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 28 HNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVT 107
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAAQRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 108 ATADTfewmaeqgKRVYGRVVPS-----RFTGV-----EQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIK 177
Cdd:cd07101 81 DVAIV--------ARYYARRAERllkprRRRGAipvltRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 178 PAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASpkVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHS 257
Cdd:cd07101 153 PDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 258 PVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAM 337
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 338 QELTDEAVKSGARLLCGGGEPVGLGDgFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYA 417
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRARPDLGP-YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736049070 418 FTRSVESMQRLQGSLQAGSVSIN---TFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:cd07101 390 WTRDGARGRRIAARLRAGTVNVNegyAAAWASIDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
29-477 |
1.11e-89 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 281.36 E-value: 1.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 29 NPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTA 108
Cdd:PRK13968 13 NPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEVAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 109 TADTFEWMAEQGKRVYgRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIA 188
Cdd:PRK13968 93 SANLCDWYAEHGPAML-KAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 189 IARICMDEGLPSGTLNVLYGVPDMISRrLIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAE 268
Cdd:PRK13968 172 IAQVFKDAGIPQGVYGWLNADNDGVSQ-MINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 269 RVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSG 348
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 349 ARLLCgGGEPVGlGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRL 428
Cdd:PRK13968 331 ARLLL-GGEKIA-GAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQM 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 736049070 429 QGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAV 477
Cdd:PRK13968 409 AARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-458 |
5.75e-86 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 273.35 E-value: 5.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 2 TYPelkLLVDGQWLGAEknqrDTQPVHNPA-TGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAI 80
Cdd:PRK03137 36 DYP---LIIGGERITTE----DKIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAII 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 81 REQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQ------GKRVYGRvvpsrfTGVEQLVVHEPVGVIGAFSPWN 154
Cdd:PRK03137 109 RRRKHEFSAWLVKEAGKPWAEADADTAEAIDFLEYYARQmlkladGKPVESR------PGEHNRYFYIPLGVGVVISPWN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 155 YPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPV 234
Cdd:PRK03137 183 FPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 235 GRHLLGLASAA------MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAK 308
Cdd:PRK03137 263 GLRIYERAAKVqpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 309 RAGQLRLGNGMDETVqMGPLVNrrrQAAMQELTD--EAVKSGARLLCGGGEpvGLGDGFFWQATVLADVGAGARAMHEEV 386
Cdd:PRK03137 343 LTKELTVGNPEDNAY-MGPVIN---QASFDKIMSyiEIGKEEGRLVLGGEG--DDSKGYFIQPTIFADVDPKARIMQEEI 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736049070 387 FGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAVTPPElPFAGIKLSG 458
Cdd:PRK03137 417 FGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgcTGAIVGYH-PFGGFNMSG 490
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
27-469 |
1.17e-82 |
|
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: 262.74 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 27 VHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTW-TALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGE 105
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDRNNWlPAHERIAILERLADLMEERADELALLIAREGGKPLVDAKVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 106 VTATADTFEWMAEQGKRVYGRVVPSRFT----GVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEE 181
Cdd:cd07148 83 VTRAIDGVELAADELGQLGGREIPMGLTpasaGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 182 TPGVMIAIARICMDEGLPSGTLNVLygVPDM-ISRRLIASPKVAQLSFTGSVPVGRHLLGLAsAAMKKITLELGGHSPVI 260
Cdd:cd07148 163 TPLSCLAFVDLLHEAGLPEGWCQAV--PCENaVAEKLVTDPRVAFFSFIGSARVGWMLRSKL-APGTRCALEHGGAAPVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 261 VDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQEL 340
Cdd:cd07148 240 VDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVEEW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 341 TDEAVKSGARLLCGGGEpvgLGDGFFwQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTR 420
Cdd:cd07148 320 VNEAVAAGARLLCGGKR---LSDTTY-APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTK 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 421 SVESMQRLQGSLQAGSVSIN---TFAVTppELPFAGIKLSGMGV--------EMGEEGLM 469
Cdd:cd07148 396 DLDVALKAVRRLDATAVMVNdhtAFRVD--WMPFAGRRQSGYGTggipytmhDMTQEKMA 453
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
5-460 |
2.52e-80 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 257.90 E-value: 2.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 5 ELKLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAF--AAWKTWTALERGRLLLRIASAIRE 82
Cdd:PRK09847 19 ENRLFINGEYTAAAENE--TFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFerGDWSLSSPAKRKAVLNKLADLMEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 83 QARSLAQILTLEQGKTLPEAL-GEVTATADTFEWMAEQGKRVYGRVVPsrfTGVEQL--VVHEPVGVIGAFSPWNYPMVL 159
Cdd:PRK09847 97 HAEELALLETLDTGKPIRHSLrDDIPGAARAIRWYAEAIDKVYGEVAT---TSSHELamIVREPVGVIAAIVPWNFPLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 160 AARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLL 239
Cdd:PRK09847 174 TCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 240 GLASAA-MKKITLELGGHSPVIVDRDVPAERVAELATAAK-FRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGN 317
Cdd:PRK09847 254 KDAGDSnMKRVWLEAGGKSANIVFADCPDLQQAASATAAGiFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 318 GMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCG--GGEPVGLGdgffwqATVLADVGAGARAMHEEVFGPIALVSR 395
Cdd:PRK09847 334 PLDPATTMGTLIDCAHADSVHSFIREGESKGQLLLDGrnAGLAAAIG------PTIFVDVDPNASLSREEIFGPVLVVTR 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736049070 396 FDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMG 460
Cdd:PRK09847 408 FTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNG 472
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
10-472 |
8.27e-80 |
|
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: 256.22 E-value: 8.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 10 VDGQWLGAEKNQRDTQPvhNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQ 89
Cdd:cd07116 5 IGGEWVAPVKGEYFDNI--TPVTGKVFCEVPRSTAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 90 ILTLEQGKTLPEALG-EVTATADTFewmaeqgkRVYGRVVPSRFTGVEQL-------VVHEPVGVIGAFSPWNYPMVLAA 161
Cdd:cd07116 83 AETWDNGKPVRETLAaDIPLAIDHF--------RYFAGCIRAQEGSISEIdentvayHFHEPLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 162 RKVATALAAGCTIVIKPAEETPGVMIAIARICMDEgLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGL 241
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 242 ASAAMKKITLELGGHSPVIVDRDVPAERVAELATA----AKFR-NAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLG 316
Cdd:cd07116 234 ASENIIPVTLELGGKSPNIFFADVMDADDAFFDKAlegfVMFAlNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 317 NGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGG--GEPVGLGDGFFWQATVLADvGAGARAMHEEVFGPIALVS 394
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGerNELGGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 395 RFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTPPELPFAGIKLSGMGVEmGEEGLMDHF 472
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRE-NHKMMLDHY 469
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
9-436 |
1.67e-73 |
|
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: 239.42 E-value: 1.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 9 LVDGQWLGAEKnqrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLA 88
Cdd:cd07130 2 VYDGEWGGGGG----VVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 89 QILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATAL 168
Cdd:cd07130 78 KLVSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHRMMEQWNPLGVVGVITAFNFPVAVWGWNAAIAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 169 AAGCTIVIKPAEETPGVMIA----IARICMDEGLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPVGRHLLGLASA 244
Cdd:cd07130 158 VCGNVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCGGAD-VGEALVKDPRVPLVSFTGSTAVGRQVGQAVAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 245 AMKKITLELGGHSPVIVDRD------VPAERVAELATaakfrnAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNG 318
Cdd:cd07130 237 RFGRSLLELGGNNAIIVMEDadldlaVRAVLFAAVGT------AGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 319 MDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGgePVGLGDGFFWQATVlADVGAGARAMHEEVFGPIALVSRFDT 398
Cdd:cd07130 311 LDDGTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGG--KVIDGPGNYVEPTI-VEGLSDAPIVKEETFAPILYVLKFDT 387
|
410 420 430
....*....|....*....|....*....|....*...
gi 736049070 399 LEQAIETANNVEFGLAAYAFTRSVESMQRLQGslQAGS 436
Cdd:cd07130 388 LEEAIAWNNEVPQGLSSSIFTTDLRNAFRWLG--PKGS 423
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
16-464 |
3.47e-67 |
|
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: 224.38 E-value: 3.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 16 GAEKNQRDTQPVHNPATGE-LLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLE 94
Cdd:cd07125 39 GEETETGEGAPVIDPADHErTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 95 QGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTI 174
Cdd:cd07125 119 AGKTLADADAEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLELHGRGVFVCISPWNFPLAIFTGQIAAALAAGNTV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 175 VIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLG-LASAAMKKITL-- 251
Cdd:cd07125 199 IAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRaLAERDGPILPLia 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 252 ELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNR 331
Cdd:cd07125 279 ETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDK 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 332 RRQAAMQELTDEAVKSgARLLCggGEPVGLGDGFFWQATVLADVGAGarAMHEEVFGPIALVSRFD--TLEQAIETANNV 409
Cdd:cd07125 359 PAGKLLRAHTELMRGE-AWLIA--PAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFKaeDLDEAIEDINAT 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 410 EFGLAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAVTPPElPFAGIKLSGMGVEMG 464
Cdd:cd07125 434 GYGLTLGIHSRDEREIEYWRERVEAGNLYINrniTGAIVGRQ-PFGGWGLSGTGPKAG 490
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
46-458 |
2.85e-64 |
|
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: 214.06 E-value: 2.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 46 DVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEALGEVTATADTFEW-MAEQGKRVY 124
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGKIDIsIKAYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 125 GRVVPSRFtgVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLN 204
Cdd:cd07095 81 ERATPMAQ--GRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 205 VLYGVPDmISRRLIASPKVAQLSFTGSVPVGRHL-LGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAG 283
Cdd:cd07095 159 LVQGGRE-TGEALAAHEGIDGLLFTGSAATGLLLhRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 284 QICHAPTRFIVHDS-VADAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEAVKSGARLLcGGGEPVGLG 362
Cdd:cd07095 238 QRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPL-LAMERLVAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 363 DGFFWQAtvLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN-- 440
Cdd:cd07095 317 TAFLSPG--IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrp 394
|
410
....*....|....*....
gi 736049070 441 -TFAvtPPELPFAGIKLSG 458
Cdd:cd07095 395 tTGA--SSTAPFGGVGLSG 411
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
49-479 |
1.12e-63 |
|
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: 212.86 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 49 QAIEAAHRA-FAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKtlPEAlgEVTAT---------ADTF----E 114
Cdd:cd07134 1 RRVFAAQQAhALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRK--PAA--EVDLTeilpvlseiNHAIkhlkK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 115 WMAeqGKRVYgrvVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARIcM 194
Cdd:cd07134 77 WMK--PKRVR---TPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKI-I 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 195 DEGLPSGTLNVLYGVPDmISRRLIASPkVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELA 274
Cdd:cd07134 151 REAFDEDEVAVFEGDAE-VAQALLELP-FDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 275 TAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKragQLRLGNGMDETVQMGP----LVNRRRQAAMQELTDEAVKSGAR 350
Cdd:cd07134 229 AWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKA---EIEKFYGKDAARKASPdlarIVNDRHFDRLKGLLDDAVAKGAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 351 LLCGGGEPVglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQG 430
Cdd:cd07134 306 VEFGGQFDA---AQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLA 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 736049070 431 SLQAGSVSINTFAV--TPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07134 383 RTSSGGVVVNDVVLhfLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
4-460 |
1.44e-63 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 216.92 E-value: 1.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 4 PELKLLVDGQWLgaEKNQRDTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQ 83
Cdd:PLN02419 112 PRVPNLIGGSFV--ESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKN 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 84 ARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARK 163
Cdd:PLN02419 190 MDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWM 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 164 VATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISrRLIASPKVAQLSFTGSVPVGRHLLGLAS 243
Cdd:PLN02419 270 FPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 244 AAMKKITLELGG--HSPVIVDRDVPAERVAELatAAKFRNAGQICHA-PTRFIVHDsvADAFEREFAKRAGQLRLGNGMD 320
Cdd:PLN02419 349 AKGKRIQSNMGAknHGLVLPDANIDATLNALL--AAGFGAAGQRCMAlSTVVFVGD--AKSWEDKLVERAKALKVTCGSE 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 321 ETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPV--GLGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDT 398
Cdd:PLN02419 425 PDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVvpGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANS 504
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 736049070 399 LEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAVTP-PELPFAGIKLSGMG 460
Cdd:PLN02419 505 FDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPlPFFSFTGNKASFAG 567
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
8-464 |
1.60e-63 |
|
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: 213.98 E-value: 1.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 8 LLVDGQWLGAEKNQRDTQPVhnpATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSL 87
Cdd:cd07083 21 LVIGGEWVDTKERMVSVSPF---APSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRREL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 88 AQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGR-VVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVAT 166
Cdd:cd07083 98 IATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRLRYPaVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 167 ALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHL------LG 240
Cdd:cd07083 178 PVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIyeaaarLA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 241 LASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMD 320
Cdd:cd07083 258 PGQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 321 ETVQMGPLVNRRRQAAMQELTDEAvKSGARLLCGGGEPVglGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRF--DT 398
Cdd:cd07083 338 NGTDLGPVIDAEQEAKVLSYIEHG-KNEGQLVLGGKRLE--GEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYkdDD 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736049070 399 LEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAVTPPElPFAGIKLSGMGVEMG 464
Cdd:cd07083 415 FAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINrkiTGALVGVQ-PFGGFKLSGTNAKTG 482
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
45-479 |
3.10e-63 |
|
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: 211.69 E-value: 3.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 45 DDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEA-LGEVTATADTFEWMAE----- 118
Cdd:cd07135 5 DEIDSIHSRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETlLTEVSGVKNDILHMLKnlkkw 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 119 -QGKRVYGRVVPSRFTGVEqlVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICmDEG 197
Cdd:cd07135 85 aKDEKVKDGPLAFMFGKPR--IRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELV-PKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 198 LPSGTLNVLYG-VPDMisRRLIASpKVAQLSFTGSVPVGRHLlglASAAMKKIT---LELGGHSPVIVDRDvpaervAEL 273
Cdd:cd07135 162 LDPDAFQVVQGgVPET--TALLEQ-KFDKIFYTGSGRVGRII---AEAAAKHLTpvtLELGGKSPVIVTKN------ADL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 274 ATAA------KFRNAGQICHAPTRFIVHDSVADAFeREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDeavKS 347
Cdd:cd07135 230 ELAAkrilwgKFGNAGQICVAPDYVLVDPSVYDEF-VEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLD---TT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 348 GARLLCGGGEpvGLGDGFFwQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQR 427
Cdd:cd07135 306 KGKVVIGGEM--DEATRFI-PPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDH 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 736049070 428 LQGSLQAGSVSIN--TFAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07135 383 ILTRTRSGGVVINdtLIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVVK 436
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
69-479 |
4.09e-63 |
|
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: 210.85 E-value: 4.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 69 RGRLLLRIASAIREQARSLAQILTLEQGKTLPEA--------LGEVTATADTF-EWMAEqgKRVYgrvVPSRFTGVEQLV 139
Cdd:cd07087 22 RKAQLKALKRMLTENEEEIAAALYADLGKPPAEAylteiavvLGEIDHALKHLkKWMKP--RRVS---VPLLLQPAKAYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 140 VHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICmDEGLPSGTLNVLYGVPDmISRRLIA 219
Cdd:cd07087 97 IPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLI-PKYFDPEAVAVVEGGVE-VATALLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 220 SPkVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRD----VPAERVAelatAAKFRNAGQICHAPTRFIVH 295
Cdd:cd07087 175 EP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDanleVAARRIA----WGKFLNAGQTCIAPDYVLVH 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 296 DSVADAFEREFaKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDeavksGARLLCGGGepVGLGDGFFwQATVLADV 375
Cdd:cd07087 250 ESIKDELIEEL-KKAIKEFYGEDPKESPDYGRIINERHFDRLASLLD-----DGKVVIGGQ--VDKEERYI-APTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 376 GAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN--TFAVTPPELPFAG 453
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNdvLLHAAIPNLPFGG 400
|
410 420
....*....|....*....|....*..
gi 736049070 454 IKLSGMGVEMGEEGLmDHF-HIKAVVR 479
Cdd:cd07087 401 VGNSGMGAYHGKAGF-DTFsHLKSVLK 426
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
65-479 |
4.95e-57 |
|
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: 195.01 E-value: 4.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 65 TALERGRLLLRIASAIREQARSLAQILTLEQGK------TLPEALGEVTATADTF----EWMAEQGkrvygRVVPSRFTG 134
Cdd:cd07133 18 SLEERRDRLDRLKALLLDNQDALAEAISADFGHrsrhetLLAEILPSIAGIKHARkhlkKWMKPSR-----RHVGLLFLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 135 VEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICmDEGLPSGTLNVLYGVPDmis 214
Cdd:cd07133 93 AKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELL-AEYFDEDEVAVVTGGAD--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 215 rrliaspkVAQ---------LSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQI 285
Cdd:cd07133 169 --------VAAafsslpfdhLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 286 CHAPTRFIVHDSVADAFEREFAKRAGQL--RLGNGMDETvqmgPLVNRRRQAAMQELTDEAVKSGARLLCGGGEPVGLGD 363
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKMypTLADNPDYT----SIINERHYARLQGLLEDARAKGARVIELNPAGEDFAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 364 GFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN--T 441
Cdd:cd07133 317 TRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINdtL 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 736049070 442 FAVTPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07133 397 LHVAQDDLPFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
8-458 |
6.86e-54 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 188.24 E-value: 6.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 8 LLVDGQWLGAEKNQRDTqpvHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSL 87
Cdd:PRK09457 3 LWINGDWIAGQGEAFES---RNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 88 AQILTLEQGKTLPEALGEVTATADTFEW-MAEQGKRVYGRVVPSrfTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVAT 166
Cdd:PRK09457 80 AEVIARETGKPLWEAATEVTAMINKIAIsIQAYHERTGEKRSEM--ADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 167 ALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMiSRRLIASPKVAQLSFTGSVPVGrHLLG--LASA 244
Cdd:PRK09457 158 ALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQGGRET-GKALAAHPDIDGLLFTGSANTG-YLLHrqFAGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 245 AMKKITLELGGHSPVIVDRdvpaerVAELATAA------KFRNAGQICHAPTRFIVHDSV-ADAFEREFAKRAGQLRLGN 317
Cdd:PRK09457 236 PEKILALEMGGNNPLVIDE------VADIDAAVhliiqsAFISAGQRCTCARRLLVPQGAqGDAFLARLVAVAKRLTVGR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 318 GMDETVQ-MGPLVNRRRQAAMqeltdeaVKSGARLLCGGGEP------VGLGDGFFWQAtvLADVGAGARAMHEEVFGPI 390
Cdd:PRK09457 310 WDAEPQPfMGAVISEQAAQGL-------VAAQAQLLALGGKSllemtqLQAGTGLLTPG--IIDVTGVAELPDEEYFGPL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049070 391 ALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAvtPPELPFAGIKLSG 458
Cdd:PRK09457 381 LQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVNWNkplTGA--SSAAPFGGVGASG 449
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
139-482 |
8.72e-53 |
|
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: 184.24 E-value: 8.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 139 VVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICmDEGLPSGTLNVLYGVPDmISRRLI 218
Cdd:cd07136 96 IYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKII-EETFDEEYVAVVEGGVE-ENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 219 ASpKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDvpaervAELATAA------KFRNAGQICHAPTRF 292
Cdd:cd07136 174 DQ-KFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDED------ANLKLAAkrivwgKFLNAGQTCVAPDYV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 293 IVHDSVADAFEREFAKragQLRLGNGMD--ETVQMGPLVNRR---RQAAMqeLTDEAVKSGarllcGGGEPvglgDGFFW 367
Cdd:cd07136 247 LVHESVKEKFIKELKE---EIKKFYGEDplESPDYGRIINEKhfdRLAGL--LDNGKIVFG-----GNTDR----ETLYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 368 QATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN--TFAVT 445
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINdtIMHLA 392
|
330 340 350
....*....|....*....|....*....|....*...
gi 736049070 446 PPELPFAGIKLSGMGVEMGEEGLmDHF-HIKAVVRSGT 482
Cdd:cd07136 393 NPYLPFGGVGNSGMGSYHGKYSF-DTFsHKKSILKKST 429
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
136-483 |
9.47e-51 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 179.84 E-value: 9.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 136 EQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICmDEGLPSGTLNVLYG-VPDMIS 214
Cdd:PTZ00381 102 KSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLL-TKYLDPSYVRVIEGgVEVTTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 215 rrlIASPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIV 294
Cdd:PTZ00381 181 ---LLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 295 HDSVADAFEREFaKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEavkSGARLLCGGgePVGLGDGFFwQATVLAD 374
Cdd:PTZ00381 258 HRSIKDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGG--EVDIENKYV-APTIIVN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 375 VGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN--TFAVTPPELPFA 452
Cdd:PTZ00381 331 PDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFG 410
|
330 340 350
....*....|....*....|....*....|..
gi 736049070 453 GIKLSGMGVEMGEEGLmDHF-HIKAVVRSGTI 483
Cdd:PTZ00381 411 GVGNSGMGAYHGKYGF-DTFsHPKPVLNKSTG 441
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
7-460 |
4.03e-50 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 178.41 E-value: 4.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 7 KLLVDGQWLGAEKNQrdTQPVHNPATGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARS 86
Cdd:PLN00412 17 KYYADGEWRTSSSGK--SVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 87 LAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGR---VVPSRFTGVEQ----LVVHEPVGVIGAFSPWNYPMVL 159
Cdd:PLN00412 95 IAECLVKEIAKPAKDAVTEVVRSGDLISYTAEEGVRILGEgkfLVSDSFPGNERnkycLTSKIPLGVVLAIPPFNYPVNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 160 AARKVATALAAGCTIVIKPAeeTPGVMIAIARI-CMD-EGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTG---SVPV 234
Cdd:PLN00412 175 AVSKIAPALIAGNAVVLKPP--TQGAVAALHMVhCFHlAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGgdtGIAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 235 GRhllglaSAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLR 314
Cdd:PLN00412 253 SK------KAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 315 LGNGMDETvQMGPLVNRRRQAAMQELTDEAVKSGARLLcgggEPVGLGDGFFWqATVLADVGAGARAMHEEVFGPIALVS 394
Cdd:PLN00412 327 VGPPEDDC-DITPVVSESSANFIEGLVMDAKEKGATFC----QEWKREGNLIW-PLLLDNVRPDMRIAWEEPFGPVLPVI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 736049070 395 RFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTF-AVTPPELPFAGIKLSGMG 460
Cdd:PLN00412 401 RINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIG 467
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
23-460 |
1.66e-47 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 176.54 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 23 DTQPVHNPA-TGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPE 101
Cdd:PRK11904 562 EARPVVSPAdRRRVVGEVAFADAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQD 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 102 ALGEVTATADTFEWMAEQGKRVYG--RVVPSrFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPA 179
Cdd:PRK11904 642 AIAEVREAVDFCRYYAAQARRLFGapEKLPG-PTGESNELRLHGRGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPA 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 180 EETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHL-LGLASAAMKKITL--ELGGH 256
Cdd:PRK11904 721 EQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTLAARDGPIVPLiaETGGQ 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 257 SPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNrrrQAA 336
Cdd:PRK11904 801 NAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVID---AEA 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 337 MQELTD--EAVKSGARLLCGGGEPVGLGDGFFWqATVLADVGaGARAMHEEVFGPIALVSRFDT--LEQAIETANNVEFG 412
Cdd:PRK11904 878 KANLDAhiERMKREARLLAQLPLPAGTENGHFV-APTAFEID-SISQLEREVFGPILHVIRYKAsdLDKVIDAINATGYG 955
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 736049070 413 LAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAVTPPElPFAGIKLSGMG 460
Cdd:PRK11904 956 LTLGIHSRIEETADRIADRVRVGNVYVNrnqIGAVVGVQ-PFGGQGLSGTG 1005
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
10-473 |
7.92e-47 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 169.63 E-value: 7.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 10 VDGQWLGAEKNQRDTQPVHNPATGELLgrlpMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQ 89
Cdd:PLN02315 25 VGGEWRANGPLVSSVNPANNQPIAEVV----EASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 90 ILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALA 169
Cdd:PLN02315 101 LVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIALV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 170 AGCTIVIKPAEETPGVMIAIARICMD----EGLPSGTLNVLYGVPDmISRRLIASPKVAQLSFTGSVPVGRHLLGLASAA 245
Cdd:PLN02315 181 CGNCVVWKGAPTTPLITIAMTKLVAEvlekNNLPGAIFTSFCGGAE-IGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNAR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 246 MKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQM 325
Cdd:PLN02315 260 FGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 326 GPLVNRRRQAAMQELTDEAVKSGARLLCGGGepVGLGDGFFWQATVLaDVGAGARAMHEEVFGPIALVSRFDTLEQAIET 405
Cdd:PLN02315 340 GPLHTPESKKNFEKGIEIIKSQGGKILTGGS--AIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEI 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 736049070 406 ANNVEFGLAAYAFTRSVESMQRLQGSLQA--GSVSINtFAVTPPEL--PFAGIKLSGMGVEMGEEGLMDHFH 473
Cdd:PLN02315 417 NNSVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVN-IPTNGAEIggAFGGEKATGGGREAGSDSWKQYMR 487
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
15-460 |
5.29e-46 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 171.97 E-value: 5.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 15 LGAEKNQRDTQPVHNPA-TGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTL 93
Cdd:PRK11905 559 LAGGDVDGGTRPVLNPAdHDDVVGTVTEASAEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVR 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 94 EQGKTLPEALGEVTATADTFEWMAEQGKRvygrvvpsrftgVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCT 173
Cdd:PRK11905 639 EAGKTLANAIAEVREAVDFLRYYAAQARR------------LLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNT 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 174 IVIKPAEETPgvMIAIA--RICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLG-LASAAMKKIT 250
Cdd:PRK11905 707 VLAKPAEQTP--LIAARavRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRtLAKRSGPPVP 784
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 251 L--ELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFeREFAKRA-GQLRLGNGMDETVQMGP 327
Cdd:PRK11905 785 LiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRV-LTMLKGAmDELRIGDPWRLSTDVGP 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 328 LVNrrrQAAMQELTD--EAVKSGARLLCGGGEPVGLGDGFFWQATVLaDVGaGARAMHEEVFGPIALVSRF--DTLEQAI 403
Cdd:PRK11905 864 VID---AEAQANIEAhiEAMRAAGRLVHQLPLPAETEKGTFVAPTLI-EID-SISDLEREVFGPVLHVVRFkaDELDRVI 938
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 404 ETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAVTPPElPFAGIKLSGMG 460
Cdd:PRK11905 939 DDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniIGAVVGVQ-PFGGEGLSGTG 997
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
16-464 |
8.31e-46 |
|
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: 166.62 E-value: 8.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 16 GAEKNQRDTQPVHNPAT-GELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLE 94
Cdd:TIGR01238 44 HSYKADGEAQPVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVRE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 95 QGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVpsrftgveqlvvHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTI 174
Cdd:TIGR01238 124 AGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFS------------VESRGVFVCISPWNFPLAIFTGQISAALAAGNTV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 175 VIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHL---LGLASAAMKKITL 251
Cdd:TIGR01238 192 IAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLInqtLAQREDAPVPLIA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 252 ELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDETVQMGPLVNR 331
Cdd:TIGR01238 272 ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDA 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 332 RrqaAMQELTD--EAVKSGARLLcgggEPVGLGDGFFWQ-----ATVLADVGAGArAMHEEVFGPIALVSRF--DTLEQA 402
Cdd:TIGR01238 352 E---AKQNLLAhiEHMSQTQKKI----AQLTLDDSRACQhgtfvAPTLFELDDIA-ELSEEVFGPVLHVVRYkaRELDQI 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736049070 403 IETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAVTPPElPFAGIKLSGMGVEMG 464
Cdd:TIGR01238 424 VDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNrnqVGAVVGVQ-PFGGQGLSGTGPKAG 487
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
47-479 |
7.11e-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: 159.88 E-value: 7.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 47 VEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEA-LGEVTATADTF--------EWMA 117
Cdd:cd07137 1 APRLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESfRDEVSVLVSSCklaikelkKWMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 118 EQGKRVYGRVVPSRFTgveqlVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARIcMDEG 197
Cdd:cd07137 81 PEKVKTPLTTFPAKAE-----IVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 198 LPSGTLNVLYGVPDMISRRLiaSPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAA 277
Cdd:cd07137 155 LDTKAIKVIEGGVPETTALL--EQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 278 KF-RNAGQICHAPTRFIVHDSVA----DAFEREFAKRAGQLRLgngmdETVQMGPLVNRRRQAAMQELTDEAvKSGARLL 352
Cdd:cd07137 233 KWgCNNGQACIAPDYVLVEESFAptliDALKNTLEKFFGENPK-----ESKDLSRIVNSHHFQRLSRLLDDP-SVADKIV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 353 CGGGEPvglGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSL 432
Cdd:cd07137 307 HGGERD---EKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAET 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 736049070 433 QAGSVSINTFAV--TPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:cd07137 384 SSGGVTFNDTVVqyAIDTLPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
15-460 |
7.76e-43 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 162.84 E-value: 7.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 15 LGAEKNQRDTQPVHNPA-TGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTL 93
Cdd:PRK11809 651 LEDPVAAGEMSPVINPAdPRDIVGYVREATPAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVR 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 94 EQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVVpsrftgveqlvvHEPVGVIGAFSPWNYPMVLAARKVATALAAGCT 173
Cdd:PRK11809 731 EAGKTFSNAIAEVREAVDFLRYYAGQVRDDFDNDT------------HRPLGPVVCISPWNFPLAIFTGQVAAALAAGNS 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 174 IVIKPAEETPGVMIAIARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVG----RHLLGLASAAMKKI 249
Cdd:PRK11809 799 VLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVArllqRNLAGRLDPQGRPI 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 250 TL--ELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADafeREFAKRAG---QLRLGNGMDETVQ 324
Cdd:PRK11809 879 PLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVAD---RTLKMLRGamaECRMGNPDRLSTD 955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 325 MGPLVNR-------RRQAAMQElTDEAVKSGARllcggGEPVGLGDGFFWQATV--LADVGagarAMHEEVFGPIALVSR 395
Cdd:PRK11809 956 IGPVIDAeakanieRHIQAMRA-KGRPVFQAAR-----ENSEDWQSGTFVPPTLieLDSFD----ELKREVFGPVLHVVR 1025
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 396 F--DTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSIN---TFAVTPPElPFAGIKLSGMG 460
Cdd:PRK11809 1026 YnrNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVNrnmVGAVVGVQ-PFGGEGLSGTG 1094
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
15-440 |
6.82e-40 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 153.94 E-value: 6.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 15 LGAEKNQRDTQPVHNPA-TGELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTL 93
Cdd:COG4230 562 IAGEAASGEARPVRNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVR 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 94 EQGKTLPEALGEVTATADTFEWMAEQGKRVYGrvvpsrftgveQLVVHEPVGVIGAFSPWNYPmvLA--ARKVATALAAG 171
Cdd:COG4230 642 EAGKTLPDAIAEVREAVDFCRYYAAQARRLFA-----------APTVLRGRGVFVCISPWNFP--LAifTGQVAAALAAG 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 172 CTIVIKPAEETPgvMIA--IARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHL-LGLASAAMKK 248
Cdd:COG4230 709 NTVLAKPAEQTP--LIAarAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLInRTLAARDGPI 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 249 ITL--ELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHApTR--FIVHDsVADAFErEFAKRAGQ-LRLGNGMDETV 323
Cdd:COG4230 787 VPLiaETGGQNAMIVDSSALPEQVVDDVLASAFDSAGQRCSA-LRvlCVQED-IADRVL-EMLKGAMAeLRVGDPADLST 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 324 QMGPLVNrrrQAAMQELTD--EAVKSGARLLCGGGEPVGLGDGFFWQATV--LADVgagaRAMHEEVFGPIALVSRF--D 397
Cdd:COG4230 864 DVGPVID---AEARANLEAhiERMRAEGRLVHQLPLPEECANGTFVAPTLieIDSI----SDLEREVFGPVLHVVRYkaD 936
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 736049070 398 TLEQAIETANNVEFGLaayAF---TRSVESMQRLQGSLQAGSVSIN 440
Cdd:COG4230 937 ELDKVIDAINATGYGL---TLgvhSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
139-460 |
2.41e-38 |
|
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: 145.06 E-value: 2.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 139 VVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPgvmiAIARIcMDEGLPSGTLNVLY-----GVPDmi 213
Cdd:cd07132 96 IYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSP----ATAKL-LAELIPKYLDKECYpvvlgGVEE-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 214 SRRLIASpKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFI 293
Cdd:cd07132 169 TTELLKQ-RFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 294 VHDSVADAFeREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTdeavkSGARLLCGGG--------EPvglgdgf 365
Cdd:cd07132 248 CTPEVQEKF-VEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLL-----SGGKVAIGGQtdekeryiAP------- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 366 fwqaTVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQGSLQAGSVSINTFAV- 444
Cdd:cd07132 315 ----TVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMh 390
|
330
....*....|....*..
gi 736049070 445 -TPPELPFAGIKLSGMG 460
Cdd:cd07132 391 yTLDSLPFGGVGNSGMG 407
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
47-410 |
7.61e-34 |
|
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: 132.67 E-value: 7.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 47 VEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGktLPEAL--GEVTATA---DTFEWMAEQGK 121
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARlqGELGRTTgqlRLFADLVREGS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 122 RVYGRV-------VPSRFTGVEQLVVhePVGVIGAFSPWNYPMV--LAARKVATALAAGCTIVIKP-------AEETPGV 185
Cdd:cd07129 79 WLDARIdpadpdrQPLPRPDLRRMLV--PLGPVAVFGASNFPLAfsVAGGDTASALAAGCPVVVKAhpahpgtSELVARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 186 MIAIARICmdeGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASA--AMKKITLELGGHSPVIVDR 263
Cdd:cd07129 157 IRAALRAT---GLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAArpEPIPFYAELGSVNPVFILP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 264 DVPAERVAELAT--AAKFR-NAGQICHAPTRFIVHDSVA-DAFE----REFAKRAGQLRLGNGMDETVQMGplVNRRRQA 335
Cdd:cd07129 234 GALAERGEAIAQgfVGSLTlGAGQFCTNPGLVLVPAGPAgDAFIaalaEALAAAPAQTMLTPGIAEAYRQG--VEALAAA 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 736049070 336 AmqeltdeavksGARLLCGGGEPVGLGDGffwQATVLADVGAGAR---AMHEEVFGPIALVSRFDTLEQAIETANNVE 410
Cdd:cd07129 312 P-----------GVRVLAGGAAAEGGNQA---APTLFKVDAAAFLadpALQEEVFGPASLVVRYDDAAELLAVAEALE 375
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
115-478 |
3.71e-33 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 131.32 E-value: 3.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 115 WMAEQGKRVYGRVVPSrftgvEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARIcM 194
Cdd:PLN02174 89 WMAPEKAKTSLTTFPA-----SAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-L 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 195 DEGLPSGTLNVLYGVPDMISRRLiaSPKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAELA 274
Cdd:PLN02174 163 EQYLDSSAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 275 TAAKFR-NAGQICHAPTRFIVHDSVA----DAFEREFAKRAGQlrlgNGMdETVQMGPLVNRRRQAAMQELTDEavKSGA 349
Cdd:PLN02174 241 IAGKWGcNNGQACISPDYILTTKEYApkviDAMKKELETFYGK----NPM-ESKDMSRIVNSTHFDRLSKLLDE--KEVS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 350 RLLCGGGEPVglGDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTRSVESMQRLQ 429
Cdd:PLN02174 314 DKIVYGGEKD--RENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFA 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 736049070 430 GSLQAGSVSINTFAV--TPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVV 478
Cdd:PLN02174 392 ATVSAGGIVVNDIAVhlALHTLPFGGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
41-479 |
1.28e-30 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 124.07 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 41 MALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEA----LGEVTATADTF--- 113
Cdd:PLN02203 2 EAPGETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAyrdeVGVLTKSANLAlsn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 114 --EWMA-EQGKrvygrvVPSRFTGVEQLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIA 190
Cdd:PLN02203 82 lkKWMApKKAK------LPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 191 RIcMDEGLPSGTLNVLYGVPDmISRRLIASpKVAQLSFTGSVPVGRHLLGLASAAMKKITLELGGHSPVIVD-------R 263
Cdd:PLN02203 156 AN-IPKYLDSKAVKVIEGGPA-VGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsssrdT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 264 DVPAERVAelatAAKFRN-AGQICHAPTRFIVHDSVAdAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRR-QAAMQELT 341
Cdd:PLN02203 233 KVAVNRIV----GGKWGScAGQACIAIDYVLVEERFA-PILIELLKSTIKKFFGENPRESKSMARILNKKHfQRLSNLLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 342 DEAVKsgARLLCGGG-EPvglgDGFFWQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFTR 420
Cdd:PLN02203 308 DPRVA--ASIVHGGSiDE----KKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTN 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736049070 421 SVESMQRLQGSLQAGSVSINTFAV--TPPELPFAGIKLSGMGVEMGEEGLMDHFHIKAVVR 479
Cdd:PLN02203 382 NEKLKRRILSETSSGSVTFNDAIIqyACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLR 442
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
23-458 |
1.12e-27 |
|
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: 115.76 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 23 DTQPVHNPAT-GELLGRLPMALEDDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILT-LEQGKTLP 100
Cdd:cd07123 46 NTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYRYELNAATmLGQGKNVW 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 101 EAlgEVTATA---DTFEWMAEQGKRVYGRVVPSRFTGVEQLVVHEPV-GVIGAFSPWNYpmvlaarkvaTALAA------ 170
Cdd:cd07123 126 QA--EIDAACeliDFLRFNVKYAEELYAQQPLSSPAGVWNRLEYRPLeGFVYAVSPFNF----------TAIGGnlagap 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 171 ---GCTIVIKPAeetPGVMIA---IARICMDEGLPSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASA 244
Cdd:cd07123 194 almGNVVLWKPS---DTAVLSnylVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 245 AMK------KITLELGGHSPVIVDRDVPAERVAELATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNG 318
Cdd:cd07123 271 NLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 319 MDETVQMGPLVNRRRQAAMQELTDEAVKS-GARLLCGGGepvglGD---GFFWQATVLADVGAGARAMHEEVFGPIALV- 393
Cdd:cd07123 351 DDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK-----CDdsvGYFVEPTVIETTDPKHKLMTEEIFGPVLTVy 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 736049070 394 ----SRFDTLEQAIETANnvEFGL--AAYAFTRSV--ESMQRLQGSlqAGSVSIN---TFAVTpPELPFAGIKLSG 458
Cdd:cd07123 426 vypdSDFEETLELVDTTS--PYALtgAIFAQDRKAirEATDALRNA--AGNFYINdkpTGAVV-GQQPFGGARASG 496
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
6-419 |
2.60e-23 |
|
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: 102.73 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 6 LKLLVDGQWLGaekNQRDTQPVHNPATGELLGR-----LPMAleDDVEQAIEAAHRAFAAWktwTALERGRLLLRIASAI 80
Cdd:cd07128 1 LQSYVAGQWHA---GTGDGRTLHDAVTGEVVARvssegLDFA--AAVAYAREKGGPALRAL---TFHERAAMLKALAKYL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 81 REQARSLAQILTLeQGKTLPEALGEVTATADTFEWMAEQGKR--------VYGRVVP----SRFTGVEQLVVHEPVGV-I 147
Cdd:cd07128 73 MERKEDLYALSAA-TGATRRDSWIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPlskdGTFVGQHILTPRRGVAVhI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 148 GAFspwNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEG-LPSGTLNVLYGVPDMISRRLIASPKVAql 226
Cdd:cd07128 152 NAF---NFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVGDLLDHLGEQDVVA-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 227 sFTGSVPVGRHLLGLASAAMKKI--TLELGGHSPVIVDRDV-PA---------ERVAELATaakfrNAGQICHAPTRFIV 294
Cdd:cd07128 227 -FTGSAATAAKLRAHPNIVARSIrfNAEADSLNAAILGPDAtPGtpefdlfvkEVAREMTV-----KAGQKCTAIRRAFV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 295 H----DSVADAFEREFAKragqLRLGNGMDETVQMGPLVNRRRQAAMQElTDEAVKSGARLLCGGGEP-----VGLGDGF 365
Cdd:cd07128 301 PearvDAVIEALKARLAK----VVVGDPRLEGVRMGPLVSREQREDVRA-AVATLLAEAEVVFGGPDRfevvgADAEKGA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 736049070 366 FWQATVL-ADVGAGARAMHE-EVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFT 419
Cdd:cd07128 376 FFPPTLLlCDDPDAATAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVT 431
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
47-438 |
1.46e-22 |
|
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: 100.00 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 47 VEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTlPEALGEVTATADTFEWMAEQGK--RVY 124
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVIYsyRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 125 GRVVPSRFTGVEQLVVHE--PVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEG-LPSG 201
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 202 TLNVLYGvPDMISRRLIASPKVAQLSFTGSVPVGRHLLGLASAAmkKITLELGGHSPVIVDRDVPA-ERVAELATAAKFR 280
Cdd:cd07084 160 DVTLING-DGKTMQALLLHPNPKMVLFTGSSRVAEKLALDAKQA--RIYLELAGFNWKVLGPDAQAvDYVAWQCVQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 281 NAGQICHAPTRFIVHdsvaDAFEREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDEavkSGARLLCGGGEPVG 360
Cdd:cd07084 237 CSGQKCTAQSMLFVP----ENWSKTPLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENL---LGSVLLFSGKELKN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 361 LGDGFFWQATVLADV-------GAGARAMHEEVFGPIALVSRfdtleqaietannVEFGLAAYAftrsVESMQRLQGSLQ 433
Cdd:cd07084 310 HSIPSIYGACVASALfvpideiLKTYELVTEEIFGPFAIVVE-------------YKKDQLALV----LELLERMHGSLT 372
|
....*
gi 736049070 434 AGSVS 438
Cdd:cd07084 373 AAIYS 377
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
5-419 |
4.45e-21 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 95.93 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 5 ELKLLVDGQWLGAeknQRDTQPVHNPATGELLGRLPmALEDDVEQAIE-AAHRAFAAWKTWTALERGRLLLRIASAIREQ 83
Cdd:PRK11903 4 LLANYVAGRWQAG---SGAGTPLFDPVTGEELVRVS-ATGLDLAAAFAfAREQGGAALRALTYAQRAALLAAIVKVLQAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 84 ARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGRVV-----------PSRFTGVEQLVVHEPVGV-IGAFs 151
Cdd:PRK11903 80 RDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGDARLlrdgeavqlgkDPAFQGQHVLVPTRGVALfINAF- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 152 pwNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEG-LPSGTLNVLYGVP-DMISRrlIASPKVaqLSFT 229
Cdd:PRK11903 159 --NFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSSaGLLDH--LQPFDV--VSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 230 GSVPVGRHLLGLASAAMKKITLELGG---HSPVIVDRDVPAERVAELATAAKFRN----AGQICHAPTRFIVHDSVADAF 302
Cdd:PRK11903 233 GSAETAAVLRSHPAVVQRSVRVNVEAdslNSALLGPDAAPGSEAFDLFVKEVVREmtvkSGQKCTAIRRIFVPEALYDAV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 303 EREFAKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTdEAVKSGARLLCGGG--EPVGL--GDGFFWQATVL-ADVGA 377
Cdd:PRK11903 313 AEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGL-AALRAQAEVLFDGGgfALVDAdpAVAACVGPTLLgASDPD 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 736049070 378 GARAMHE-EVFGPIALVSRFDTLEQAIETANNVEFGLAAYAFT 419
Cdd:PRK11903 392 AATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
9-357 |
1.88e-13 |
|
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: 72.14 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 9 LVDGQWLGAeknqRDTQPVHNPATGELLGRLPMALEDDVEQAIEAA--------HRAFAAWKTWtaLERGRLLLRIASAI 80
Cdd:cd07126 2 LVAGKWKGA----SNYTTLLDPLNGDKFISVPDTDEDEINEFVDSLrqcpksglHNPLKNPERY--LLYGDVSHRVAHEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 81 R--EQARSLAQILTLEQGKTLPEALGEVTATADTFEWMAEQGKRVYGR--VVPSRFTGVEQLVVHEPVGVIGAFSPWNYP 156
Cdd:cd07126 76 RkpEVEDFFARLIQRVAPKSDAQALGEVVVTRKFLENFAGDQVRFLARsfNVPGDHQGQQSSGYRWPYGPVAIITPFNFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 157 MVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEGLPSGTLNVLY-GVPDMISRRLIASPKVAQlsFTGSVPVG 235
Cdd:cd07126 156 LEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHsDGPTMNKILLEANPRMTL--FTGSSKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 236 RHllgLASAAMKKITLELGGHSPVIVDRDVP-AERVAELATAAKFRNAGQICHAPTRFIVHDSVADA-FEREFAKRAGQL 313
Cdd:cd07126 234 ER---LALELHGKVKLEDAGFDWKILGPDVSdVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQAgILDKLKALAEQR 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 736049070 314 RLgngmdETVQMGPLVNRRRQAAMQELTDEAVKSGARLLCGGGE 357
Cdd:cd07126 311 KL-----EDLTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKP 349
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
45-321 |
6.10e-11 |
|
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: 64.21 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 45 DDVEQAIEAAHRAFAawkTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEalgevtataDTFEWMAEQGKRVY 124
Cdd:cd07081 2 DDAVAAAKVAQQGLS---CKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVE---------DKVIKNHFAAEYIY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 125 GRVVPSRFTGVEQ-------LVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDEG 197
Cdd:cd07081 70 NVYKDEKTCGVLTgdenggtLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 198 LPSGTLNVLYGV---PDM-ISRRLIASPKVAQLSFTGsvpvGRHLLGLASAAMKKITLELGGHSPVIVDRDVPAERVAEL 273
Cdd:cd07081 150 VAAGAPENLIGWidnPSIeLAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQS 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 736049070 274 ATAAKFRNAGQICHAPTRFIVHDSVADAFEREFAKRAGQLRLGNGMDE 321
Cdd:cd07081 226 IVKSKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQGAYKLTAEELQQ 273
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
14-440 |
1.65e-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: 60.18 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 14 WLGAEKNqrdtqpvhnPATGELLGRLPMAledDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQ--IL 91
Cdd:cd07127 65 WVGGEVS---------PYGVELGVTYPQC---DPDALLAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHavMH 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 92 TLEQGKTLP-------------EALG----EVTATADTFEWMAEQGKRVYGRVvPSRFTgveqlVVHEPVG-VIG--AFS 151
Cdd:cd07127 133 TTGQAFMMAfqaggphaqdrglEAVAyawrEMSRIPPTAEWEKPQGKHDPLAM-EKTFT-----VVPRGVAlVIGcsTFP 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 152 PWN-YPMVLAArkvataLAAGCTIVIKPAEET--PGVM-IAIARICMDE-GL-PSGTLNVLYGVPDMISRRLIASPKVAQ 225
Cdd:cd07127 207 TWNgYPGLFAS------LATGNPVIVKPHPAAilPLAItVQVAREVLAEaGFdPNLVTLAADTPEEPIAQTLATRPEVRI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 226 LSFTGSVPVGRHLLglASAAMKKITLELGGHSPVIVDR-DVPAERVAELATAAKFRnAGQICHAPTRFIV---------- 294
Cdd:cd07127 281 IDFTGSNAFGDWLE--ANARQAQVYTEKAGVNTVVVDStDDLKAMLRNLAFSLSLY-SGQMCTTPQNIYVprdgiqtddg 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 295 ---HDSVADAFEREFAKRAGQLRLGNGMdetvqMGPLVNrrrQAAMQELTdEAVKSGARLLcgGGEPVGLGDgfFWQATV 371
Cdd:cd07127 358 rksFDEVAADLAAAIDGLLADPARAAAL-----LGAIQS---PDTLARIA-EARQLGEVLL--ASEAVAHPE--FPDARV 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 736049070 372 ----LADVGAGARAMH-EEVFGPIALVSRFDTLEQAIETANNV--EFG-LAAYAFTRSVESMQRLQ-GSLQAG-SVSIN 440
Cdd:cd07127 425 rtplLLKLDASDEAAYaEERFGPIAFVVATDSTDHSIELARESvrEHGaMTVGVYSTDPEVVERVQeAALDAGvALSIN 503
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
45-427 |
9.92e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 57.22 E-value: 9.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 45 DDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGktlpeaLGEVtatADTFEWMAEQGKRVY 124
Cdd:PRK15398 36 ASVDDAVAAAKVAQQRYQQKSLAMRQRIIDAIREALLPHAEELAELAVEETG------MGRV---EDKIAKNVAAAEKTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 125 G--RVVPSRFTGVEQLVVHE--PVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAeetPGV---------MI--AI 189
Cdd:PRK15398 107 GveDLTTEALTGDNGLTLIEyaPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPH---PGAkkvslraieLLneAI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 190 ARICmdeglpsGTLNVLYGV--PDMIS-RRLIASPKVAQLSFTGSVPVGRhllglasAAMK--KITLELG-GHSPVIVDR 263
Cdd:PRK15398 184 VAAG-------GPENLVVTVaePTIETaQRLMKHPGIALLVVTGGPAVVK-------AAMKsgKKAIGAGaGNPPVVVDE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 264 DVPAERVAE-LATAAKFRNaGQICHAPTRFIVHDSVADAFEREFaKRAGQLRLgnGMDETVQMGPLVNRRRQAAMQELTD 342
Cdd:PRK15398 250 TADIEKAARdIVKGASFDN-NLPCIAEKEVIVVDSVADELMRLM-EKNGAVLL--TAEQAEKLQKVVLKNGGTVNKKWVG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 343 eavKSGARLLCGGGEPVGLGdgffwQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGL--AAYAFTR 420
Cdd:PRK15398 326 ---KDAAKILEAAGINVPKD-----TRLLIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALAVKLEHGNrhTAIMHSR 397
|
....*..
gi 736049070 421 SVESMQR 427
Cdd:PRK15398 398 NVDNLNK 404
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
45-427 |
1.38e-07 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 53.78 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 45 DDVEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGktlpeaLGEVtatADTFEWMAEQGKRVY 124
Cdd:cd07121 4 ATVDDAVAAAKAAQKQYRKCTLADREKIIEAIREALLSNAEELAEMAVEETG------MGRV---EDKIAKNHLAAEKTP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 125 G--RVVPSRFTGVEQLVVHE--PVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKP---AEETPGVMIA-IARICMDE 196
Cdd:cd07121 75 GteDLTTTAWSGDNGLTLVEyaPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgAKKVSAYAVElINKAIAEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 197 GLPSGtLNVLYGVPDMIS-RRLIASPKVAQLSFTGSVPVGRHLLglasAAMKKITLELGGHSPVIVDRDVPAERVAE-LA 274
Cdd:cd07121 155 GGPDN-LVVTVEEPTIETtNELMAHPDINLLVVTGGPAVVKAAL----SSGKKAIGAGAGNPPVVVDETADIEKAARdIV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 275 TAAKFRNaGQICHAPTRFIVHDSVADAFEREFaKRAGQLRLGNGMDETVQMGPLVNRRRQAAMQELTDeavKSGARLLCG 354
Cdd:cd07121 230 QGASFDN-NLPCIAEKEVIAVDSVADYLIAAM-QRNGAYVLNDEQAEQLLEVVLLTNKGATPNKKWVG---KDASKILKA 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 736049070 355 GGEPVGLGdgffwQATVLADVGAGARAMHEEVFGPIALVSRFDTLEQAIETANNVEFGL--AAYAFTRSVESMQR 427
Cdd:cd07121 305 AGIEVPAD-----IRLIIVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTK 374
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
36-307 |
1.22e-06 |
|
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: 50.68 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 36 LGRLPMALEDDVEQAIEAAHRAFAAwktwtaLERGRLLLRIASAIREQARSLAQILTleqgKTLPEALGEVTATADTFEW 115
Cdd:cd07077 6 AQRTLAVNHDEQRDLIINAIANALY------DTRQRLASEAVSERGAYIRSLIANWI----AMMGCSESKLYKNIDTERG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 116 MAEQGKRVYGRVVPSRFtgvEQLVVHEPVGVIGAFSPWNYPMvLAARKVATALAAGCTIVIKPAEETPGVMIAIArICMD 195
Cdd:cd07077 76 ITASVGHIQDVLLPDNG---ETYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALA-LLFQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 196 EGLPSGTLNVLYG-VP---DMISRRLIASPKVAQLSFTGsvpvGRHLLGLASAAMKKITLeLG---GHSPVIVDRDVPAE 268
Cdd:cd07077 151 AADAAHGPKILVLyVPhpsDELAEELLSHPKIDLIVATG----GRDAVDAAVKHSPHIPV-IGfgaGNSPVVVDETADEE 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 736049070 269 RVAELATAAKFRNaGQICHAPTRFIVHDSVADAFEREFA 307
Cdd:cd07077 226 RASGSVHDSKFFD-QNACASEQNLYVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
47-313 |
2.23e-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: 49.80 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 47 VEQAIEAAHRAFAAWKTWTALERGRLLLRIASAIREQARSLAQILTLEQGKTLPEalGEVT----ATADTFEWMAeqGKR 122
Cdd:cd07122 1 VDELVERARKAQREFATFSQEQVDKIVEAVAWAAADAAEELAKMAVEETGMGVVE--DKVIknhfASEYVYNDIK--DMK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 123 VYGRVVPSRFTGVeqLVVHEPVGVIGAFSPWNYPMVLAARKVATALAAGCTIVIKPAEETPGVMIAIARICMDE----GL 198
Cdd:cd07122 77 TVGVIEEDEEKGI--VEIAEPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMREAavaaGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049070 199 PSGTLNVLYGVPDMISRRLIASPKVAQLSFTGSVpvgrhllGLASAAMKKITLELG---GHSPVIVDRDvpaervAELAT 275
Cdd:cd07122 155 PEGLIQWIEEPSIELTQELMKHPDVDLILATGGP-------GMVKAAYSSGKPAIGvgpGNVPAYIDET------ADIKR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 736049070 276 AAK-------FRNaGQICHAPTRFIVHDSVADAFEREFAKRAGQL 313
Cdd:cd07122 222 AVKdiilsktFDN-GTICASEQSVIVDDEIYDEVRAELKRRGAYF 265
|
|
| |
