|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
6-488 |
0e+00 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 881.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPAL 165
Cdd:cd07119 81 RLETLNTGKTLRESEIDIDDVANCFRYYAGLATKETGEVYDVP-PHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 166 AAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKK 245
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 246 IALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPL 325
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 326 ISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELA 405
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDELAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 406 NDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRNTKPAAV 485
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLSPQPI 479
|
...
gi 1803004483 486 NWF 488
Cdd:cd07119 480 GWF 482
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
6-474 |
0e+00 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 762.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEES-KADMDDIANVFQYYAGLADKDGGEIISSPIPdSESKIIREPIGVCGQITPWNYPLLQASWKIAPA 164
Cdd:TIGR01804 79 KLETLDTGKTLQETiVADMDSGADVFEFFAGLAPALNGEIIPLGGP-SFAYTIREPLGVCVGIGAWNYPLQIASWKIAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 165 LAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVK 244
Cdd:TIGR01804 158 LAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAAGHLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 245 KIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGP 324
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 325 LISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIEL 404
Cdd:TIGR01804 318 LISAAHRDKVLSYIEKGKAEGATLATGGGRPENVGLQNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIAR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 405 ANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:TIGR01804 398 ANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
5-480 |
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: 646.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDaikaiaaarraFDK---------GEWSSLSGLERGKIVLKIAE 75
Cdd:COG1012 8 LFIGGEWVAAASGETFDVINPATGEVLARVPAATAED-----------VDAavaaaraafPAWAATPPAERAAILLRAAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 76 LIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLL 155
Cdd:COG1012 77 LLEERREELAALLTLETGKPLAEARGEVDRAADFLRYYAGEARRLYGETIPSDAPGTRAYVRREPLGVVGAITPWNFPLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 156 QASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKI 235
Cdd:COG1012 157 LAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 236 MRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNG 315
Cdd:COG1012 237 AAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 316 FHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETF 395
Cdd:COG1012 317 LDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGE---GGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 396 SSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYF-AQAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:COG1012 394 DDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAvPQAPFGGVKQSGIGREGGREGLEEYTETK 473
|
....*.
gi 1803004483 475 HVYRNT 480
Cdd:COG1012 474 TVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
11-476 |
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: 625.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 11 WISAEKEQIRSIiNPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESL 90
Cdd:pfam00171 1 WVDSESETIEVI-NPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 91 DTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNT 170
Cdd:pfam00171 78 ENGKPLAEARGEVDRAIDVLRYYAGLARRLDGETLPSD-PGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 171 IVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALEL 250
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 251 GGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEH 330
Cdd:pfam00171 237 GGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 331 RAKVEKYVEIGLEEGAKLETGGKRPEDpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIY 410
Cdd:pfam00171 317 LERVLKYVEDAKEEGAKLLTGGEAGLD----NGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 411 GLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFA-QAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
5-477 |
0e+00 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 594.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07091 6 LFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEES-KADMDDIANVFQYYAGLADKDGGEIIssPIPDSE-SKIIREPIGVCGQITPWNYPLLQASWKIA 162
Cdd:cd07091 86 AALESLDNGKPLEESaKGDVALSIKCLRYYAGWADKIQGKTI--PIDGNFlAYTRREPIGVCGQIIPWNFPLLMLAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 163 PALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS-G 241
Cdd:cd07091 164 PALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAAAkS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 242 NVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETE 321
Cdd:cd07091 244 NLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 322 SGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEV 401
Cdd:cd07091 324 QGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGS----KGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEV 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1803004483 402 IELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07091 400 IERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
57-477 |
0e+00 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 585.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKI 136
Cdd:cd07078 13 AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEVIPSPDPGELAIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 137 IREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAV 216
Cdd:cd07078 93 RREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGAALAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 217 NKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIH 296
Cdd:cd07078 173 HPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLVHESIY 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 297 DQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPalqNGFFYEPTIFSNCNS 376
Cdd:cd07078 253 DEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGG---KGYFVPPTVLTDVDP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 377 DMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPY-FAQAPWGGYKQ 455
Cdd:cd07078 330 DMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVGaEPSAPFGGVKQ 409
|
410 420
....*....|....*....|..
gi 1803004483 456 SGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07078 410 SGIGREGGPYGLEEYTEPKTVT 431
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
22-477 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 570.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPL 181
Cdd:cd07114 81 QVRYLAEWYRYYAGLADKIEGAVIPVDKGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 182 TTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKD 261
Cdd:cd07114 161 STLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 262 ADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIG 341
Cdd:cd07114 241 ADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYVARA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 342 LEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDI 421
Cdd:cd07114 321 REEGARVLTGGERPSGADLGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1803004483 422 EKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07114 401 ARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
22-476 |
0e+00 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 547.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 -DMDDIANVFQYYAGLADKDGGEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITP 180
Cdd:cd07093 79 rDIPRAAANFRFFADYILQLDGESYPQD-GGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 181 LTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFK 260
Cdd:cd07093 158 LTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 261 DADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEI 340
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 341 GLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKD 420
Cdd:cd07093 318 ARAEGATILTGGGRPELPDLEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1803004483 421 IEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
22-479 |
0e+00 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 540.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESK- 100
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 101 ADMDDIANVFQYYAGLADKDGGEIIssPI-PDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEIT 179
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVI--PVrGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 180 PLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVF 259
Cdd:cd07115 157 PLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 260 KDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVE 339
Cdd:cd07115 237 ADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 340 IGLEEGAKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSK 419
Cdd:cd07115 317 VGREEGARLLTGGKRPGAR----GFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 420 DIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRN 479
Cdd:cd07115 393 DLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
5-490 |
0e+00 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 529.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDK---GEWSSLSGLERGKIVLKIAELIRRDL 81
Cdd:PLN02467 10 LFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgKDWARTTGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 82 EELAELESLDTGKTLEESKADMDDIANVFQYYAGLA---DKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQAS 158
Cdd:PLN02467 90 SELAKLETLDCGKPLDEAAWDMDDVAGCFEYYADLAealDAKQKAPVSLPMETFKGYVLKEPLGVVGLITPWNYPLLMAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 159 WKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRA 238
Cdd:PLN02467 170 WKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 239 ASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHA 318
Cdd:PLN02467 250 AAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 319 ETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDpaLQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSE 398
Cdd:PLN02467 330 GCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEH--LKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 399 EEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:PLN02467 408 DEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQVTK 487
|
490
....*....|..
gi 1803004483 479 NTKPAAVNWFNS 490
Cdd:PLN02467 488 YISDEPWGWYPP 499
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
22-478 |
0e+00 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 520.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLA---DKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEI 178
Cdd:cd07110 79 DVDDVAGCFEYYADLAeqlDAKAERAVPLPSEDFKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 179 TPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIV 258
Cdd:cd07110 159 TSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 259 FKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYV 338
Cdd:cd07110 239 FDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVLSFI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 339 EIGLEEGAKLETGGKRPEDpaLQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWS 418
Cdd:cd07110 319 ARGKEEGARLLCGGRRPAH--LEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVIS 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 419 KDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:cd07110 397 RDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQITR 456
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
5-477 |
0e+00 |
|
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: 518.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKG-EWSSLSGLERGKIVLKIAELIRRDLEE 83
Cdd:cd07141 9 IFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIERDRAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 84 LAELESLDTGKTLEESK-ADMDDIANVFQYYAGLADKDGGEIIssPIPDSESKIIR-EPIGVCGQITPWNYPLLQASWKI 161
Cdd:cd07141 89 LASLETLDNGKPFSKSYlVDLPGAIKVLRYYAGWADKIHGKTI--PMDGDFFTYTRhEPVGVCGQIIPWNFPLLMAAWKL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 162 APALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS- 240
Cdd:cd07141 167 APALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQAAGk 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 241 GNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAET 320
Cdd:cd07141 247 SNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 321 ESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEE 400
Cdd:cd07141 327 EQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDK----GYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 401 VIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07141 403 VIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
22-476 |
0e+00 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 516.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07103 1 VINPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPL 181
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPAPGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 182 TTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKD 261
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 262 ADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIG 341
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 342 LEEGAKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDI 421
Cdd:cd07103 319 VAKGAKVLTGGKRLGLG----GYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDL 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1803004483 422 EKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07103 395 ARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
22-481 |
2.18e-180 |
|
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: 513.39 E-value: 2.18e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPL 181
Cdd:cd07090 79 DIDSSADCLEYYAGLAPTLSGEHVPLP-GGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 182 TTIKVFKLMEEAGVPKGVANLVLGPGATvGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKD 261
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 262 ADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIG 341
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 342 LEEGAKLETGGKR-PEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKD 420
Cdd:cd07090 317 KQEGAKVLCGGERvVPEDGLENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 421 IEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRNTK 481
Cdd:cd07090 397 LQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVEMG 457
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
23-474 |
6.75e-180 |
|
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: 512.15 E-value: 6.75e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 23 INPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA- 101
Cdd:cd07112 7 INPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISDALAv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPL 181
Cdd:cd07112 87 DVPSAANTFRWYAEAIDKVYGEVAPTG-PDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPAEQSPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 182 TTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMR-AASGNVKKIALELGGKNPNIVFK 260
Cdd:cd07112 166 TALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEySGQSNLKRVWLECGGKSPNIVFA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 261 DA-DLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVE 339
Cdd:cd07112 246 DApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 340 IGLEEGAKLETGGKRpeDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSK 419
Cdd:cd07112 326 SGKAEGARLVAGGKR--VLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTS 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1803004483 420 DIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:cd07112 404 DLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELK 458
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
5-478 |
4.91e-177 |
|
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: 505.11 E-value: 4.91e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELI--RRDle 82
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYeaRAD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 83 elaeleslDTGKTL-EESKADMDdIANVFQYYAGLAD----KDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQA 157
Cdd:cd07138 77 --------ELAQAItLEMGAPIT-LARAAQVGLGIGHlraaADALKDFEFEERRGNSLVVREPIGVCGLITPWNWPLNQI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 158 SWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMR 237
Cdd:cd07138 148 VLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 238 AASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFH 317
Cdd:cd07138 228 AAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 318 AETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGkrPEDPA-LQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFS 396
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPEgLERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 397 SEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN--DFHPyfaQAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:cd07138 386 DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHINgaAFNP---GAPFGGYKQSGNGREWGRYGLEEFLEVK 462
|
....
gi 1803004483 475 HVYR 478
Cdd:cd07138 463 SIQG 466
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
5-479 |
2.73e-176 |
|
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: 503.86 E-value: 2.73e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWI-SAEKEQIRSIiNPFNQEEIATVSEGGREDAIKAIAAARRAFdKGEWSSLSGLERGKIVLKIAELIRRDLEE 83
Cdd:cd07144 10 LFINNEFVkSSDGETIKTV-NPSTGEVIASVYAAGEEDVDKAVKAARKAF-ESWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 84 LAELESLDTGKTLEE-SKADMDDIANVFQYYAGLADKDGGEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIA 162
Cdd:cd07144 88 LAAIEALDSGKPYHSnALGDLDEIIAVIRYYAGWADKIQGKTIPTS-PNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 163 PALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGN 242
Cdd:cd07144 167 PALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAAQN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 VKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAK-RIKLGNGFHAETE 321
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 322 SGPLISAEHRAKVEKYVEIGLEEGAKLETGGKrPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEV 401
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGE-KAPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803004483 402 IELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRN 479
Cdd:cd07144 406 IKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHIN 483
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
1-476 |
1.29e-174 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 499.05 E-value: 1.29e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 1 MSQTLFIDGEWISAEKEQIrSIINPFNQEEIATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRD 80
Cdd:PRK13473 1 MQTKLLINGELVAGEGEKQ-PVYNPATGEVLAEIAEASAAQVDAAVAAADAAF--PEWSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 81 LEELAELESLDTGKTLEESKAD-MDDIANVFQYYAG----LADKDGGEIIsspiPDSESKIIREPIGVCGQITPWNYPLL 155
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDeIPAIVDVFRFFAGaarcLEGKAAGEYL----EGHTSMIRRDPVGVVASIAPWNYPLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 156 QASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAgVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKI 235
Cdd:PRK13473 154 MAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 236 MRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNG 315
Cdd:PRK13473 233 LSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 316 FHAETESGPLISAEHRAKVEKYVEIGLEEG-AKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVET 394
Cdd:PRK13473 313 DDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGK----GYYYEPTLLAGARQDDEIVQREVFGPVVSVTP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 395 FSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:PRK13473 389 FDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVR 468
|
..
gi 1803004483 475 HV 476
Cdd:PRK13473 469 HV 470
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
30-476 |
1.83e-174 |
|
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: 498.02 E-value: 1.83e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 30 EIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANV 109
Cdd:cd07118 9 VVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIEGAADL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 110 FQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKL 189
Cdd:cd07118 89 WRYAASLARTLHGDSYNNLGDDMLGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 190 MEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVD 269
Cdd:cd07118 169 LIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAAD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 270 QALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLE 349
Cdd:cd07118 249 AVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 350 TGGKRpedPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAA 429
Cdd:cd07118 329 LGGER---LASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVAR 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1803004483 430 RLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07118 406 RIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
22-476 |
2.40e-174 |
|
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: 497.62 E-value: 2.40e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07092 1 VVDPATGEEIATVPDASAADVDAAVAAAHAAFP--SWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 D-MDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITP 180
Cdd:cd07092 79 DeLPGAVDNFRFFAGAARTLEGPAAGEYLPGHTSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 181 LTTIKVFKLMEEaGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFK 260
Cdd:cd07092 159 LTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 261 DADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEi 340
Cdd:cd07092 238 DADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVE- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 341 GLEEGAKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKD 420
Cdd:cd07092 317 RAPAHARVLTGGRRAEGP----GYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRD 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1803004483 421 IEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07092 393 VGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHV 448
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
3-477 |
1.03e-172 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 494.78 E-value: 1.03e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 3 QTLFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRDLE 82
Cdd:PRK13252 7 QSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRILRRAVDILRERND 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 83 ELAELESLDTGKTLEE-SKADMDDIANVFQYYAGLADKDGGEIIssPIPDSE-SKIIREPIGVCGQITPWNYPLLQASWK 160
Cdd:PRK13252 85 ELAALETLDTGKPIQEtSVVDIVTGADVLEYYAGLAPALEGEQI--PLRGGSfVYTRREPLGVCAGIGAWNYPIQIACWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 161 IAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGAtVGDELAVNKDVDLISFTGGIETGKKIMRAAS 240
Cdd:PRK13252 163 SAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGR-VGAWLTEHPDIAKVSFTGGVPTGKKVMAAAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 241 GNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAET 320
Cdd:PRK13252 242 ASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPAT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 321 ESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEE 400
Cdd:PRK13252 322 NFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEGGFANGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDE 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 401 VIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:PRK13252 402 VIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQ 478
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
22-476 |
1.05e-171 |
|
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: 490.98 E-value: 1.05e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSsLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07109 1 VFDPSTGEVFARIARGGAADVDRAVQAARRAFESGWLR-LSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEIIssPI-PDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITP 180
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETI--PLgPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 181 LTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFK 260
Cdd:cd07109 158 LTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 261 DADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHaETESGPLISAEHRAKVEKYVEI 340
Cdd:cd07109 238 DADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLE-DPDLGPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 341 GLEEGAKLETGGKRPEDPaLQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKD 420
Cdd:cd07109 317 ARARGARIVAGGRIAEGA-PAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 421 IEKCERVAARLRMGTVWINDfhpYFA----QAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07109 396 GDRALRVARRLRAGQVFVNN---YGAgggiELPFGGVKKSGHGREKGLEALYNYTQTKTV 452
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
5-479 |
9.68e-169 |
|
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: 484.72 E-value: 9.68e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFETDWGLKVSGSKRGRCLSKLADLMERNLDYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKA-DMDDIANVFQYYAGLADKDGGEIISSpipdSESKII---REPIGVCGQITPWNYPLLQASWK 160
Cdd:cd07143 89 ASIEALDNGKTFGTAKRvDVQASADTFRYYGGWADKIHGQVIET----DIKKLTytrHEPIGVCGQIIPWNFPLLMCAWK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 161 IAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS 240
Cdd:cd07143 165 IAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 241 -GNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAE 319
Cdd:cd07143 245 kSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAED 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 320 TESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEE 399
Cdd:cd07143 325 TFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGN----EGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 400 EVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRN 479
Cdd:cd07143 401 EAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
6-477 |
4.39e-167 |
|
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: 479.84 E-value: 4.39e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPAL 165
Cdd:cd07088 79 KLIVEEQGKTLSLARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 166 AAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKK 245
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAENITK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 246 IALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPL 325
Cdd:cd07088 239 VSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 326 ISAEHRAKVEKYVEIGLEEGAKLETGGKRPEdpaLQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELA 405
Cdd:cd07088 319 VNEAALDKVEEMVERAVEAGATLLTGGKRPE---GEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1803004483 406 NDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07088 396 NDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
22-476 |
1.61e-164 |
|
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: 472.88 E-value: 1.61e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSsLSGLERGKIVLKIAELIRRDLEELAELESLDTGKT--LEES 99
Cdd:cd07089 1 VINPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWS-TDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 100 KADMDDIANvFQYYAGLADKDGGEIISSPIPD----SESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKP 175
Cdd:cd07089 80 MQVDGPIGH-LRYFADLADSFPWEFDLPVPALrggpGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 176 SEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNP 255
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 256 NIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVE 335
Cdd:cd07089 239 NIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 336 KYVEIGLEEGAKLETGGKRPEDpaLQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGA 415
Cdd:cd07089 319 GYIARGRDEGARLVTGGGRPAG--LDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 416 VWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07089 397 VWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-478 |
2.92e-164 |
|
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: 472.89 E-value: 2.92e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEqiRSIINPFN-QEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07097 4 YIDGEWVAGGDG--EENRNPSDtSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPA 164
Cdd:cd07097 80 ARLLTREEGKTLPEARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGVEVETTREPLGVVGLITPWNFPIAIPAWKIAPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 165 LAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVK 244
Cdd:cd07097 160 LAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 245 KIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGP 324
Cdd:cd07097 240 RVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 325 LISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPalQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIEL 404
Cdd:cd07097 320 VVSERQLEKDLRYIEIARSEGAKLVYGGERLKRP--DEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 405 ANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN------DFHpyfaqAPWGGYKQSGFG-RELGKIGLEEYTEVKHVY 477
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlptagvDYH-----VPFGGRKGSSYGpREQGEAALEFYTTIKTVY 472
|
.
gi 1803004483 478 R 478
Cdd:cd07097 473 V 473
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
5-477 |
8.75e-164 |
|
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: 471.83 E-value: 8.75e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07559 3 NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESK-ADMDDIANVFQYYAG--LADKDGGEIISSpipDSESKIIREPIGVCGQITPWNYPLLQASWKI 161
Cdd:cd07559 81 AVAETLDNGKPIRETLaADIPLAIDHFRYFAGviRAQEGSLSEIDE---DTLSYHFHEPLGVVGQIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 162 APALAAGNTIVMKPSEITPLTTIKVFKLMEEAgVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASG 241
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 242 NVKKIALELGGKNPNIVFKDA-----DLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGF 316
Cdd:cd07559 237 NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 317 HAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFS 396
Cdd:cd07559 317 DPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 397 SEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07559 397 DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
.
gi 1803004483 477 Y 477
Cdd:cd07559 477 L 477
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
5-477 |
5.03e-162 |
|
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: 467.36 E-value: 5.03e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07142 6 LFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESK-ADMDDIANVFQYYAGLADKDGGEIISSPIPdSESKIIREPIGVCGQITPWNYPLLQASWKIAP 163
Cdd:cd07142 86 AALETWDNGKPYEQARyAEVPLAARLFRYYAGWADKIHGMTLPADGP-HHVYTLHEPIGVVGQIIPWNFPLLMFAWKVGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 164 ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS-GN 242
Cdd:cd07142 165 ALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLAAkSN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 VKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETES 322
Cdd:cd07142 245 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 323 GPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVI 402
Cdd:cd07142 325 GPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGS----KGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1803004483 403 ELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVV 475
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
57-478 |
8.08e-160 |
|
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: 457.46 E-value: 8.08e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKI 136
Cdd:cd06534 9 AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPGGEAYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 137 IREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAV 216
Cdd:cd06534 89 RREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGAALLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 217 NKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIH 296
Cdd:cd06534 169 HPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLVHESIY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 297 DQFLAELVkrakriklgngfhaetesgplisaehrakvekyveigleegakletggkrpedpalqngffyepTIFSNCNS 376
Cdd:cd06534 249 DEFVEKLV----------------------------------------------------------------TVLVDVDP 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 377 DMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHP-YFAQAPWGGYKQ 455
Cdd:cd06534 265 DMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGGVKN 344
|
410 420
....*....|....*....|...
gi 1803004483 456 SGFGRELGKIGLEEYTEVKHVYR 478
Cdd:cd06534 345 SGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
5-478 |
2.61e-156 |
|
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: 452.41 E-value: 2.61e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESK-ADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAP 163
Cdd:cd07139 81 ARLWTAENGMPISWSRrAQGPGPAALLRYYAALARDFPFEERRPGSGGGHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 164 ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGpGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNV 243
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 244 KKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESG 323
Cdd:cd07139 240 ARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 324 PLISAEHRAKVEKYVEIGLEEGAKLETGGKRPedPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIE 403
Cdd:cd07139 320 PLASARQRERVEGYIAKGRAEGARLVTGGGRP--AGLDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1803004483 404 LANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAqAPWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGFRLDFG-APFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
6-476 |
5.33e-153 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 445.29 E-value: 5.33e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPAL 165
Cdd:PLN02278 106 QLMTLEQGKPLKEAIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGPAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 166 AAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKK 245
Cdd:PLN02278 186 AAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAATVKR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 246 IALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPL 325
Cdd:PLN02278 266 VSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 326 ISAEHRAKVEKYVEIGLEEGAKLETGGKRpedpALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELA 405
Cdd:PLN02278 346 INEAAVQKVESHVQDAVSKGAKVLLGGKR----HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIA 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 406 NDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:PLN02278 422 NDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| HpaE |
TIGR02299 |
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the ... |
5-476 |
1.17e-152 |
|
5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase; This model represents the dehydrogenase responsible for the conversion of 5-carboxymethyl-2-hydroxymuconate semialdehyde to 5-carboxymethyl-2-hydroxymuconate (a tricarboxylic acid). This is the step in the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate following the oxidative opening of the aromatic ring.
Pssm-ID: 131352 Cd Length: 488 Bit Score: 443.86 E-value: 1.17e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:TIGR02299 3 HFIDGEFVPSESGETFETLSPATNEVLGSVARGGAADVDRAAKAAKEAFKR--WAELKAAERKRYLHKIADLIEQHADEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKADMDDIANVFQYYAGLAD--KDGgeiISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIA 162
Cdd:TIGR02299 81 AVLECLDCGQPLRQTRQQVIRAAENFRFFADKCEeaMDG---RTYPVDTHLNYTVRVPVGPVGLITPWNAPFMLSTWKIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 163 PALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGN 242
Cdd:TIGR02299 158 PALAFGNTVVLKPAEWSPLTAARLAEIAKEAGLPDGVFNLVHGFGEEAGKALVAHPDVKAVSFTGETATGSIIMRNGADT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 VKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETES 322
Cdd:TIGR02299 238 LKRFSMELGGKSPVIVFDDADLERALDAVVFMIFSFNGERCTASSRLLVQESIAEDFVEKLVERVRAIRVGHPLDPETEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 323 GPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPE---DPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEE 399
Cdd:TIGR02299 318 GPLIHPEHLAKVLGYVEAAEKEGATILVGGERAPtfrGEDLGRGNYVLPTVFTGADNHMRIAQEEIFGPVLTVIPFKDEE 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 400 EVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:TIGR02299 398 EAIEKANDTRYGLAGYVWTNDVGRAHRVALALEAGMIWVNSQNVRHLPTPFGGVKASGIGREGGTYSFDFYTETKNV 474
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
22-478 |
1.00e-150 |
|
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: 437.35 E-value: 1.00e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFdKGeWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07106 1 VINPATGEVFASAPVASEAQLDQAVAAAKAAF-PG-WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDggEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPL 181
Cdd:cd07106 79 EVGGAVAWLRYTASLDLPD--EVIEDD-DTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 182 TTIKVFKLMEEAgVPKGVANLVLGpGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKD 261
Cdd:cd07106 156 CTLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 262 ADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIG 341
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 342 LEEGAKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDI 421
Cdd:cd07106 314 KAKGAKVLAGGEPLDGP----GYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDL 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 422 EKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:cd07106 390 ERAEAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
5-480 |
2.52e-150 |
|
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: 437.66 E-value: 2.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07117 3 LFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKA-DMDDIANVFQYYAG--LADKDGGEIISSpipDSESKIIREPIGVCGQITPWNYPLLQASWKI 161
Cdd:cd07117 81 AMVETLDNGKPIRETRAvDIPLAADHFRYFAGviRAEEGSANMIDE---DTLSIVLREPIGVVGQIIPWNFPFLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 162 APALAAGNTIVMKPSEITPLTTIKVFKLMEEAgVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASG 241
Cdd:cd07117 158 APALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 242 NVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETE 321
Cdd:cd07117 237 KLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 322 SGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEV 401
Cdd:cd07117 317 MGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENGLDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803004483 402 IELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRNT 480
Cdd:cd07117 397 IDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
6-479 |
2.17e-148 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 432.54 E-value: 2.17e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIINPFNQEE-IATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEvVGTFPLSTASDVDAAVEAAREAFP--EWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPA 164
Cdd:cd07131 80 ARLVTREMGKPLAEGRGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 165 LAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVK 244
Cdd:cd07131 160 LVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPNK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 245 KIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGP 324
Cdd:cd07131 240 RVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 325 LISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIEL 404
Cdd:cd07131 320 LINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803004483 405 ANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDfhPYF---AQAPWGGYKQSGFG-RELGKIGLEEYTEVKHVYRN 479
Cdd:cd07131 400 ANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNA--PTIgaeVHLPFGGVKKSGNGhREAGTTALDAFTEWKAVYVD 476
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
5-484 |
7.29e-148 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 433.46 E-value: 7.29e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:PLN02466 60 LLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEES-KADMDDIANVFQYYAGLADKDGGEIISSPIPdSESKIIREPIGVCGQITPWNYPLLQASWKIAP 163
Cdd:PLN02466 140 AALETWDNGKPYEQSaKAELPMFARLFRYYAGWADKIHGLTVPADGP-HHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 164 ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMR-AASGN 242
Cdd:PLN02466 219 ALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLElAAKSN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 VKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETES 322
Cdd:PLN02466 299 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 323 GPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVI 402
Cdd:PLN02466 379 GPQIDSEQFEKILRYIKSGVESGATLECGGDRFGS----KGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVI 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 403 ELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRNTKP 482
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPLKN 534
|
..
gi 1803004483 483 AA 484
Cdd:PLN02466 535 PA 536
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
5-476 |
1.70e-147 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 431.17 E-value: 1.70e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:PLN02766 23 LFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKA-DMDDIANVFQYYAGLADKDGGEIISSPIPdSESKIIREPIGVCGQITPWNYPLLQASWKIAP 163
Cdd:PLN02766 103 AALDTIDAGKLFALGKAvDIPAAAGLLRYYAGAADKIHGETLKMSRQ-LQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 164 ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS-GN 242
Cdd:PLN02766 182 ALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTEVGRKIMQAAAtSN 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 VKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETES 322
Cdd:PLN02766 262 LKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQ 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 323 GPLISAEHRAKVEKYVEIGLEEGAKLETGGKrpedPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVI 402
Cdd:PLN02766 342 GPQVDKQQFEKILSYIEHGKREGATLLTGGK----PCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAI 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1803004483 403 ELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:PLN02766 418 KKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
23-477 |
2.88e-147 |
|
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: 429.07 E-value: 2.88e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 23 INPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLeRGKIVLKIAELIRRDLEELAELESLDTGKTLEESKAD 102
Cdd:cd07120 2 IDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPRL-RARVLLELADAFEANAERLARLLALENGKILGEARFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 103 MDDIANVFQYYAGLADKDGGEIISsPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLT 182
Cdd:cd07120 81 ISGAISELRYYAGLARTEAGRMIE-PEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 183 TIKVFKLMEEA-GVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKD 261
Cdd:cd07120 160 NAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 262 ADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIG 341
Cdd:cd07120 240 ADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVERA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 342 LEEGAK-LETGGKRPEDpaLQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKD 420
Cdd:cd07120 320 IAAGAEvVLRGGPVTEG--LAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 421 IEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-478 |
2.33e-146 |
|
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: 427.58 E-value: 2.33e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESK-ADMDDIANVFQYYAGLADKDGGEIISspipdseskiiREPIGVCGQITPWNYPLLQASWKIAP 163
Cdd:cd07111 102 AVLESLDNGKPIRESRdCDIPLVARHFYHHAGWAQLLDTELAG-----------WKPVGVVGQIVPWNFPLLMLAWKICP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 164 ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATvGDELAVNKDVDLISFTGGIETGKKIMRAASGNV 243
Cdd:cd07111 171 ALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 244 KKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESG 323
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 324 PLISAEHRAKVEKYVEIGLEEGAKLetggKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIE 403
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADV----FQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1803004483 404 LANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPSWEPA 480
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
57-474 |
2.82e-146 |
|
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: 425.41 E-value: 2.82e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKI 136
Cdd:cd07104 15 AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEGEILPSDVPGKESMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 137 IREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTT-IKVFKLMEEAGVPKGVANLVLGPGATVGDELA 215
Cdd:cd07104 95 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPKGVLNVVPGGGSEIGDALV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 216 VNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAI 295
Cdd:cd07104 175 EHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRILVHESV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 296 HDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRpedpalqNGFFYEPTIFSNCN 375
Cdd:cd07104 255 YDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY-------EGLFYQPTVLSDVT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 376 SDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDfHPYF--AQAPWGGY 453
Cdd:cd07104 328 PDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND-QTVNdePHVPFGGV 406
|
410 420
....*....|....*....|.
gi 1803004483 454 KQSGFGRELGKIGLEEYTEVK 474
Cdd:cd07104 407 KASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
22-476 |
1.07e-144 |
|
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: 422.55 E-value: 1.07e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP--EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPL 181
Cdd:cd07107 79 DVMVAAALLDYFAGLVTELKGETIPVG-GRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 182 TTIKVFKLMEEAgVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKD 261
Cdd:cd07107 158 SALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 262 ADLEVAVDQALNAVFFH-AGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEI 340
Cdd:cd07107 237 ADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYIDS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 341 GLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKD 420
Cdd:cd07107 317 AKREGARLVTGGGRPEGPALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTND 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1803004483 421 IEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07107 397 ISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
1-476 |
6.53e-142 |
|
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: 416.51 E-value: 6.53e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 1 MSQTLFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRD 80
Cdd:cd07140 4 MPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 81 LEELAELESLDTGK--TLEeSKADMDDIANVFQYYAGLADKDGGEIIssPIPDSESK-----IIREPIGVCGQITPWNYP 153
Cdd:cd07140 84 QEELATIESLDSGAvyTLA-LKTHVGMSIQTFRYFAGWCDKIQGKTI--PINQARPNrnltlTKREPIGVCGIVIPWNYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 154 LLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGK 233
Cdd:cd07140 161 LMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 234 KIMR-AASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKL 312
Cdd:cd07140 241 HIMKsCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 313 GNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTV 392
Cdd:cd07140 321 GDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRP----GFFFEPTVFTDVEDHMFIAKEESFGPIMII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 393 ETFSSE--EEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEY 470
Cdd:cd07140 397 SKFDDGdvDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEY 476
|
....*.
gi 1803004483 471 TEVKHV 476
Cdd:cd07140 477 LKTKTV 482
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
24-474 |
1.77e-140 |
|
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: 411.34 E-value: 1.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 24 NPFNQEEIATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADM 103
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 104 DDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTT 183
Cdd:cd07150 83 TFTPELLRAAAGECRRVRGETLPSDSPGTVSMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 184 IKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDAD 263
Cdd:cd07150 163 LKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADAD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 264 LEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLE 343
Cdd:cd07150 243 LDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQVEDAVA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 344 EGAKLETGGKRpedpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEK 423
Cdd:cd07150 323 KGAKLLTGGKY-------DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1803004483 424 CERVAARLRMGTVWINDfhPYF---AQAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:cd07150 396 AFKLAERLESGMVHIND--PTIldeAHVPFGGVKASGFGREGGEWSMEEFTELK 447
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
21-474 |
1.10e-138 |
|
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: 407.12 E-value: 1.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 21 SIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESK 100
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 101 ADMDDIANVFQYYAGLADKDGGEII-SSPIPDSESKII---REPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPS 176
Cdd:cd07145 80 VEVERTIRLFKLAAEEAKVLRGETIpVDAYEYNERRIAftvREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 177 EITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPN 256
Cdd:cd07145 160 SNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 257 IVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEK 336
Cdd:cd07145 240 IVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERMEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 337 YVEIGLEEGAKLETGGKRPEdpalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAV 416
Cdd:cd07145 320 LVNDAVEKGGKILYGGKRDE------GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1803004483 417 WSKDIEKCERVAARLRMGTVWINDFHPY-FAQAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINDSTRFrWDNLPFGGFKKSGIGREGVRYTMLEMTEEK 452
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
22-476 |
1.02e-137 |
|
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: 404.82 E-value: 1.02e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLE-ESK 100
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALRtQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 101 ADMDDIANVFQYYAGLADKDGGEIISsPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITP 180
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLP-FGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 181 LTTIKVFKLMEEAgVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFK 260
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 261 DADLEVAVDQALNAVFFH-AGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVE 339
Cdd:cd07108 237 DADLDDAVDGAIAGMRFTrQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 340 IGLEE-GAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWS 418
Cdd:cd07108 317 LGLSTsGATVLRGGPLPGEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWT 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1803004483 419 KDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIG-LEEYTEVKHV 476
Cdd:cd07108 397 RDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
6-479 |
1.81e-133 |
|
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: 394.62 E-value: 1.81e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIiNPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:cd07086 2 VIGGEWVGSGGETFTSR-NPANGEPIARVFPASPEDVEAAVAAAREAFK--EWRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPAL 165
Cdd:cd07086 79 RLVSLEMGKILPEGLGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLMEQWNPLGVVGVITAFNFPVAVPGWNAAIAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 166 AAGNTIVMKPSEITPLTTIKVFKLMEEA----GVPKGVANLVLGpGATVGDELAVNKDVDLISFTGGIETGKKIMRAASG 241
Cdd:cd07086 159 VCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTG-GGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 242 NVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETE 321
Cdd:cd07086 238 RFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 322 SGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPAlqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEV 401
Cdd:cd07086 318 VGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGGE--PGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 402 IELANDTIYGLAGAVWSKDIEKCERV--AARLRMGTVWIN------DFHpyfaqAPWGGYKQSGFGRELGKIGLEEYTEV 473
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWlgPKGSDCGIVNVNiptsgaEIG-----GAFGGEKETGGGRESGSDAWKQYMRR 470
|
....*.
gi 1803004483 474 KHVYRN 479
Cdd:cd07086 471 STCTIN 476
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
9-476 |
1.35e-132 |
|
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: 391.67 E-value: 1.35e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 9 GEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAfdKGEWSSLSGLERGKIVLKIAELIRRDLEELAELE 88
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 89 SLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAG 168
Cdd:cd07151 79 IRESGSTRIKANIEWGAAMAITREAATFPLRMEGRILPSDVPGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 169 NTIVMKPSEITPLTTIKVF-KLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIA 247
Cdd:cd07151 159 NAVVLKPASDTPITGGLLLaKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 248 LELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLIS 327
Cdd:cd07151 239 LELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLIN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 328 AEHRAKVEKYVEIGLEEGAKLETGGKRpedpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELAND 407
Cdd:cd07151 319 ESQVDGLLDKIEQAVEEGATLLVGGEA-------EGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 408 TIYGLAGAVWSKDIEKCERVAARLRMGTVWINDfHPY--FAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHIND-QPVndEPHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
5-477 |
5.46e-132 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 391.57 E-value: 5.46e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:PRK09847 22 LFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEES-KADMDDIANVFQYYAGLADKDGGEIISSPiPDSESKIIREPIGVCGQITPWNYPLLQASWKIAP 163
Cdd:PRK09847 102 ALLETLDTGKPIRHSlRDDIPGAARAIRWYAEAIDKVYGEVATTS-SHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 164 ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMR-AASGN 242
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKdAGDSN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 VKKIALELGGKNPNIVFKDA-DLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETE 321
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 322 SGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQngffyePTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEV 401
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREGESKGQLLLDGRNAGLAAAIG------PTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1803004483 402 IELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIW 490
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
22-476 |
2.41e-128 |
|
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: 380.40 E-value: 2.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDKGewSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07149 3 VISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEM--KSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEIIssPI---PDSESKI---IREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKP 175
Cdd:cd07149 81 EVDRAIETLRLSAEEAKRLAGETI--PFdasPGGEGRIgftIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 176 SEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASgnVKKIALELGGKNP 255
Cdd:cd07149 159 ASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 256 NIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVE 335
Cdd:cd07149 237 VIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 336 KYVEIGLEEGAKLETGGKRpedpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGA 415
Cdd:cd07149 317 EWVEEAVEGGARLLTGGKR-------DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1803004483 416 VWSKDIEKCERVAARLRMGTVWINDFHPY-FAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07149 390 VFTNDLQKALKAARELEVGGVMINDSSTFrVDHMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
57-476 |
2.72e-128 |
|
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: 380.41 E-value: 2.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADK--DGGEIISSPI-PDSE 133
Cdd:cd07099 33 AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVLLALEAIDWAARNAPRvlAPRKVPTGLLmPNKK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 134 SKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATvGDE 213
Cdd:cd07099 113 ATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 214 LaVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVED 293
Cdd:cd07099 192 L-IDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 294 AIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPalqnGFFYEPTIFSN 373
Cdd:cd07099 271 SVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGG----GPFYEPTVLTD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 374 CNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDfHPYFA---QAPW 450
Cdd:cd07099 347 VPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSIND-VLLTAgipALPF 425
|
410 420
....*....|....*....|....*.
gi 1803004483 451 GGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07099 426 GGVKDSGGGRRHGAEGLREFCRPKAI 451
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
6-474 |
3.00e-128 |
|
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: 381.41 E-value: 3.00e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEES-KADMDDIANVFQYYAGLADKDGGEIiSSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPA 164
Cdd:cd07116 82 VAETWDNGKPVRETlAADIPLAIDHFRYFAGCIRAQEGSI-SEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 165 LAAGNTIVMKPSEITPLTtikVFKLMEEAG--VPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGN 242
Cdd:cd07116 161 LAAGNCVVLKPAEQTPAS---ILVLMELIGdlLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYASEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 VKKIALELGGKNPNIVFKD--ADLEVAVDQALN--AVF-FHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFH 317
Cdd:cd07116 238 IIPVTLELGGKSPNIFFADvmDADDAFFDKALEgfVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 318 AETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNsDMRIVQEEVFGPVLTVETFSS 397
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGLLGGGYYVPTTFKGGN-KMRIFQEEIFGPVLAVTTFKD 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 398 EEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:cd07116 397 EEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTK 473
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
5-476 |
1.22e-126 |
|
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: 377.17 E-value: 1.22e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDkGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKA-DMDDIANVFQYYAGLADKDGGEIISSPIPDSESK-----IIREPIGVCGQITPWNYPLLQAS 158
Cdd:cd07113 81 AQLETLCSGKSIHLSRAfEVGQSANFLRYFAGWATKINGETLAPSIPSMQGErytafTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 159 WKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGAtVGDELAVNKDVDLISFTGGIETGKKIMRA 238
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGA-VGAQLISHPDVAKVSFTGSVATGKKIGRQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 239 ASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHA 318
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 319 ETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEdpalQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSE 398
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALA----GEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDE 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1803004483 399 EEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINdFHPYF-AQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN-MHTFLdPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
20-476 |
6.54e-126 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 376.91 E-value: 6.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 20 RSIINPFNQEEIATVSEGGREDAIKAiaaarraFDK-----GEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGK 94
Cdd:PRK09407 34 REVTAPFTGEPLATVPVSTAADVEAA-------FARaraaqRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 95 T----LEESKadmdDIANVFQYYAG-----LADKDggeiISSPIPD-SESKIIREPIGVCGQITPWNYPLLQASWKIAPA 164
Cdd:PRK09407 107 ArrhaFEEVL----DVALTARYYARrapklLAPRR----RAGALPVlTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 165 LAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNkdVDLISFTGGIETGKKIMRAASGNVK 244
Cdd:PRK09407 179 LLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAGRRLI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 245 KIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGP 324
Cdd:PRK09407 257 GFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 325 LISAEHRAKVEKYVEIGLEEGAKLETGGKRPED--PalqngFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVI 402
Cdd:PRK09407 337 LISEAQLETVSAHVDDAVAKGATVLAGGKARPDlgP-----LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAV 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 403 ELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND-FHPYFA--QAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:PRK09407 412 ERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEgYAAAWGsvDAPMGGMKDSGLGRRHGAEGLLKYTESQTI 488
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
5-470 |
4.87e-124 |
|
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: 371.56 E-value: 4.87e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEkEQIRSIiNPFNQEEI-ATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEE 83
Cdd:cd07124 35 LVIGGKEVRTE-EKIESR-NPADPSEVlGTVQKATKEEAEAAVQAARAAFP--TWRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 84 LAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIiSSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAP 163
Cdd:cd07124 111 LAAWMVLEVGKNWAEADADVAEAIDFLEYYAREMLRLRGFP-VEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 164 ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS--- 240
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkvq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 241 ---GNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFH 317
Cdd:cd07124 270 pgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 318 AETESGPLISAEHRAKVEKYVEIGLEEGaKLETGGKRPEDPAlqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSS 397
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEVLELAA--EGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 398 EEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN--------DFHPYfaqapwGGYKQSGFGrelGKIGLEE 469
Cdd:cd07124 427 FDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkitgalvGRQPF------GGFKMSGTG---SKAGGPD 497
|
.
gi 1803004483 470 Y 470
Cdd:cd07124 498 Y 498
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
23-476 |
2.15e-123 |
|
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: 367.79 E-value: 2.15e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 23 INPFNQEEIATVSEGGREDAIKAIAAARRAfdKGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKAD 102
Cdd:cd07101 1 EAPFTGEPLGELPQSTPADVEAAFARARAA--QRAWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 103 MDDIANVFQYYAGLADKD-GGEIISSPIPD-SESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITP 180
Cdd:cd07101 79 VLDVAIVARYYARRAERLlKPRRRRGAIPVlTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 181 LTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNkdVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFK 260
Cdd:cd07101 159 LTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 261 DADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEI 340
Cdd:cd07101 237 DADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 341 GLEEGAKLETGGK-RPE-DPalqngFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWS 418
Cdd:cd07101 317 AVAKGATVLAGGRaRPDlGP-----YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 419 KDIEKCERVAARLRMGTVWIND-FHPYFA--QAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07101 392 RDGARGRRIAARLRAGTVNVNEgYAAAWAsiDAPMGGMKDSGLGRRHGAEGLLKYTETQTV 452
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
57-477 |
3.13e-123 |
|
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: 366.40 E-value: 3.13e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAG-----LADkdggEIIssPIPD 131
Cdd:cd07100 14 AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAEnaeafLAD----EPI--ETDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGV-ANLVLGPGATv 210
Cdd:cd07100 88 GKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVfQNLLIDSDQV- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 211 gDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLL 290
Cdd:cd07100 167 -EAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAAKRFI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 291 VEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPalqnGFFYEPTI 370
Cdd:cd07100 246 VHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGP----GAFYPPTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 371 FSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPW 450
Cdd:cd07100 322 LTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRLPF 401
|
410 420
....*....|....*....|....*..
gi 1803004483 451 GGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07100 402 GGVKRSGYGRELGRFGIREFVNIKTVW 428
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
22-476 |
1.49e-120 |
|
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: 360.59 E-value: 1.49e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07094 3 VHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEIIssPIPDSESK------IIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKP 175
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIRGEEI--PLDATQGSdnrlawTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 176 SEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGnvKKIALELGGKNP 255
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 256 NIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVE 335
Cdd:cd07094 237 VIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 336 KYVEIGLEEGAKLETGGKRpedpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGA 415
Cdd:cd07094 317 RWVEEAVEAGARLLCGGER-------DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1803004483 416 VWSKDIEKCERVAARLRMGTVWINDfHPYFAQ--APWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVND-SSAFRTdwMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
72-477 |
7.51e-117 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 349.42 E-value: 7.51e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 72 KIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWN 151
Cdd:PRK10090 3 KIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPGENILLFKRALGVTTGILPWN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 152 YPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIET 231
Cdd:PRK10090 83 FPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGSVSA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 232 GKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIK 311
Cdd:PRK10090 163 GEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 312 LGNGFHAET-ESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEdpalQNGFFYEPTIFSNCNSDMRIVQEEVFGPVL 390
Cdd:PRK10090 243 FGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVE----GKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 391 TVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEY 470
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKHGLHEY 398
|
....*..
gi 1803004483 471 TEVKHVY 477
Cdd:PRK10090 399 LQTQVVY 405
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
57-476 |
2.07e-115 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 346.49 E-value: 2.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKI 136
Cdd:cd07105 15 AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLITQIIGGSIPSDKPGTLAMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 137 IREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVL-GP--GATVGDE 213
Cdd:cd07105 95 VKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVThSPedAPEVVEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 214 LAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVED 293
Cdd:cd07105 175 LIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFLNSGQICMSTERIIVHE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 294 AIHDQFLAELVKRAKRIKLGNgfhaeTESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPalqNGFFYEPTIFSN 373
Cdd:cd07105 255 SIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADESP---SGTSMPPTILDN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 374 CNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN-----DfhpyFAQA 448
Cdd:cd07105 327 VTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHINgmtvhD----EPTL 402
|
410 420
....*....|....*....|....*...
gi 1803004483 449 PWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07105 403 PHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
3-476 |
1.87e-111 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 338.42 E-value: 1.87e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 3 QTLFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLE 82
Cdd:PRK11241 11 QQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALPA--WRALTAKERANILRRWFNLMMEHQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 83 ELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIA 162
Cdd:PRK11241 89 DLARLMTLEQGKPLAEAKGEISYAASFIEWFAEEGKRIYGDTIPGHQADKRLIVIKQPIGVTAAITPWNFPAAMITRKAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 163 PALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGN 242
Cdd:PRK11241 169 PALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAKD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 VKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETES 322
Cdd:PRK11241 249 IKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTI 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 323 GPLISAEHRAKVEKYVEIGLEEGAKLETGGKrpedPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVI 402
Cdd:PRK11241 329 GPLIDEKAVAKVEEHIADALEKGARVVCGGK----AHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVI 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1803004483 403 ELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:PRK11241 405 AQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYM 478
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
21-474 |
2.47e-110 |
|
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: 334.33 E-value: 2.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 21 SIINPFNQEEIATVSEGGREDAIKAIAAARrafdkGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESK 100
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAA-----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 101 ADMDDIANVFQYYAGLADKDGGEIISSPI--PDSESKII--REPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPS 176
Cdd:cd07146 77 YEVGRAADVLRFAAAEALRDDGESFSCDLtaNGKARKIFtlREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 177 EITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKImrAASGNVKKIALELGGKNPN 256
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI--AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 257 IVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEK 336
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 337 YVEIGLEEGAKLETGGKRpedpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAV 416
Cdd:cd07146 315 RVEEAIAQGARVLLGNQR-------QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGV 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 417 WSKDIEKCERVAARLRMGTVWINDFhPYF--AQAPWGGYKQSGFG-RELGKIGLEEYTEVK 474
Cdd:cd07146 388 CTNDLDTIKRLVERLDVGTVNVNEV-PGFrsELSPFGGVKDSGLGgKEGVREAMKEMTNVK 447
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
5-476 |
6.18e-109 |
|
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: 331.79 E-value: 6.18e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07085 3 LFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPA 164
Cdd:cd07085 81 ARLITLEHGKTLADARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 165 LAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVgDELAVNKDVDLISFTGGIETGKKIMRAASGNVK 244
Cdd:cd07085 161 IACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAV-NALLDHPDIKAVSFVGSTPVGEYIYERAAANGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 245 KIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGP 324
Cdd:cd07085 240 RVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 325 LISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIEL 404
Cdd:cd07085 320 VISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPGYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAI 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803004483 405 ANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHP----YFaqaPWGGYKQSGFG--RELGKIGLEEYTEVKHV 476
Cdd:cd07085 400 INANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVPIPvplaFF---SFGGWKGSFFGdlHFYGKDGVRFYTQTKTV 474
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
23-477 |
6.67e-109 |
|
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: 330.75 E-value: 6.67e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 23 INPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKAD 102
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 103 MDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLT 182
Cdd:cd07102 79 IRGMLERARYMISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 183 TIKVFKLMEEAGVPKGVANLVLGPGATvGDELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDA 262
Cdd:cd07102 159 GERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 263 DLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGL 342
Cdd:cd07102 238 DLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 343 EEGAKLETGGKRpEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIE 422
Cdd:cd07102 318 AKGARALIDGAL-FPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1803004483 423 KCERVAARLRMGTVWIN--DF-HPYFaqaPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:cd07102 397 RAEALGEQLETGTVFMNrcDYlDPAL---AWTGVKDSGRGVTLSRLGYDQLTRPKSYH 451
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
57-472 |
1.37e-106 |
|
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: 324.63 E-value: 1.37e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPiPDSESKI 136
Cdd:cd07152 28 AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSA-PGRLSLA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 137 IREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTT-IKVFKLMEEAGVPKGVANlVLGPGATVGDELA 215
Cdd:cd07152 107 RRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLH-VLPGGADAGEALV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 216 VNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAI 295
Cdd:cd07152 186 EDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 296 HDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRpedpalqNGFFYEPTIFSNCN 375
Cdd:cd07152 266 ADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGTY-------DGLFYRPTVLSGVK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 376 SDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND---FHPyfAQAPWGG 452
Cdd:cd07152 339 PGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDqtvNDE--PHNPFGG 416
|
410 420
....*....|....*....|.
gi 1803004483 453 YKQSGFG-RELGKIGLEEYTE 472
Cdd:cd07152 417 MGASGNGsRFGGPANWEEFTQ 437
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
5-457 |
3.93e-105 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 323.04 E-value: 3.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEkEQIRSIiNPFNQEE-IATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEE 83
Cdd:PRK03137 39 LIIGGERITTE-DKIVSI-NPANKSEvVGRVSKATKELAEKAMQAALEAFE--TWKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 84 LAELESLDTGKTLEESKADMDDIANVFQYYA--GLADKDGGEIIssPIPDSESKIIREPIGVCGQITPWNYPLLQASWKI 161
Cdd:PRK03137 115 FSAWLVKEAGKPWAEADADTAEAIDFLEYYArqMLKLADGKPVE--SRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 162 APALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIM-RAAS 240
Cdd:PRK03137 193 LAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYeRAAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 241 GN-----VKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNG 315
Cdd:PRK03137 273 VQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 316 FHAeTESGPLISAEHRAKVEKYVEIGLEEGaKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETF 395
Cdd:PRK03137 353 EDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSK----GYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 396 SSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN--------DFHPYfaqapwGGYKQSG 457
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgctgaivGYHPF------GGFNMSG 490
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
6-461 |
3.53e-100 |
|
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: 309.12 E-value: 3.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIrSIINPFNQEEIATVSEGGREDAIKAIAAARRAFdKGEWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:cd07082 5 LINGEWKESSGKTI-EVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKEEVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEESKADMDDIANVFQYyaglADKDGGEIISSPIP--------DSESKIIREPIGVCGQITPWNYPLLQA 157
Cdd:cd07082 83 NLLMWEIGKTLKDALKEVDRTIDYIRD----TIEELKRLDGDSLPgdwfpgtkGKIAQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 158 SWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMR 237
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 238 AASgnVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFH 317
Cdd:cd07082 239 QHP--MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 318 AETESGPLISaEHRAK-VEKYVEIGLEEGAKLETGGKRpedpalQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFS 396
Cdd:cd07082 317 NGVDITPLID-PKSADfVEGLIDDAVAKGATVLNGGGR------EGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 397 SEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDfHP-----YFaqaPWGGYKQSGFGRE 461
Cdd:cd07082 390 DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINS-KCqrgpdHF---PFLGRKDSGIGTQ 455
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
22-474 |
3.94e-99 |
|
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: 305.71 E-value: 3.94e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKA 101
Cdd:cd07147 3 VTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 102 DMDDIANVFQYYAGLADKDGGEII---SSPIPDSESKIIRE-PIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSE 177
Cdd:cd07147 81 EVARAIDTFRIAAEEATRIYGEVLpldISARGEGRQGLVRRfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 178 ITPLTTIKVFKLMEEAGVPKGVANLVlgPGATVG-DELAVNKDVDLISFTGGIETGKKIMRAASGnvKKIALELGGKNPN 256
Cdd:cd07147 161 RTPLSALILGEVLAETGLPKGAFSVL--PCSRDDaDLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 257 IVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEK 336
Cdd:cd07147 237 IVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 337 YVEIGLEEGAKLETGGKRpedpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAV 416
Cdd:cd07147 317 WVNEAVDAGAKLLTGGKR-------DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 417 WSKDIEKCERVAARLRMGTVWINDFhPYFA--QAPWGGYKQSGFGRELGKIGLEEYTEVK 474
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVINDV-PTFRvdHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
5-479 |
8.43e-93 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 291.38 E-value: 8.43e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKeQIRSIiNPFNQEE-IATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEE 83
Cdd:TIGR01237 35 LVINGERVETEN-KIVSI-NPCDKSEvVGTVSKASQEHAEHALQAAAKAFE--AWKKTDPEERAAILFKAAAIVRRRRHE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 84 LAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAP 163
Cdd:TIGR01237 111 FSALLVKEVGKPWNEADAEVAEAIDFMEYYARQMIELAKGKPVNSREGETNQYVYTPTGVTVVISPWNFPFAIMVGMTVA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 164 ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS--- 240
Cdd:TIGR01237 191 PIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGSREVGTRIFERAAkvq 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 241 ---GNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFH 317
Cdd:TIGR01237 271 pgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVERFVEITESLKVGPPDS 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 318 AETESGPLISAEHRAKVEKYVEIGLEEGaKLETGGKrpEDPAlqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSS 397
Cdd:TIGR01237 351 ADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGC--GDDS--KGYFIGPTIFADVDRKARLAQEEIFGPVVAFIRASD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 398 EEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN--------DFHPYfaqapwGGYKQSGFGRELGKIG-LE 468
Cdd:TIGR01237 426 FDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNrnitgaivGYQPF------GGFKMSGTDSKAGGPDyLA 499
|
490
....*....|.
gi 1803004483 469 EYTEVKHVYRN 479
Cdd:TIGR01237 500 LFMQAKTVTEM 510
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
139-476 |
1.70e-90 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 283.81 E-value: 1.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 139 EPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEA----GVPKGVANLVLGPGATvGDEL 214
Cdd:cd07098 119 EPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEAL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 215 AVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDA 294
Cdd:cd07098 198 TSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEK 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 295 IHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNC 374
Cdd:cd07098 278 IYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHPEYPQGHYFPPTLLVDV 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 375 NSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHP-YFAQA-PWGG 452
Cdd:cd07098 358 TPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVnYYVQQlPFGG 437
|
330 340
....*....|....*....|....
gi 1803004483 453 YKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07098 438 VKGSGFGRFAGEEGLRGLCNPKSV 461
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
5-463 |
1.01e-84 |
|
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: 269.83 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIrsIINPFNQ-EEIATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRDLEE 83
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPFAPsEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 84 LAELESLDTGKTLEESKADMDDIANVFQYYAGLADK-DGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIA 162
Cdd:cd07083 97 LIATLTYEVGKNWVEAIDDVAEAIDFIRYYARAALRlRYPAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 163 PALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASGN 242
Cdd:cd07083 177 APVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 243 ------VKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGF 316
Cdd:cd07083 257 apgqtwFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 317 HAETESGPLISAEHRAKVEKYVEIGLEEGaKLETGGKRPEDpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFS 396
Cdd:cd07083 337 ENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEG----EGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYK 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 397 SEE--EVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND--FHPYFAQAPWGGYKQSGFGRELG 463
Cdd:cd07083 412 DDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRkiTGALVGVQPFGGFKLSGTNAKTG 482
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
6-486 |
8.97e-81 |
|
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: 260.21 E-value: 8.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEwiSAEKEQIRSIINPFNQEE-IATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:cd07125 36 IINGE--ETETGEGAPVIDPADHERtIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKADMD---DIANvfqYYAGLADKDGGEIISsPIPDSESKIIR-EPIGVCGQITPWNYPLLQASWK 160
Cdd:cd07125 112 IALAAAEAGKTLADADAEVReaiDFCR---YYAAQARELFSDPEL-PGPTGELNGLElHGRGVFVCISPWNFPLAIFTGQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 161 IAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS 240
Cdd:cd07125 188 IAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRALA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 241 GN----VKKIAlELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGF 316
Cdd:cd07125 268 ERdgpiLPLIA-ETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 317 HAETESGPLISAEHRAKVEKYVEIGLEEGAKLEtggkrPEDPALQNGFFYEPTIFSNCNSDmrIVQEEVFGPVLTVETFS 396
Cdd:cd07125 347 DLSTDVGPLIDKPAGKLLRAHTELMRGEAWLIA-----PAPLDDGNGYFVAPGIIEIVGIF--DLTTEVFGPILHVIRFK 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 397 SE--EEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDfhpyfAQA-------PWGGYKQSGFGRelgKIG- 466
Cdd:cd07125 420 AEdlDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINR-----NITgaivgrqPFGGWGLSGTGP---KAGg 491
|
490 500
....*....|....*....|...
gi 1803004483 467 ---LEEYTEVKHVYRNTKPAAVN 486
Cdd:cd07125 492 pnyLLRFGNEKTVSLNTTAAGGN 514
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
8-426 |
1.97e-80 |
|
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: 257.91 E-value: 1.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 8 DGEWISAEKEQirSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAEL 87
Cdd:cd07130 4 DGEWGGGGGVV--TSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 88 ESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDsesKIIRE---PIGVCGQITPWNYPLLQASWKIAPA 164
Cdd:cd07130 80 VSLEMGKILPEGLGEVQEMIDICDFAVGLSRQLYGLTIPSERPG---HRMMEqwnPLGVVGVITAFNFPVAVWGWNAAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 165 LAAGNTIVMKPSEITPLTTIKVFKLMEEA----GVPKGVANLVLGpGATVGDELAVNKDVDLISFTGGIETGKKIMRAAS 240
Cdd:cd07130 157 LVCGNVVVWKPSPTTPLTAIAVTKIVARVleknGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 241 GNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAET 320
Cdd:cd07130 236 ARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 321 ESGPLISaehRAKVEKY---VEIGLEEGAKLETGGKRPEDPalqnGFFYEPTIFSNcNSDMRIVQEEVFGPVLTVETFSS 397
Cdd:cd07130 316 LVGPLHT---KAAVDNYlaaIEEAKSQGGTVLFGGKVIDGP----GNYVEPTIVEG-LSDAPIVKEETFAPILYVLKFDT 387
|
410 420
....*....|....*....|....*....
gi 1803004483 398 EEEVIELANDTIYGLAGAVWSKDIEKCER 426
Cdd:cd07130 388 LEEAIAWNNEVPQGLSSSIFTTDLRNAFR 416
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
57-460 |
4.58e-80 |
|
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: 255.66 E-value: 4.58e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIAN-----VFQYYAGLADKDggeiisSPIPD 131
Cdd:cd07095 15 GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEVAAMAGkidisIKAYHERTGERA------TPMAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGpGATVG 211
Cdd:cd07095 89 GRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQG-GRETG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 212 DELAVNKDVDLISFTGGIETGKKIMRAASGNVKKI-ALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLL 290
Cdd:cd07095 168 EALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKIlALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRCTCARRLI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 291 VED-AIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEdpalQNGFFYEPT 369
Cdd:cd07095 248 VPDgAVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLV----AGTAFLSPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 370 IFSncNSDMRIVQ-EEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINdfHPY-FA- 446
Cdd:cd07095 324 IID--VTDAADVPdEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWN--RPTtGAs 399
|
410
....*....|....*
gi 1803004483 447 -QAPWGGYKQSGFGR 460
Cdd:cd07095 400 sTAPFGGVGLSGNHR 414
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
23-477 |
7.56e-80 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 255.82 E-value: 7.56e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 23 INPFNQEEIATVSEGGREDAIKAIAAARRAFDKGEWSSLSglERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKAD 102
Cdd:PRK09406 6 INPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFA--QRARWANAAADLLEAEADQVAALMTLEMGKTLASAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 103 MDDIANVFQYYAG-----LADKDGGeiiSSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSE 177
Cdd:PRK09406 84 ALKCAKGFRYYAEhaealLADEPAD---AAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 178 ITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAvNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNI 257
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILR-DPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 258 VFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKY 337
Cdd:PRK09406 240 VMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 338 VEIGLEEGAKLETGGKRPEDPalqnGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVW 417
Cdd:PRK09406 320 VDDAVAAGATILCGGKRPDGP----GWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 418 SKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVY 477
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTVW 455
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
5-476 |
3.90e-77 |
|
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, methylmalonate-semialdehyde dehydrogenase catalyzes the irreversible NAD+- and CoA-dependent oxidative decarboxylation of methylmalonate semialdehyde to propionyl-CoA. Methylmalonate-semialdehyde dehydrogenase has been characterized in both prokaryotes and eukaryotes, functioning as a mammalian tetramer and a bacterial homodimer. Although similar in monomeric molecular mass and enzymatic activity, the N-terminal sequence in P.aeruginosa does not correspond with the N-terminal sequence predicted for rat liver. Sequence homology to a variety of prokaryotic and eukaryotic aldehyde dehydrogenases places MMSDH in the aldehyde dehydrogenase (NAD+) superfamily (pfam00171), making MMSDH's CoA requirement unique among known ALDHs. Methylmalonate semialdehyde dehydrogenase is closely related to betaine aldehyde dehydrogenase, 2-hydroxymuconic semialdehyde dehydrogenase, and class 1 and 2 aldehyde dehydrogenase. In Bacillus, a highly homologous protein to methylmalonic acid semialdehyde dehydrogenase, groups out from the main MMSDH clade with Listeria and Sulfolobus. This Bacillus protein has been suggested to be located in an iol operon and/or involved in myo-inositol catabolism, converting malonic semialdehyde to acetyl CoA ad CO2. The preceeding enzymes responsible for valine catabolism are present in Bacillus, Listeria, and Sulfolobus. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130783 Cd Length: 477 Bit Score: 249.41 E-value: 3.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRDLEEL 84
Cdd:TIGR01722 3 HWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF--LTWGQTSLAQRTSVLLRYQALLKEHRDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 85 AELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPA 164
Cdd:TIGR01722 81 AELITAEHGKTHSDALGDVARGLEVVEHACGVNSLLKGETSTQVATRVDVYSIRQPLGVCAGITPFNFPAMIPLWMFPIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 165 LAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVgDELAVNKDVDLISFTGGIETGKKIMRAASGNVK 244
Cdd:TIGR01722 161 IACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHGDKEAV-DRLLEHPDVKAVSFVGSTPIGRYIHTTGSAHGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 245 KIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIhDQFLAELVKRAKRIKLGNGFHAETESGP 324
Cdd:TIGR01722 240 RVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAISAAVLVGAA-DEWVPEIRERAEKIRIGPGDDPGAEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 325 LISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIEL 404
Cdd:TIGR01722 319 LITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYEEGNWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEAIAL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1803004483 405 ANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHP----YFAqapWGGYKQSGFG--RELGKIGLEEYTEVKHV 476
Cdd:TIGR01722 399 INASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVNVPIPvplpYFS---FTGWKDSFFGdhHIYGKQGTHFYTRGKTV 473
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
23-479 |
2.44e-73 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 238.99 E-value: 2.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 23 INPFNQEEIATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKAD 102
Cdd:PRK13968 12 VNPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 103 MDDIANVFQYYAgladkDGGEIISSPIP----DSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEI 178
Cdd:PRK13968 90 VAKSANLCDWYA-----EHGPAMLKAEPtlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 179 TPLTTIKVFKLMEEAGVPKGVANLVLGPGATVgdELAVNKD-VDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNI 257
Cdd:PRK13968 165 VMGCAQLIAQVFKDAGIPQGVYGWLNADNDGV--SQMINDSrIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 258 VFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKY 337
Cdd:PRK13968 243 VLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 338 VEIGLEEGAKLETGGKRPEDpalqNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVW 417
Cdd:PRK13968 323 VEATLAEGARLLLGGEKIAG----AGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIF 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1803004483 418 SKDIEKCERVAARLRMGTVWINDFHPYFAQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYRN 479
Cdd:PRK13968 399 TTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTVWKD 460
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
132-478 |
1.59e-69 |
|
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: 227.79 E-value: 1.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQAswkIAP---ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVAnLVLGpGA 208
Cdd:cd07087 92 AKAYVIPEPLGVVLIIGPWNYPLQLA---LAPligAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA-VVEG-GV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 209 TVGDELAVNKdVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSR 288
Cdd:cd07087 167 EVATALLAEP-FDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 289 LLVEDAIHDQFLAELVKRAKRiKLGNGFHAETESGPLISAEHRAKVEKYVeigleEGAKLETGGKRpeDPALQngfFYEP 368
Cdd:cd07087 246 VLVHESIKDELIEELKKAIKE-FYGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQV--DKEER---YIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 369 TIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND--FHPYFA 446
Cdd:cd07087 315 TILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDvlLHAAIP 394
|
330 340 350
....*....|....*....|....*....|..
gi 1803004483 447 QAPWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:cd07087 395 NLPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
125-478 |
1.73e-69 |
|
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: 228.26 E-value: 1.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 125 ISSPI--PDSESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVAnL 202
Cdd:cd07134 83 VRTPLllFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVA-V 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 203 VLGpGATVGDELaVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQV 282
Cdd:cd07134 162 FEG-DAEVAQAL-LELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 283 CSAGSRLLVEDAIHDQFLAELVKRAKRIkLGNGFHAETES--GPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPAl 360
Cdd:cd07134 240 CIAPDYVFVHESVKDAFVEHLKAEIEKF-YGKDAARKASPdlARIVNDRHFDRLKGLLDDAVAKGAKVEFGGQFDAAQR- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 361 qngfFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND 440
Cdd:cd07134 318 ----YIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVND 393
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1803004483 441 -----FHPyfaQAPWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:cd07134 394 vvlhfLNP---NLPFGGVNNSGIGSYHGVYGFKAFSHERAVLR 433
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
22-466 |
3.13e-68 |
|
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: 225.38 E-value: 3.13e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 22 IINPFNQEEIATVSEGGREDAIKAIAAARRAF-DKGEWssLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESK 100
Cdd:cd07148 3 VVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 101 ADMDD-IANVFQYYAGLADKDGGEIISSPIPDSESKI---IREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPS 176
Cdd:cd07148 81 VEVTRaIDGVELAADELGQLGGREIPMGLTPASAGRIaftTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 177 EITPLTTIKVFKLMEEAGVPKGVANLVLgPGATVGDELAVNKDVDLISFTGGIETGKKI-MRAASGNvkKIALELGGKNP 255
Cdd:cd07148 161 LATPLSCLAFVDLLHEAGLPEGWCQAVP-CENAVAEKLVTDPRVAFFSFIGSARVGWMLrSKLAPGT--RCALEHGGAAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 256 NIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVE 335
Cdd:cd07148 238 VIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREVDRVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 336 KYVEIGLEEGAKLETGGKRPEDPAlqngffYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGA 415
Cdd:cd07148 318 EWVNEAVAAGARLLCGGKRLSDTT------YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAA 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1803004483 416 VWSKDIEKCERVAARLRMGTVWINDfHPYFAQ--APWGGYKQSGFGreLGKIG 466
Cdd:cd07148 392 VFTKDLDVALKAVRRLDATAVMVND-HTAFRVdwMPFAGRRQSGYG--TGGIP 441
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
6-486 |
3.40e-67 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 226.55 E-value: 3.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPL--WRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPAL 165
Cdd:PLN02419 195 MNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAV 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 166 AAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVgDELAVNKDVDLISFTGGIETGKKIMRAASGNVKK 245
Cdd:PLN02419 275 TCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTV-NAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKR 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 246 IALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLL-VEDAihDQFLAELVKRAKRIKLGNGFHAETESGP 324
Cdd:PLN02419 354 IQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVfVGDA--KSWEDKLVERAKALKVTCGSEPDADLGP 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 325 LISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIEL 404
Cdd:PLN02419 432 VISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 405 ANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINdfHPYFAQAPWGGY--KQSGFGREL---GKIGLEEYTEVKHVYRN 479
Cdd:PLN02419 512 INKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGIN--VPIPVPLPFFSFtgNKASFAGDLnfyGKAGVDFFTQIKLVTQK 589
|
....*....
gi 1803004483 480 TK--PAAVN 486
Cdd:PLN02419 590 QKdiHSPFS 598
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
4-457 |
1.28e-65 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 219.44 E-value: 1.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 4 TLFIDGEWISAEKEQIRSIiNPFNQEEI-----ATVseggrEDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIR 78
Cdd:PRK09457 2 TLWINGDWIAGQGEAFESR-NPVSGEVLwqgndATA-----AQVDAAVRAARAAFP--AWARLSFEERQAIVERFAALLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 79 RDLEELAELESLDTGKTLEESK----ADMDDIANVFQYYAgladKDGGEIiSSPIPDSESKIIREPIGVCGQITPWNYPL 154
Cdd:PRK09457 74 ENKEELAEVIARETGKPLWEAAtevtAMINKIAISIQAYH----ERTGEK-RSEMADGAAVLRHRPHGVVAVFGPYNFPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 155 LQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGpGATVGDELAVNKDVDLISFTGGIETGKK 234
Cdd:PRK09457 149 HLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 235 IMRAASGNVKKI-ALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIH-DQFLAELVKRAKRIKL 312
Cdd:PRK09457 228 LHRQFAGQPEKIlALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 313 GnGFHAETES--GPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDpalQNGFFyEPTIFsncnsDMRIVQ----EEVF 386
Cdd:PRK09457 308 G-RWDAEPQPfmGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQA---GTGLL-TPGII-----DVTGVAelpdEEYF 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1803004483 387 GPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTV-WINDFHPYFAQAPWGGYKQSG 457
Cdd:PRK09457 378 GPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
132-478 |
5.52e-63 |
|
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: 211.19 E-value: 5.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQAswkIAP---ALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVAnLVLGpGA 208
Cdd:cd07133 93 AKAEVEYQPLGVVGIIVPWNYPLYLA---LGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVA-VVTG-GA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 209 TVGDELAvNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSR 288
Cdd:cd07133 168 DVAAAFS-SLPFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQTCVAPDY 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 289 LLVEDAIHDQFLAELVKRAKRiklgngFHAETESGP----LISAEHRAKVEKYVEIGLEEGAKLETGGkrPEDPALQNGF 364
Cdd:cd07133 247 VLVPEDKLEEFVAAAKAAVAK------MYPTLADNPdytsIINERHYARLQGLLEDARAKGARVIELN--PAGEDFAATR 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 365 FYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND--FH 442
Cdd:cd07133 319 KLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDtlLH 398
|
330 340 350
....*....|....*....|....*....|....*...
gi 1803004483 443 pyFAQ--APWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:cd07133 399 --VAQddLPFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
132-489 |
3.69e-62 |
|
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: 209.28 E-value: 3.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQAswkIAP---ALAAGNTIVMKPSEITPLTTIKVFKLMEEAgVPKGVANLVLGpGA 208
Cdd:cd07136 92 SKSYIYYEPYGVVLIIAPWNYPFQLA---LAPligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-GV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 209 TVGDELaVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSR 288
Cdd:cd07136 167 EENQEL-LDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDY 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 289 LLVEDAIHDQFLAELVkraKRIKLGNGFHAETES--GPLISAEHRAKVEKYVEIGleegaKLETGGKRPEDpalqnGFFY 366
Cdd:cd07136 246 VLVHESVKEKFIKELK---EEIKKFYGEDPLESPdyGRIINEKHFDRLAGLLDNG-----KIVFGGNTDRE-----TLYI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 367 EPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND--FH-- 442
Cdd:cd07136 313 EPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDtiMHla 392
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1803004483 443 -PYFaqaPWGGYKQSGFGRELGKIGLEEYTEVKHVYRNTkpaavNWFN 489
Cdd:cd07136 393 nPYL---PFGGVGNSGMGSYHGKYSFDTFSHKKSILKKS-----TWFD 432
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
6-439 |
6.81e-60 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 212.37 E-value: 6.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEW-----ISAEKEQiRSIINPFNQEE-IATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRR 79
Cdd:PRK11904 546 FLEKQWqagpiINGEGEA-RPVVSPADRRRvVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEA 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 80 DLEELAELESLDTGKTLEeskadmDDIANV-----F-QYYAGLADKDGGEIISSPIPDSESKIIR-EPIGV--CgqITPW 150
Cdd:PRK11904 623 NRAELIALCVREAGKTLQ------DAIAEVreavdFcRYYAAQARRLFGAPEKLPGPTGESNELRlHGRGVfvC--ISPW 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 151 NYPLL----QaswkIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFT 226
Cdd:PRK11904 695 NFPLAiflgQ----VAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFT 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 227 GGIETGKKIMR--AASGN--VKKIAlELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAE 302
Cdd:PRK11904 771 GSTETARIINRtlAARDGpiVPLIA-ETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQEDIADRVIEM 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 303 LVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEiGLEEGAKLetGGKRPEDPALQNGFFYEPTIFSncNSDMRIVQ 382
Cdd:PRK11904 850 LKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIE-RMKREARL--LAQLPLPAGTENGHFVAPTAFE--IDSISQLE 924
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1803004483 383 EEVFGPVLTVETFSSEE--EVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN 439
Cdd:PRK11904 925 REVFGPILHVIRYKASDldKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN 983
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
132-478 |
2.18e-59 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 203.34 E-value: 2.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAgVPKGVANLVLGpGATVG 211
Cdd:PTZ00381 101 GKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 212 DELaVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLV 291
Cdd:PTZ00381 179 TEL-LKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 292 EDAIHDQFLAELvKRAKRIKLGNGFHAETESGPLISAEHrakVEKYVEIGLEEGAKLETGGKrpedpALQNGFFYEPTIF 371
Cdd:PTZ00381 258 HRSIKDKFIEAL-KEAIKEFFGEDPKKSEDYSRIVNEFH---TKRLAELIKDHGGKVVYGGE-----VDIENKYVAPTII 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 372 SNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND--FHPYFAQAP 449
Cdd:PTZ00381 329 VNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDcvFHLLNPNLP 408
|
330 340
....*....|....*....|....*....
gi 1803004483 450 WGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:PTZ00381 409 FGGVGNSGMGAYHGKYGFDTFSHPKPVLN 437
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
6-422 |
7.08e-59 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 202.37 E-value: 7.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKeqIRSIINPFNQEEIATVSEGGREDAIKAIAAARRAfdKGEWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:PLN02315 24 YVGGEWRANGP--LVSSVNPANNQPIAEVVEASLEDYEEGLRACEEA--AKIWMQVPAPKRGEIVRQIGDALRAKLDYLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISSPIPDSESKIIREPIGVCGQITPWNYPLLQASWKIAPAL 165
Cdd:PLN02315 100 RLVSLEMGKILAEGIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMEVWNPLGIVGVITAFNFPCAVLGWNACIAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 166 AAGNTIVMKPSEITPLTTIKVFKL----MEEAGVPKGVANLVLGpGATVGDELAVNKDVDLISFTGGIETGKKIMRAASG 241
Cdd:PLN02315 180 VCGNCVVWKGAPTTPLITIAMTKLvaevLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 242 NVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETE 321
Cdd:PLN02315 259 RFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 322 SGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEdpalQNGFFYEPTIFSnCNSDMRIVQEEVFGPVLTVETFSSEEEV 401
Cdd:PLN02315 339 LGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIE----SEGNFVQPTIVE-ISPDADVVKEELFGPVLYVMKFKTLEEA 413
|
410 420
....*....|....*....|.
gi 1803004483 402 IELANDTIYGLAGAVWSKDIE 422
Cdd:PLN02315 414 IEINNSVPQGLSSSIFTRNPE 434
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
134-471 |
1.52e-58 |
|
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: 199.37 E-value: 1.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 134 SKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPlTTIKVFKLMEEAGVPKGVANLVLGPGATVGDE 213
Cdd:cd07135 102 PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTP-HTAALLAELVPKYLDPDAFQVVQGGVPETTAL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 214 LavNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVED 293
Cdd:cd07135 181 L--EQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 294 AIHDQFLAELVKRAKRIkLGNGFHAETESGPLISAEHRAKVEKYVEiglEEGAKLETGGKRPEDPAlqngfFYEPTIFSN 373
Cdd:cd07135 259 SVYDEFVEELKKVLDEF-YPGGANASPDYTRIVNPRHFNRLKSLLD---TTKGKVVIGGEMDEATR-----FIPPTIVSD 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 374 CNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND--FHPYFAQAPWG 451
Cdd:cd07135 330 VSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDtlIHVGVDNAPFG 409
|
330 340
....*....|....*....|
gi 1803004483 452 GYKQSGFGRELGKIGLEEYT 471
Cdd:cd07135 410 GVGDSGYGAYHGKYGFDTFT 429
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-459 |
2.55e-57 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 197.67 E-value: 2.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEQIRSIINPF-----------NQEEIATVSEGGREDAIKaiaaarrafdkgeWSSLSGLERGKIVLKIA 74
Cdd:PLN00412 19 YADGEWRTSSSGKSVAITNPStrktqykvqacTQEEVNKAMESAKAAQKA-------------WAKTPLWKRAELLHKAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 75 ELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYA--GL-ADKDGGEIISSPIPDSE-------SKIirePIGVC 144
Cdd:PLN00412 86 AILKEHKAPIAECLVKEIAKPAKDAVTEVVRSGDLISYTAeeGVrILGEGKFLVSDSFPGNErnkycltSKI---PLGVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 145 GQITPWNYPLLQASWKIAPALAAGNTIVMKP---SEITPLTTIKVFKLmeeAGVPKGVANLVLGPGATVGDELAVNKDVD 221
Cdd:PLN00412 163 LAIPPFNYPVNLAVSKIAPALIAGNAVVLKPptqGAVAALHMVHCFHL---AGFPKGLISCVTGKGSEIGDFLTMHPGVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 222 LISFTGGiETGKKIMRAASgnVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLA 301
Cdd:PLN00412 240 CISFTGG-DTGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 302 ELVKRAKRIKLGNGfHAETESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRpedpalqNGFFYEPTIFSNCNSDMRIV 381
Cdd:PLN00412 317 KVNAKVAKLTVGPP-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR-------EGNLIWPLLLDNVRPDMRIA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 382 QEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDfhpyfAQA------PWGGYKQ 455
Cdd:PLN00412 389 WEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINS-----APArgpdhfPFQGLKD 463
|
....
gi 1803004483 456 SGFG 459
Cdd:PLN00412 464 SGIG 467
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
13-439 |
1.50e-56 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 203.17 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 13 SAEKEQIRSIINPFNQEEI-ATVSEGGREDAIKAIAAARRAFDkgEWSSLSGLERGKIVLKIAELIRRDLEELAELESLD 91
Cdd:PRK11905 562 GDVDGGTRPVLNPADHDDVvGTVTEASAEDVERALAAAQAAFP--EWSATPAAERAAILERAADLMEAHMPELFALAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 92 TGKTLeeskadMDDIANV-----F-QYYAGladkdggEIISSPIPDSeskiiREPIGVCGQITPWNYPLLQASWKIAPAL 165
Cdd:PRK11905 640 AGKTL------ANAIAEVreavdFlRYYAA-------QARRLLNGPG-----HKPLGPVVCISPWNFPLAIFTGQIAAAL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 166 AAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRA----ASG 241
Cdd:PRK11905 702 VAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTlakrSGP 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 242 NVKKIAlELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETE 321
Cdd:PRK11905 782 PVPLIA-ETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTD 860
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 322 SGPLISAEHRAKVEKYVEIGLEEGAKLEtggKRPEDPALQNGFFYEPTIFSncNSDMRIVQEEVFGPVLTVETFSSEE-- 399
Cdd:PRK11905 861 VGPVIDAEAQANIEAHIEAMRAAGRLVH---QLPLPAETEKGTFVAPTLIE--IDSISDLEREVFGPVLHVVRFKADEld 935
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1803004483 400 EVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN 439
Cdd:PRK11905 936 RVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN 975
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
7-439 |
2.45e-54 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 196.70 E-value: 2.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 7 IDGEWISAEKeqiRSIINPFNQEEIA-TVSEGGREDAIKAIAAARRAFDKgeWSSLSGLERGKIVLKIAELIRRDLEELA 85
Cdd:COG4230 562 IAGEAASGEA---RPVRNPADHSDVVgTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELM 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 86 ELESLDTGKTLEeskadmDDIANV-----F-QYYAGLADKDGGEiisspipdsesKIIREPIGVCGQITPWNYPLL---- 155
Cdd:COG4230 637 ALLVREAGKTLP------DAIAEVreavdFcRYYAAQARRLFAA-----------PTVLRGRGVFVCISPWNFPLAiftg 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 156 QaswkIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKI 235
Cdd:COG4230 700 Q----VAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLI 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 236 MRA----ASGNVKKIAlELGGKNPNIVfkD--ADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLaELVKRA-K 308
Cdd:COG4230 776 NRTlaarDGPIVPLIA-ETGGQNAMIV--DssALPEQVVDDVLASAFDSAGQRCSALRVLCVQEDIADRVL-EMLKGAmA 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 309 RIKLGNGFHAETESGPLISAEHRAKVEKYVEigleegaKLETGGKR----PEDPALQNGFFYEPTIFSnCNSdMRIVQEE 384
Cdd:COG4230 852 ELRVGDPADLSTDVGPVIDAEARANLEAHIE-------RMRAEGRLvhqlPLPEECANGTFVAPTLIE-IDS-ISDLERE 922
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1803004483 385 VFGPVLTVETFSSEE--EVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN 439
Cdd:COG4230 923 VFGPVLHVVRYKADEldKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
3-463 |
8.36e-54 |
|
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: 188.58 E-value: 8.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 3 QTLFIDGEWISAEKEqIRSIINPFNQEEI-ATVSEGGREDAIKAIAAARRAFdkGEWSSLSGLERGKIVLKIAELIRRDL 81
Cdd:TIGR01238 37 QAAPIIGHSYKADGE-AQPVTNPADRRDIvGQVFHANLAHVQAAIDSAQQAF--PTWNATPAKERAAKLDRLADLLELHM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 82 EELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGEIISspipdseskiirEPIGVCGQITPWNYPLLQASWKI 161
Cdd:TIGR01238 114 PELMALCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSV------------ESRGVFVCISPWNFPLAIFTGQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 162 APALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMRAASG 241
Cdd:TIGR01238 182 SAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 242 N----VKKIAlELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFH 317
Cdd:TIGR01238 262 RedapVPLIA-ETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 318 AETESGPLISAEHRAKVEKYVEiGLEEGAKLETGGKRPEDPALQNGFFYEPTIFSncNSDMRIVQEEVFGPVLTVETFSS 397
Cdd:TIGR01238 341 LTTDVGPVIDAEAKQNLLAHIE-HMSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKA 417
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 398 EE--EVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND--FHPYFAQAPWGGYKQSGFGRELG 463
Cdd:TIGR01238 418 REldQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRnqVGAVVGVQPFGGQGLSGTGPKAG 487
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
5-457 |
3.74e-52 |
|
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: 184.33 E-value: 3.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 5 LFIDGEWIsaEKEQIRSIINPFN-QEEIATVSEGGREDAIKAIAAARRAfdKGEWSSLSGLERGKIVLKIAELI----RR 79
Cdd:cd07123 35 LVIGGKEV--RTGNTGKQVMPHDhAHVLATYHYADAALVEKAIEAALEA--RKEWARMPFEDRAAIFLKAADLLsgkyRY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 80 DLEELaelesldT----GKTLEEskADMDDIA--------NVfqYYAglADKDGGEIISSPiPDSESKIIREPI-GVCGQ 146
Cdd:cd07123 111 ELNAA-------TmlgqGKNVWQ--AEIDAACelidflrfNV--KYA--EELYAQQPLSSP-AGVWNRLEYRPLeGFVYA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 147 ITPWNYPLLQASWKIAPALAaGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDelAVNKDVDL--IS 224
Cdd:cd07123 177 VSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGD--TVLASPHLagLH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 225 FTGGIETGKKIMRAASGNVK------KIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAIHDQ 298
Cdd:cd07123 254 FTGSTPTFKSLWKQIGENLDryrtypRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 299 FLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEE-GAKLETGGKrPEDpalQNGFFYEPTIFSNCNSD 377
Cdd:cd07123 334 VKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGK-CDD---SVGYFVEPTVIETTDPK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 378 MRIVQEEVFGPVLTVETFSSE--EEVIELANDT-IYGLAGAVWSKDIEKCERVAARLRM--GTVWINDfHPYFA---QAP 449
Cdd:cd07123 410 HKLMTEEIFGPVLTVYVYPDSdfEETLELVDTTsPYALTGAIFAQDRKAIREATDALRNaaGNFYIND-KPTGAvvgQQP 488
|
....*...
gi 1803004483 450 WGGYKQSG 457
Cdd:cd07123 489 FGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
136-486 |
5.95e-46 |
|
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: 165.86 E-value: 5.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 136 IIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTikvfKLMEEAgVPKGVAN----LVLGpGATVG 211
Cdd:cd07132 96 IYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATA----KLLAEL-IPKYLDKecypVVLG-GVEET 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 212 DELAVNKdVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLV 291
Cdd:cd07132 170 TELLKQR-FDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAPDYVLC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 292 EDAIHDQFLAELVKRAKRIkLGNGFHAETESGPLISAEHRAKVEKyveigLEEGAKLETGGKrpEDPALQngfFYEPTIF 371
Cdd:cd07132 249 TPEVQEKFVEALKKTLKEF-YGEDPKESPDYGRIINDRHFQRLKK-----LLSGGKVAIGGQ--TDEKER---YIAPTVL 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 372 SNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIND--FHPYFAQAP 449
Cdd:cd07132 318 TDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDtiMHYTLDSLP 397
|
330 340 350
....*....|....*....|....*....|....*...
gi 1803004483 450 WGGYKQSGFGRELGKIGLEEYTEVKHV-YRNTKPAAVN 486
Cdd:cd07132 398 FGGVGNSGMGAYHGKYSFDTFSHKRSClVKSLNMEKLN 435
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
58-439 |
2.81e-43 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 164.38 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 58 WSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGgeiisspipDSESKIi 137
Cdd:PRK11809 698 WFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDDF---------DNDTHR- 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 138 rePIG--VCgqITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGDELA 215
Cdd:PRK11809 768 --PLGpvVC--ISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALV 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 216 VNKDVDLISFTGGIETGKKIMRAASGNV----KKIAL--ELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRL 289
Cdd:PRK11809 844 ADARVRGVMFTGSTEVARLLQRNLAGRLdpqgRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVL 923
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 290 LVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIGLEEGAKLeTGGKRPEDPALQNGFFYEPT 369
Cdd:PRK11809 924 CLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGRPV-FQAARENSEDWQSGTFVPPT 1002
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1803004483 370 IFSNCNSDMriVQEEVFGPVLTVETFSSEE--EVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWIN 439
Cdd:PRK11809 1003 LIELDSFDE--LKREVFGPVLHVVRYNRNQldELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYVN 1072
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
132-476 |
4.28e-41 |
|
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: 152.57 E-value: 4.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVAnlVLGPGATVG 211
Cdd:cd07137 93 AKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIK--VIEGGVPET 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 212 DELAVNKdVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVF-FHAGQVCSAGSRLL 290
Cdd:cd07137 171 TALLEQK-WDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 291 VEdaihDQFLAELVKRAKRIKLgnGFHAET--ESGPL---ISAEHRAKVEKYVEiGLEEGAKLETGGKRPEDpalqnGFF 365
Cdd:cd07137 250 VE----ESFAPTLIDALKNTLE--KFFGENpkESKDLsriVNSHHFQRLSRLLD-DPSVADKIVHGGERDEK-----NLY 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 366 YEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYF 445
Cdd:cd07137 318 IEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQY 397
|
330 340 350
....*....|....*....|....*....|...
gi 1803004483 446 A--QAPWGGYKQSGFGRELGKIGLEEYTEVKHV 476
Cdd:cd07137 398 AidTLPFGGVGESGFGAYHGKFSFDAFSHKKAV 430
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
132-478 |
2.21e-32 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 129.08 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVAnlVLGPGATVG 211
Cdd:PLN02203 100 ATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDSKAVK--VIEGGPAVG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 212 DELAVNKdVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIV---FKDADLEVAVDQALNAVFFH-AGQVCSAGS 287
Cdd:PLN02203 178 EQLLQHK-WDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVAVNRIVGGKWGScAGQACIAID 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 288 RLLVEDAIHdQFLAELVKraKRIKlgnGFHAETESGP-----LISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDpalqn 362
Cdd:PLN02203 257 YVLVEERFA-PILIELLK--STIK---KFFGENPRESksmarILNKKHFQRLSNLLKDPRVAASIVHGGSIDEKK----- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 363 gFFYEPTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFH 442
Cdd:PLN02203 326 -LFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTFNDAI 404
|
330 340 350
....*....|....*....|....*....|....*...
gi 1803004483 443 PYFA--QAPWGGYKQSGFGRELGKIGLEEYTEVKHVYR 478
Cdd:PLN02203 405 IQYAcdSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLR 442
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
132-479 |
1.57e-31 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 126.70 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLvlgPGATVG 211
Cdd:PLN02174 104 ASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVV---EGAVTE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 212 DELAVNKDVDLISFTGGIETGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVF-FHAGQVCSAGSRLL 290
Cdd:PLN02174 181 TTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDYIL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 291 VEDAIHDQFLAELVKRAKRIKLGNGFHAETESgPLISAEHRAKVEKYVEiGLEEGAKLETGGKRPEDpalqnGFFYEPTI 370
Cdd:PLN02174 261 TTKEYAPKVIDAMKKELETFYGKNPMESKDMS-RIVNSTHFDRLSKLLD-EKEVSDKIVYGGEKDRE-----NLKIAPTI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 371 FSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVWINDFHPYFA--QA 448
Cdd:PLN02174 334 LLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLAlhTL 413
|
330 340 350
....*....|....*....|....*....|..
gi 1803004483 449 PWGGYKQSGFGRELGKIGLEEYTEVKHV-YRN 479
Cdd:PLN02174 414 PFGGVGESGMGAYHGKFSFDAFSHKKAVlYRS 445
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
54-463 |
5.16e-31 |
|
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: 124.66 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 54 DKGEWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTlEESKADMDDIANVFQYYAGLADKDG--GEIISSPIPD 131
Cdd:cd07084 11 STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKG-WMFAENICGDQVQLRARAFVIYSYRipHEPGNHLGQG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 132 SESKIIRE--PIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAG-VPKGVANLVLGPGA 208
Cdd:cd07084 90 LKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGDGK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 209 TvGDELAVNKDVDLISFTGGIETGKKImrAASGNVKKIALELGGKNPNIVFKDADLEVAV-DQALNAVFFHAGQVCSAGS 287
Cdd:cd07084 170 T-MQALLLHPNPKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQAVDYVaWQCVQDMTACSGQKCTAQS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 288 RLLV-EDAIHDQFLAELVKRAKRIKLGNgfhaeTESGPLISAEHRAKVEkyvEIGLEEGAKLETGGKrpEDPALQNGFFY 366
Cdd:cd07084 247 MLFVpENWSKTPLVEKLKALLARRKLED-----LLLGPVQTFTTLAMIA---HMENLLGSVLLFSGK--ELKNHSIPSIY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 367 ----EPTIFSNCNSDMR---IVQEEVFGPVLTVETFSSEEE--VIELANDTIYGLAGAVWSKDIEKCERVAARLRM---- 433
Cdd:cd07084 317 gacvASALFVPIDEILKtyeLVTEEIFGPFAIVVEYKKDQLalVLELLERMHGSLTAAIYSNDPIFLQELIGNLWVagrt 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 1803004483 434 -------GTVWINDFHpyfaqapWGGYKQSGFGRELG 463
Cdd:cd07084 397 yailrgrTGVAPNQNH-------GGGPAADPRGAGIG 426
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
6-428 |
8.82e-30 |
|
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: 121.99 E-value: 8.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 6 FIDGEWISAEKEqIRSIINPFNQEEIATVSEGGREdaikAIAAARRAFDKG--EWSSLSGLERGKIVLKIAELI--RRDL 81
Cdd:cd07128 4 YVAGQWHAGTGD-GRTLHDAVTGEVVARVSSEGLD----FAAAVAYAREKGgpALRALTFHERAAMLKALAKYLmeRKED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 82 EELAELeslDTGKTLEESKADMDDIANVFQYYAGLADK---DGGEII-SSPIPDS-ESKIIREPI-----GVCGQITPWN 151
Cdd:cd07128 79 LYALSA---ATGATRRDSWIDIDGGIGTLFAYASLGRRelpNAHFLVeGDVEPLSkDGTFVGQHIltprrGVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 152 YPllqaSW----KIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGV-PKGVANLVLGPgatVGDELAVNKDVDLISFT 226
Cdd:cd07128 156 FP----VWgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLlPEGALQLICGS---VGDLLDHLGEQDVVAFT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 227 GGIETGKKImRAASGNVKK---IALELGGKNPNIVFKDA-------DL---EVAVDQALNAvffhaGQVCSAGSRLLVED 293
Cdd:cd07128 229 GSAATAAKL-RAHPNIVARsirFNAEADSLNAAILGPDAtpgtpefDLfvkEVAREMTVKA-----GQKCTAIRRAFVPE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 294 AIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEIgLEEGAKLETGGKRPEDPALQN---GFFYEPTI 370
Cdd:cd07128 303 ARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFEVVGADaekGAFFPPTL 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 371 FSnCNSDM--RIVQE-EVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVA 428
Cdd:cd07128 382 LL-CDDPDaaTAVHDvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
61-463 |
6.26e-25 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 107.87 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 61 LSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKADMDDIANVFQYYAGLADKDGGeiiSSPIPDSES-KIIRE 139
Cdd:PRK11903 60 LTYAQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDSAVDIDGGIFTLGYYAKLGAALGD---ARLLRDGEAvQLGKD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 140 PI-----------GVCGQITPWNYPllqaSW----KIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGV-PKGVANLV 203
Cdd:PRK11903 137 PAfqgqhvlvptrGVALFINAFNFP----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 204 LGPGATVGDELavnKDVDLISFTGGIETGKkIMRAASGNVK---KIALELGGKNPNIVFKDAD-----LEVAVDQALNAV 275
Cdd:PRK11903 213 CGSSAGLLDHL---QPFDVVSFTGSAETAA-VLRSHPAVVQrsvRVNVEADSLNSALLGPDAApgseaFDLFVKEVVREM 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 276 FFHAGQVCSAGSRLLVEDAIHDQFLAELVKRAKRIKLGNGFHAETESGPLISAEHRAKVEKYVEiGLEEGAKLETGGKRP 355
Cdd:PRK11903 289 TVKSGQKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLA-ALRAQAEVLFDGGGF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 356 E----DPALqnGFFYEPTIFSNCNSD-MRIVQE-EVFGPVLTVETFSSEEEVIELANDTIYGLAGAVWSKDIEKCERVA- 428
Cdd:PRK11903 368 AlvdaDPAV--AACVGPTLLGASDPDaATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAAl 445
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1803004483 429 ------ARLRMGTVWINDFHP----YFAQAPWGGYKQSGFGRELG 463
Cdd:PRK11903 446 eladshGRVHVISPDVAALHTghgnVMPQSLHGGPGRAGGGEELG 490
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
162-432 |
1.80e-15 |
|
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: 78.35 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 162 APALAAGNTIVMKPSEITPLTTIKVFKLMEEA----GVPKGVANLVLGPGATVGDELAVNKDVDLISFTGGIETGKKIMR 237
Cdd:cd07129 129 ASALAAGCPVVVKAHPAHPGTSELVARAIRAAlratGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 238 AASGNVKKIA--LELGGKNPNIVFKDA---DLEVAVDQALNAVFFHAGQVC-SAGSRLLVEDAIHDQFLAELVKRAkrik 311
Cdd:cd07129 209 AAAARPEPIPfyAELGSVNPVFILPGAlaeRGEAIAQGFVGSLTLGAGQFCtNPGLVLVPAGPAGDAFIAALAEAL---- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 312 lgngfhAETESGPLISAEHRAKVEKYVEiGLEE--GAKLETGGKRPEDPALqngffYEPTIFSNCNSDMR---IVQEEVF 386
Cdd:cd07129 285 ------AAAPAQTMLTPGIAEAYRQGVE-ALAAapGVRVLAGGAAAEGGNQ-----AAPTLFKVDAAAFLadpALQEEVF 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1803004483 387 GPVLTVETFSSEEEVIELAND-------TIYGLAGavwskDIEKCERVAARLR 432
Cdd:cd07129 353 GPASLVVRYDDAAELLAVAEAlegqltaTIHGEED-----DLALARELLPVLE 400
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
68-439 |
4.16e-14 |
|
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: 74.06 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 68 KIVLKIAELIRRDLEELAELESLDTGKTLEESKAdmddIANVF---QYYAGLADKDGGEIISSpipDSESKI--IREPIG 142
Cdd:cd07122 25 KIVEAVAWAAADAAEELAKMAVEETGMGVVEDKV----IKNHFaseYVYNDIKDMKTVGVIEE---DEEKGIveIAEPVG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 143 VCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLM----EEAGVPKGVANLVLGPGATVGDELAVNK 218
Cdd:cd07122 98 VIAALIPSTNPTSTAIFKALIALKTRNAIIFSPHPRAKKCSIEAAKIMreaaVAAGAPEGLIQWIEEPSIELTQELMKHP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 219 DVDLISFTGgietGKKIMRAA--SGnvkKIALELG-GKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRLLVEDAI 295
Cdd:cd07122 178 DVDLILATG----GPGMVKAAysSG---KPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVDDEI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 296 HDQFLAELVKRakriklgnGFHaetesgpLISAEHRAKVEKYVeigLEEGAKLETG--GKRPEDPALQNGFfyepTIFSN 373
Cdd:cd07122 251 YDEVRAELKRR--------GAY-------FLNEEEKEKLEKAL---FDDGGTLNPDivGKSAQKIAELAGI----EVPED 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 374 CNsdMRIVQEEVFG-----------PVLTVETFSSEEEVIELANDTI-YGLAG---AVWSKDIEKCERVAARLRMGTVWI 438
Cdd:cd07122 309 TK--VLVAEETGVGpeeplsreklsPVLAFYRAEDFEEALEKARELLeYGGAGhtaVIHSNDEEVIEEFALRMPVSRILV 386
|
.
gi 1803004483 439 N 439
Cdd:cd07122 387 N 387
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
144-442 |
1.05e-13 |
|
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: 73.28 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 144 CGQITPWN-YPLLQASwkiapaLAAGNTIVMKP--SEITPLT-TIKVFK-LMEEAGV-PKGVANLVLGPGATVGDELAVN 217
Cdd:cd07127 202 CSTFPTWNgYPGLFAS------LATGNPVIVKPhpAAILPLAiTVQVAReVLAEAGFdPNLVTLAADTPEEPIAQTLATR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 218 KDVDLISFTGGIETGKKIMRAASGnvKKIALELGGKNPNIVFKDADLeVAVDQALN-AVFFHAGQVCSAGSRLLV-EDAI 295
Cdd:cd07127 276 PEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVDSTDDL-KAMLRNLAfSLSLYSGQMCTTPQNIYVpRDGI 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 296 --------HDQFLAELVKRAKRIkLGNGFHAETESGPLISAEHRAKVEKYVEIGLeegakLETGGKRPEDPALQNGFFYE 367
Cdd:cd07127 353 qtddgrksFDEVAADLAAAIDGL-LADPARAAALLGAIQSPDTLARIAEARQLGE-----VLLASEAVAHPEFPDARVRT 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 368 PTIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELANDTI----------YGLAGAVWSKDIEKCERVAARLRM---G 434
Cdd:cd07127 427 PLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVrehgamtvgvYSTDPEVVERVQEAALDAGVALSInltG 506
|
330
....*....|....
gi 1803004483 435 TVWIN------DFH 442
Cdd:cd07127 507 GVFVNqsaafsDFH 520
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
138-437 |
4.55e-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: 70.99 E-value: 4.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 138 REPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVLGPGATVGdELAVN 217
Cdd:cd07126 140 RWPYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMN-KILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 218 KDVDLISFTGGIETGKKIMRAASGNVKkiaLELGGKNPNIVFKD-ADLEVAVDQALNAVFFHAGQVCSAGSRLLV-EDAI 295
Cdd:cd07126 219 ANPRMTLFTGSSKVAERLALELHGKVK---LEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAhENWV 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 296 HDQFLAELVKRAKRIKLGNgfhaeTESGPLISAEHRAKVEKYVEIGLEEGAKLETGGKRPEDPALQNGF-FYEPT-IF-- 371
Cdd:cd07126 296 QAGILDKLKALAEQRKLED-----LTIGPVLTWTTERILDHVDKLLAIPGAKVLFGGKPLTNHSIPSIYgAYEPTaVFvp 370
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 372 ---SNCNSDMRIVQEEVFGPVLTVETFSSEEE--VIELANDTIYGLAGAVWSKDIEKCERVAARLRMGTVW 437
Cdd:cd07126 371 leeIAIEENFELVTTEVFGPFQVVTEYKDEQLplVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
57-306 |
1.06e-09 |
|
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: 60.36 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 57 EWSSLSGLERGKIVLKIAELIRRDLEELAELESLDTGKTLEESKAdmddIANVFQ---YYAGLADKDGGEIISSPIPDSe 133
Cdd:cd07081 14 GLSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGMGRVEDKV----IKNHFAaeyIYNVYKDEKTCGVLTGDENGG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 134 SKIIREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEA----GVPKGVANLVLGPGAT 209
Cdd:cd07081 89 TLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLIGWIDNPSIE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 210 VGDELAVNKDVDLISFTGgietGKKIMRAASGNVKKIALELGGKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRL 289
Cdd:cd07081 169 LAQRLMKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSV 244
|
250
....*....|....*..
gi 1803004483 290 LVEDAIHDQFLAELVKR 306
Cdd:cd07081 245 IVVDSVYDEVMRLFEGQ 261
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
133-320 |
1.78e-08 |
|
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: 56.46 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 133 ESKIIREPIGVCGQITPWNYPLLqASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPKGVANLVL---GPGAT 209
Cdd:cd07077 93 ETYVRAFPIGVTMHILPSTNPLS-GITSALRGIATRNQCIFRPHPSAPFTNRALALLFQAADAAHGPKILVLyvpHPSDE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 210 VGDELAVNKDVDLISFTGGIETGKKIMRAASGnvkKIALELGGKNPNIVF-KDADLEVAVDQALNAVFFHaGQVCSAGSR 288
Cdd:cd07077 172 LAEELLSHPKIDLIVATGGRDAVDAAVKHSPH---IPVIGFGAGNSPVVVdETADEERASGSVHDSKFFD-QNACASEQN 247
|
170 180 190
....*....|....*....|....*....|..
gi 1803004483 289 LLVEDAIHDQFLAELVKRAKRIKLgnGFHAET 320
Cdd:cd07077 248 LYVVDDVLDPLYEEFKLKLVVEGL--KVPQET 277
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
137-439 |
1.72e-07 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 54.04 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 137 IREPIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLM----EEAGVPKGVANLVLGPGATVGD 212
Cdd:PRK13805 105 IAEPVGVIAGITPTTNPTSTAIFKALIALKTRNPIIFSFHPRAQKSSIAAAKIVldaaVAAGAPKDIIQWIEEPSVELTN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 213 ELAVNKDVDLISFTGgietGKKIMRAA--SGnvkKIALELG-GKNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSRL 289
Cdd:PRK13805 185 ALMNHPGIALILATG----GPGMVKAAysSG---KPALGVGaGNVPAYIDKTADIKRAVNDILLSKTFDNGMICASEQAV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 290 LVEDAIHDQFLAELVKRakriklgnGFHaetesgpLISAEHRAKVEKYVeIGLEEGA-KLETGGKRPEDPALQNGFFYEP 368
Cdd:PRK13805 258 IVDDEIYDEVKEEFASH--------GAY-------FLNKKELKKLEKFI-FGKENGAlNADIVGQSAYKIAEMAGFKVPE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 369 tifsncnsDMRIVQEEVFG-------------PVLTVETFSSEEEVIELANDTI-YGLAG---AVWSKDIEKCERVAARL 431
Cdd:PRK13805 322 --------DTKILIAEVKGvgeseplsheklsPVLAMYKAKDFEDAVEKAEKLVeFGGLGhtaVIYTNDDELIKEFGLRM 393
|
....*...
gi 1803004483 432 RMGTVWIN 439
Cdd:PRK13805 394 KACRILVN 401
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
138-305 |
2.69e-05 |
|
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: 46.46 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 138 REPIGVCGQITPWNYPLlqaSWKIAPA---LAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPK-GVANLVL---GPGATV 210
Cdd:cd07121 95 YAPFGVIGAITPSTNPT---ETIINNSismLAAGNAVVFNPHPGAKKVSAYAVELINKAIAEAgGPDNLVVtveEPTIET 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 211 GDELAVNKDVDLISFTGG-------IETGKKIMRAASGNvkkialelggkNPNIVFKDADLEVAVDQALNAVFFHAGQVC 283
Cdd:cd07121 172 TNELMAHPDINLLVVTGGpavvkaaLSSGKKAIGAGAGN-----------PPVVVDETADIEKAARDIVQGASFDNNLPC 240
|
170 180
....*....|....*....|..
gi 1803004483 284 SAGSRLLVEDAIHDQFLAELVK 305
Cdd:cd07121 241 IAEKEVIAVDSVADYLIAAMQR 262
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
140-405 |
1.66e-04 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 44.12 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 140 PIGVCGQITPWNYPLLQASWKIAPALAAGNTIVMKPSEITPLTTIKVFKLMEEAGVPK-GVANLVL---GPGATVGDELA 215
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNEAIVAAgGPENLVVtvaEPTIETAQRLM 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 216 VNKDVDLISFTGG-------IETGKKIMRAASGNvkkialelggkNPNIVFKDADLEVAVDQALNAVFFHAGQVCSAGSR 288
Cdd:PRK15398 209 KHPGIALLVVTGGpavvkaaMKSGKKAIGAGAGN-----------PPVVVDETADIEKAARDIVKGASFDNNLPCIAEKE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 289 LLVEDAIHDQFLAELVKrakriklgngfhaetESGPLISAEHRAKVEKYVeigLEEGAKLET--------------GGKR 354
Cdd:PRK15398 278 VIVVDSVADELMRLMEK---------------NGAVLLTAEQAEKLQKVV---LKNGGTVNKkwvgkdaakileaaGINV 339
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1803004483 355 PEDPALqngffyeptIFSNCNSDMRIVQEEVFGPVLTVETFSSEEEVIELA 405
Cdd:PRK15398 340 PKDTRL---------LIVETDANHPFVVTELMMPVLPVVRVKDVDEAIALA 381
|
|
| LuxC |
pfam05893 |
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) ... |
124-310 |
6.95e-04 |
|
Acyl-CoA reductase (LuxC); This family consists of several bacterial Acyl-CoA reductase (LuxC) proteins. The channelling of fatty acids into the fatty aldehyde substrate for the bacterial bioluminescence reaction is catalyzed by a fatty acid reductase multienzyme complex, which channels fatty acids through the thioesterase (LuxD), synthetase (LuxE) and reductase (LuxC) components.
Pssm-ID: 399113 Cd Length: 401 Bit Score: 42.04 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 124 IISSPIPDSESKIIREPIGVCGQITPWNYPLLqASWKIAPALAAGNTIVMKPSEITPLTTIKVFK--LMEEAGVPKGVAN 201
Cdd:pfam05893 72 ILDEWLPTKPSYEKAFPPGLVFHVLSGNVPLL-PVMSILMGLLVKNVNLLKVSSSDPFTAAALLAsfADLDPTHPLADSL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1803004483 202 LVL---GPGATVGDELAVNKDVdlISFTGGIETGKKIMRAASGNVK------KIALElggknpnIVFKDADLEVAVDQAL 272
Cdd:pfam05893 151 SVVywdGGSTQLEDLIVANADV--VIAWGGEDAINAIRECLKPGKQwidfgaKISFA-------VVDREAALDKAAERAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1803004483 273 NAVFFHAGQVCSAGSRLLVE--DAIH-DQF----LAELVKRAKRI 310
Cdd:pfam05893 222 DDICVFDQQACLSPQTVFVEsdDKITpDEFaerlAAALAKRARIL 266
|
|
| |
