|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
1-534 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 1133.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 1 MAAHRFSSLLSRSV-----PLLSRGGKQSYLGRGVYRYGTAAAAaLEEPIKPPVSVQYDKLLINGQFVDAASGKTFPTLD 75
Cdd:PLN02466 1 MAARRISSLLSRSLsasssALLRSRGRNGGRGRGIRRFSTAAAA-VEEPITPPVQVSYTQLLINGQFVDAASGKTFPTLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 76 PRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEI 155
Cdd:PLN02466 80 PRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEKHNDELAALETWDNGKPYEQSAKAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 156 PMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSAL 235
Cdd:PLN02466 160 PMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSAL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 236 LVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSNLKPVTLELGGKSPFIVCEDAD 315
Cdd:PLN02466 240 YAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELAAKSNLKPVTLELGGKSPFIVCEDAD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 316 VDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAE 395
Cdd:PLN02466 320 VDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 396 SGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTM 475
Cdd:PLN02466 400 SGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTL 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939884057 476 MRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVTALKNPAWL 534
Cdd:PLN02466 480 SRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPLKNPAWL 538
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
51-526 |
0e+00 |
|
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: 973.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 51 VQYDKLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEK 130
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 131 HNDEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGW 210
Cdd:cd07142 81 HADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 211 KVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELS 290
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 291 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKA 370
Cdd:cd07142 241 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 371 GMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
51-525 |
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: 849.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 51 VQYDKLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEK 130
Cdd:cd07091 1 EQPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 131 HNDEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGW 210
Cdd:cd07091 81 DRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLMLAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 211 KVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELS 290
Cdd:cd07091 161 KLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIMEAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 291 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKA 370
Cdd:cd07091 241 AKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 371 GMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:cd07091 321 DTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07091 401 ERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
51-525 |
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: 798.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 51 VQYDKLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEG-PWPKMPAYERQKIMLRFADLVE 129
Cdd:cd07141 4 IKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 130 KHNDEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFG 209
Cdd:cd07141 84 RDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLMAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 210 WKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLEL 289
Cdd:cd07141 164 WKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 290 SAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFK 369
Cdd:cd07141 244 AGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 370 AGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEV 449
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEV 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 450 IRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07141 404 IERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVT 479
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
42-534 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 718.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 42 EEPIKPPvSVQYDKLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIM 121
Cdd:PLN02766 10 ASGVKVP-EIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFERGRIM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 122 LRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPW 201
Cdd:PLN02766 89 MKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 202 NFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTE 281
Cdd:PLN02766 169 NFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKVSFTGSTE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 282 TGKIVLELSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALK 361
Cdd:PLN02766 249 VGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKD 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 362 RTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTIL 441
Cdd:PLN02766 329 WVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLM 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 442 KFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQV 521
Cdd:PLN02766 409 KFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQV 488
|
490
....*....|...
gi 1939884057 522 KAVVTALKNPAWL 534
Cdd:PLN02766 489 KSVVTPLYNSPWL 501
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
55-528 |
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: 679.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdeGPWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGP-HHVQTLHEPIGVAGQIIPWNFPLVMFGWKVG 213
Cdd:COG1012 85 LAALLTLETGKPLAE-ARGEVDRAADFLRYYAGEARRLYGETIPSDAPgTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 214 PALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKs 293
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAAE- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 294 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGME 373
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 374 QGPQVDADQFEKILKYIRSGAESGATLETGGDRL-GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRR 452
Cdd:COG1012 323 MGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939884057 453 ANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTF-DAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVTAL 528
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIRL 479
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
62-524 |
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: 657.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 62 FVDAASgKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAW 141
Cdd:pfam00171 1 WVDSES-ETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPA--WRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 142 DSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNS 221
Cdd:pfam00171 78 ENGKPLAE-ARGEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 222 VVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLE 301
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAAQ-NLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 302 LGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDAD 381
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 382 QFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLA 461
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939884057 462 AGVFTQNLDTANTMMRALRAGTVWINCFDTFDA-AIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
56-524 |
0e+00 |
|
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: 651.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 56 LLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdEGPWP-KMPAYERQKIMLRFADLVEKHNDE 134
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAF-ETDWGlKVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGP 214
Cdd:cd07143 88 LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 215 ALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSN 294
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQ 374
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 375 GPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRAN 454
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAN 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 455 NSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07143 408 DSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
55-524 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 641.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdEGPWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAF-ESWWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGP 214
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 215 ALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAkSN 294
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-QN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRT-VGDPFKAGME 373
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 374 QGPQVDADQFEKILKYIRSGAESGATLETGGDRLGT---KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGEKAPEglgKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
68-524 |
0e+00 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 624.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 68 GKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPY 147
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 148 EQCAQVEIPMFVRLFRYYAGWADKIHGLTIPAdgPHHVQTL--HEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLK 225
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPT--GPDALALitREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 226 TAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSNLKPVTLELGGK 305
Cdd:cd07112 159 PAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 306 SPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFE 384
Cdd:cd07112 239 SPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 385 KILKYIRSGAESGATLETGGDRL--GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAA 462
Cdd:cd07112 319 KVLGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939884057 463 GVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07112 399 SVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
94-526 |
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: 598.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 94 NRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIH 173
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEE-ALGEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 174 GLTIPADGPHHV-QTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLN 252
Cdd:cd07078 78 GEVIPSPDPGELaIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 253 IVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQG 332
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAAE-NLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 333 QCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRL-GTKG 411
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLeGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 412 YYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDT 491
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....*.
gi 1939884057 492 F-DAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07078 397 GaEPSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
58-529 |
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: 578.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 58 INGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAA 137
Cdd:cd07119 2 IDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 138 LEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALA 217
Cdd:cd07119 82 LETLNTGKTLRE-SEIDIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 218 CGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKSNLKP 297
Cdd:cd07119 161 AGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMR-AAAGNVKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 298 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQ 377
Cdd:cd07119 240 VALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 378 VDADQFEKILKYIRSGAESGATLETGGDRLG----TKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRA 453
Cdd:cd07119 320 VSAEHREKVLSYIQLGKEEGARLVCGGKRPTgdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLA 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 454 NNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVTALK 529
Cdd:cd07119 400 NDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHININLS 475
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
73-525 |
0e+00 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 577.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQC-A 151
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETrA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 152 QVE-IPMFvrlFRYYAGWADKIHGLTIPAD-GPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQ 229
Cdd:cd07114 81 QVRyLAEW---YRYYAGLADKIEGAVIPVDkGDYLNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 230 TPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFI 309
Cdd:cd07114 158 TPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAAE-NLAPVTLELGGKSPNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 310 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEK--AKARALKrtVGDPFKAGMEQGPQVDADQFEKIL 387
Cdd:cd07114 237 VFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERlvARARAIR--VGDPLDPETQMGPLATERQLEKVE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 388 KYIRSGAESGATLETGGDRLGT----KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAG 463
Cdd:cd07114 315 RYVARAREEGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAG 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939884057 464 VFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07114 395 IWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVW 456
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
73-524 |
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: 569.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQ 152
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 153 VEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPL 232
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 233 SALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCE 312
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAAP-NLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 313 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRS 392
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 393 GAESGATLETGGDRLGT----KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQN 468
Cdd:cd07093 318 ARAEGATILTGGGRPELpdleGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 469 LDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNV 453
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
73-528 |
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: 565.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDegPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQ 152
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 153 VEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPL 232
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 233 SALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAkSNLKPVTLELGGKSPFIVCE 312
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 313 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRS 392
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 393 GAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTA 472
Cdd:cd07115 318 GREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 473 NTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVTAL 528
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVNL 453
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
55-524 |
0e+00 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 536.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQKI--WAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGP 214
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 215 ALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTaGAALCRHMDVDKLAFTGSTETGKIVLELSAKSn 294
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQ 374
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 375 GPQVDADQFEKILKYIRSGAESGATLETGGDRLGT----KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
53-522 |
0e+00 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 532.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 53 YDkLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHN 132
Cdd:cd07559 1 YD-NFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 133 DEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKV 212
Cdd:cd07559 78 ELLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 213 GPALACGNSVVLKTAEQTPLSALLVSKLFHEAgLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAK 292
Cdd:cd07559 158 APALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAAE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 293 sNLKPVTLELGGKSPFIVCEDA-----DVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDP 367
Cdd:cd07559 237 -NLIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 368 FKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRL----GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKF 443
Cdd:cd07559 316 LDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITF 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939884057 444 KELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVK 522
Cdd:cd07559 396 KDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTK 474
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
74-524 |
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: 532.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 74 LDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQV 153
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKT--WRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAE-ARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 154 EIPMFVRLFRYYAGWADKIHGLTIPADGPHH-VQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPL 232
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPAPGKrILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 233 SALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAkSNLKPVTLELGGKSPFIVCE 312
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 313 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRS 392
Cdd:cd07103 238 DADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVED 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 393 GAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTA 472
Cdd:cd07103 318 AVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1939884057 473 NTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07103 398 WRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYV 449
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
74-525 |
0e+00 |
|
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: 526.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 74 LDPRSGEVIAHVAEGDAEDINRAVAAARKAFdEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQV 153
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAF-ESGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQ-ARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 154 EIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLS 233
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 234 ALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCED 313
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAAE-NVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 314 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGdPFKAGMEQGPQVDADQFEKILKYIRSG 393
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVG-PGLEDPDLGPLISAKQLDRVEGFVARA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 394 AESGATLETGGDRLGT---KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLD 470
Cdd:cd07109 318 RARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1939884057 471 TANTMMRALRAGTVWINCFdtFDAA---IPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07109 398 RALRVARRLRAGQVFVNNY--GAGGgieLPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
55-524 |
0e+00 |
|
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: 523.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:cd07140 7 QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLMEEHQEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADG--PHHVQTL--HEPIGVAGQIIPWNFPLVMFGW 210
Cdd:cd07140 87 LATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQarPNRNLTLtkREPIGVCGIVIPWNYPLMMLAW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 211 KVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELS 290
Cdd:cd07140 167 KMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKHIMKSC 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 291 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKA 370
Cdd:cd07140 247 AVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 371 GMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFK--ELDE 448
Cdd:cd07140 327 STDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDdgDVDG 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 449 VIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07140 407 VLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTV 482
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
73-524 |
1.11e-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: 515.70 E-value: 1.11e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQ 152
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEE-AR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 153 VEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPL 232
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 233 SALLVSKLFHEAGLPEGVLNIVSGFGPTaGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCE 312
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAAK-GIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 313 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRS 392
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 393 GAESGATLETGGDRLGTK-----GYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQ 467
Cdd:cd07090 316 AKQEGAKVLCGGERVVPEdglenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939884057 468 NLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
56-525 |
2.36e-176 |
|
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: 2.36e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 56 LLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDegPWPKMPAYERQKIMLRFADLVEKHNDEV 135
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 136 AALEAWDSGKPYEQCAQVEIPMFVRLFRYYAG------WADKIHGLTIpadgphhvqtLHEPIGVAGQIIPWNFPLVMFG 209
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV----------VREPIGVCGLITPWNWPLNQIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 210 WKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLEL 289
Cdd:cd07138 149 LKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 290 SAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFK 369
Cdd:cd07138 229 AADT-VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 370 AGMEQGPQVDADQFEKILKYIRSGAESGATLETGG----DRLgTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKE 445
Cdd:cd07138 308 PATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGGpgrpEGL-ERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 446 LDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07138 387 EDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
76-524 |
2.90e-176 |
|
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: 504.56 E-value: 2.90e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 76 PRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQVEI 155
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQ-ARGEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 156 PMFVRLFRYYAGWADKIHGLTIPADGPHHVQ-TLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSA 234
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNLGDDMLGlVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 235 LLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDA 314
Cdd:cd07118 163 LMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAAR-NLKKVSLELGGKNPQIVFADA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 315 DVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGA 394
Cdd:cd07118 242 DLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 395 ESGATLETGGDRLGT-KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTAN 473
Cdd:cd07118 322 AEGATLLLGGERLASaAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTAL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1939884057 474 TMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07118 402 TVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
58-522 |
1.04e-173 |
|
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: 498.57 E-value: 1.04e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 58 INGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAA 137
Cdd:TIGR01804 2 IDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQGE--WAAMSPMERGRILRRAADLIRERNEELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 138 LEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALA 217
Cdd:TIGR01804 80 LETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 218 CGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKSNLKP 297
Cdd:TIGR01804 160 AGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMA-AAAGHLKH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 298 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQ 377
Cdd:TIGR01804 239 VTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGPL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 378 VDADQFEKILKYIRSGAESGATLETGGDRLGT----KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRA 453
Cdd:TIGR01804 319 ISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939884057 454 NNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVK 522
Cdd:TIGR01804 399 NDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
58-525 |
1.19e-173 |
|
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: 498.33 E-value: 1.19e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 58 INGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAA 137
Cdd:cd07088 2 INGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 138 LEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPH-HVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPAL 216
Cdd:cd07088 80 LIVEEQGKTLSL-ARVEVEFTADYIDYMAEWARRIEGEIIPSDRPNeNIFIFKVPIGVVAGILPWNFPFFLIARKLAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 217 ACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLK 296
Cdd:cd07088 159 VTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE-NIT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 297 PVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGP 376
Cdd:cd07088 238 KVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 377 QVDADQFEKILKYIRSGAESGATLETGGDRL-GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANN 455
Cdd:cd07088 318 LVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELAND 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939884057 456 SSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDtFDAAIPF-GGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07088 398 SEYGLTSYIYTENLNTAMRATNELEFGETYINREN-FEAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVVY 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
55-528 |
3.95e-173 |
|
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: 497.36 E-value: 3.95e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGP 214
Cdd:cd07117 80 LAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 215 ALACGNSVVLKTAEQTPLSALLVSKLFHEAgLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsN 294
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAAK-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQ 374
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 375 GPQVDADQFEKILKYIRSGAESGATLETGGDRLGT----KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTEngldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVTAL 528
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNIYIDL 475
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
73-526 |
1.58e-169 |
|
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: 487.24 E-value: 1.58e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQ 152
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDE-AA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 153 VEIPMFVRLFRYYAGWADKIH-----GLTIPADGpHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTA 227
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLDakaerAVPLPSED-FKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 228 EQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKSNLKPVTLELGGKSP 307
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQ-AAAQDIKPVSLELGGKSP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 308 FIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKIL 387
Cdd:cd07110 236 IIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKVL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 388 KYIRSGAESGATLETGGDR--LGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVF 465
Cdd:cd07110 316 SFIARGKEEGARLLCGGRRpaHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVI 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939884057 466 TQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07110 396 SRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQITR 456
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
74-525 |
3.51e-169 |
|
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: 486.37 E-value: 3.51e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 74 LDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWpKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKP--YEQCA 151
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPvmTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 152 QVEIPMFVrlFRYYAGWADKIHG-LTIPADGPHHVQTL----HEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKT 226
Cdd:cd07089 81 QVDGPIGH--LRYFADLADSFPWeFDLPVPALRGGPGRrvvrREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 227 AEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAkSNLKPVTLELGGKS 306
Cdd:cd07089 159 APDTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 307 PFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKI 386
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 387 LKYIRSGAESGATLETGGDRL--GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGV 464
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939884057 465 FTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07089 398 WSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
98-525 |
7.06e-169 |
|
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: 482.11 E-value: 7.06e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 98 AAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEqCAQVEIPMFVRLFRYYAGWADKIHGLTI 177
Cdd:cd06534 1 AAARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPIE-EALGEVARAIDTFRYAAGLADKLGGPEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 178 PADGPHHV-QTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSG 256
Cdd:cd06534 78 PSPDPGGEaYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 257 FGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCC 336
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMK-AAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 337 AGSRTFVHEKVYDEFVEKAKaralkrtvgdpfkagmeqgpqvdadqfekilkyirsgaesgatletggdrlgtkgyyiqp 416
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 417 TVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTF-DAA 495
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGvGPE 336
|
410 420 430
....*....|....*....|....*....|
gi 1939884057 496 IPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTVV 366
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
56-519 |
2.95e-168 |
|
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: 484.98 E-value: 2.95e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 56 LLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEV 135
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 136 AALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADK----IHGltipadgphhvqtlHEPIGVAGQIIPWNFPLVMFGWK 211
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLldteLAG--------------WKPVGVVGQIVPWNFPLLMLAWK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 212 VGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSA 291
Cdd:cd07111 168 ICPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTG-NGSFGSALANHPGVDKVAFTGSTEVGRALRRATA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 292 KSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAG 371
Cdd:cd07111 247 GTG-KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 372 MEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIR 451
Cdd:cd07111 326 IDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVA 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939884057 452 RANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYL 519
Cdd:cd07111 406 LANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
56-525 |
3.82e-166 |
|
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: 479.38 E-value: 3.82e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 56 LLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDEV 135
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 136 AALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKiHGLTIPADGPHHVQTL--HEPIGVAGQIIPWNFPLVMFGWKVG 213
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARD-FPFEERRPGSGGGHVLvrREPVGVVAAIVPWNAPLFLAALKIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 214 PALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAkS 293
Cdd:cd07139 160 PALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG-E 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 294 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGME 373
Cdd:cd07139 238 RLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 374 QGPQVDADQFEKILKYIRSGAESGATLETGGDRLG--TKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIR 451
Cdd:cd07139 318 IGPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939884057 452 RANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFdTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07139 398 IANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIY 470
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
55-533 |
1.02e-163 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 474.22 E-value: 1.02e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDE---GPWPKMPAYERQKIMLRFADLVEKH 131
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 132 NDEVAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHG-----LTIPADgPHHVQTLHEPIGVAGQIIPWNFPLV 206
Cdd:PLN02467 89 KSELAKLETLDCGKPLDE-AAWDMDDVAGCFEYYADLAEALDAkqkapVSLPME-TFKGYVLKEPLGVVGLITPWNYPLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 207 MFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIV 286
Cdd:PLN02467 167 MATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTATGRKI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 287 LeLSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGD 366
Cdd:PLN02467 247 M-TAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISD 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 367 PFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLG--TKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFK 444
Cdd:PLN02467 326 PLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKRPEhlKKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFS 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 445 ELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:PLN02467 406 TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENYLSVKQV 485
|
....*....
gi 1939884057 525 VTALKNPAW 533
Cdd:PLN02467 486 TKYISDEPW 494
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
54-524 |
1.88e-163 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 472.47 E-value: 1.88e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 54 DKLLINGQFVdAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHND 133
Cdd:PRK13473 3 TKLLINGELV-AGEGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 134 EVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGltiPADG---PHHVQTLH-EPIGVAGQIIPWNFPLVMFG 209
Cdd:PRK13473 80 EFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEG---KAAGeylEGHTSMIRrDPVGVVASIAPWNYPLMMAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 210 WKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAgLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLEL 289
Cdd:PRK13473 157 WKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 290 SAKSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFK 369
Cdd:PRK13473 236 AADS-VKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 370 AGMEQGPQVDADQFEKILKYI-RSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDE 448
Cdd:PRK13473 315 EDTELGPLISAAHRDRVAGFVeRAKALGHIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQ 394
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 449 VIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:PRK13473 395 AVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
74-526 |
1.35e-161 |
|
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: 466.80 E-value: 1.35e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 74 LDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWpKMPAyERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQV 153
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRR-TTPA-ERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 154 EIPMFVRLFRYYAGWADKIHGltiPADG---PHHVQTL-HEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQ 229
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEG---PAAGeylPGHTSMIrREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 230 TPLSALLVSKLFHEaGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKSNLKPVTLELGGKSPFI 309
Cdd:cd07092 157 TPLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVAR-AAADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 310 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKY 389
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 390 IrSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNL 469
Cdd:cd07092 315 V-ERAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDV 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939884057 470 DTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07092 394 GRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
73-525 |
6.22e-160 |
|
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: 462.99 E-value: 6.22e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdeGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQ 152
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNALRTQAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 153 VEIPMFVRLFRYYAGWADKIHGLTIPAdGPHHVQ-TLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTP 231
Cdd:cd07108 79 PEAAVLADLFRYFGGLAGELKGETLPF-GPDVLTyTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 232 LSALLVSKLFHEAgLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVC 311
Cdd:cd07108 158 LAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAAD-RLIPVSLELGGKSPMIVF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 312 EDADVDKAVELAHFAL-FFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYI 390
Cdd:cd07108 236 PDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 391 RSG-AESGATLETGG----DRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVF 465
Cdd:cd07108 316 DLGlSTSGATVLRGGplpgEGPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVW 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939884057 466 TQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKG-EYSLKNYLQVKAVV 525
Cdd:cd07108 396 TRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVN 456
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
74-524 |
2.37e-157 |
|
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: 455.83 E-value: 2.37e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 74 LDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQV 153
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAE-AQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 154 EIPMFVRLFRYYAGWADKIHglTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLS 233
Cdd:cd07106 79 EVGGAVAWLRYTASLDLPDE--VIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 234 ALLVSKLFHEAgLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKSNLKPVTLELGGKSPFIVCED 313
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMA-SAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 314 ADVDKAVE-LAHFAlFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRS 392
Cdd:cd07106 234 VDIDAVAPkLFWGA-FINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVED 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 393 GAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTA 472
Cdd:cd07106 313 AKAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1939884057 473 NTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07106 393 EAVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
57-524 |
2.41e-157 |
|
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: 457.10 E-value: 2.41e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 57 LINGQFVDAASGKtfPTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEV 135
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPsDTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 136 AALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPH-HVQTLHEPIGVAGQIIPWNFPLVMFGWKVGP 214
Cdd:cd07097 80 ARLLTREEGKTLPE-ARGEVTRAGQIFRYYAGEALRLSGETLPSTRPGvEVETTREPLGVVGLITPWNFPIAIPAWKIAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 215 ALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKSN 294
Cdd:cd07097 159 ALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAA-AAAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQ 374
Cdd:cd07097 238 GARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 375 GPQVDADQFEKILKYIRSGAESGATLETGGDRL--GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRR 452
Cdd:cd07097 318 GPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939884057 453 ANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDT-FDAAIPFGGYKMSGIG-REKGEYSLKNYLQVKAV 524
Cdd:cd07097 398 ANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
55-529 |
8.75e-152 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 443.57 E-value: 8.75e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGP 214
Cdd:PRK09847 101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 215 ALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSN 294
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 LKPVTLELGGKSPFIVCEDA-DVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGME 373
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 374 QGPQVDADQFEKILKYIRSGAESGATLETGgdRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRA 453
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREGESKGQLLLDG--RNAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 454 NNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVTALK 529
Cdd:PRK09847 419 NDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWISLE 494
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
92-524 |
3.87e-150 |
|
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: 436.96 E-value: 3.87e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 92 DINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADK 171
Cdd:cd07104 1 DVDRAYAAAAAAQKA--WAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPK-AAFEVGAAIAILREAAGLPRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 172 IHGLTIPADGPHHVQ-TLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLS-ALLVSKLFHEAGLPEG 249
Cdd:cd07104 78 PEGEILPSDVPGKESmVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 250 VLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFF 329
Cdd:cd07104 158 VLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 330 NQGQCCCAGSRTFVHEKVYDEFVEK--AKARALKrtVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRl 407
Cdd:cd07104 237 HQGQICMAAGRILVHESVYDEFVEKlvAKAKALP--VGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTY- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 408 gtKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWIN 487
Cdd:cd07104 314 --EGLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
410 420 430
....*....|....*....|....*....|....*...
gi 1939884057 488 CFDTFDAA-IPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07104 392 DQTVNDEPhVPFGGVKASGGGRFGGPASLEEFTEWQWI 429
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
57-524 |
1.99e-149 |
|
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: 436.78 E-value: 1.99e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 57 LINGQFVDAASGKTFPTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEV 135
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFPE--WRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 136 AALEAWDSGKPYEQCaQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQ-TLHEPIGVAGQIIPWNFPLVMFGWKVGP 214
Cdd:cd07131 80 ARLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVPSELPNKDAmTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 215 ALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSN 294
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 lKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQ 374
Cdd:cd07131 239 -KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 375 GPQVDADQFEKILKYIRSGAESGATLETGGDRL----GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcFDTFDAAI--PFGGYKMSGIG-REKGEYSLKNYLQVKAV 524
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN-APTIGAEVhlPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
53-527 |
8.01e-147 |
|
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: 430.34 E-value: 8.01e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 53 YDKLlINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHN 132
Cdd:cd07116 1 YDNF-IGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 133 DEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKV 212
Cdd:cd07116 78 EMLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 213 GPALACGNSVVLKTAEQTPLSALLVSKLFHEAgLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELsAK 292
Cdd:cd07116 158 APALAAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY-AS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 293 SNLKPVTLELGGKSPFIVCE------DADVDKAVElaHFALF-FNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVG 365
Cdd:cd07116 236 ENIIPVTLELGGKSPNIFFAdvmdadDAFFDKALE--GFVMFaLNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 366 DPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDR----LGTKGYYIQPTVFSDvKDDMLIAKDEIFGPVQTIL 441
Cdd:cd07116 314 NPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelgGLLGGGYYVPTTFKG-GNKMRIFQEEIFGPVLAVT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 442 KFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQV 521
Cdd:cd07116 393 TFKDEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQT 472
|
....*.
gi 1939884057 522 KAVVTA 527
Cdd:cd07116 473 KNLLVS 478
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
73-524 |
9.68e-147 |
|
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: 429.10 E-value: 9.68e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPY-EQCA 151
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVsAMLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 152 QVEipMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTP 231
Cdd:cd07107 79 DVM--VAAALLDYFAGLVTELKGETIPVGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 232 LSALLVSKLFHEAgLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSnLKPVTLELGGKSPFIVC 311
Cdd:cd07107 157 LSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAAEG-IKHVTLELGGKNALIVF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 312 EDADVDKAVELAHFALFFN-QGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYI 390
Cdd:cd07107 235 PDADPEAAADAAVAGMNFTwCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMHYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 391 RSGAESGATLETGGDR----LGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFT 466
Cdd:cd07107 315 DSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWT 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1939884057 467 QNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07107 395 NDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
71-524 |
8.01e-146 |
|
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: 426.75 E-value: 8.01e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 71 FPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdeGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQc 150
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 151 AQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQ-TLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQ 229
Cdd:cd07150 78 AWFETTFTPELLRAAAGECRRVRGETLPSDSPGTVSmSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 230 TPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFI 309
Cdd:cd07150 158 TPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 310 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKY 389
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 390 IRSGAESGATLETGGDRlgtKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNL 469
Cdd:cd07150 317 VEDAVAKGAKLLTGGKY---DGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 470 DTANTMMRALRAGTVWINCFDTFDAA-IPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07150 394 QRAFKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWI 449
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
71-525 |
5.96e-145 |
|
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: 424.70 E-value: 5.96e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 71 FPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPwpKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQc 150
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK--SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 151 AQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQ-----TLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLK 225
Cdd:cd07149 78 ARKEVDRAIETLRLSAEEAKRLAGETIPFDASPGGEgrigfTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 226 TAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIvleLSAKSNLKPVTLELGGK 305
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEA---IARKAGLKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 306 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEK 385
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 386 ILKYIRSGAESGATLETGGDRLGTkgyYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVF 465
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939884057 466 TQNLDTANTMMRALRAGTVWINCFDTFDA-AIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMINDSSTFRVdHMPYGGVKESGTGREGPRYAIEEMTEIKLVC 452
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
58-524 |
3.80e-144 |
|
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: 423.39 E-value: 3.80e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 58 INGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDeGPWPKMPAYERQKIMLRFADLVEKHNDEVAA 137
Cdd:cd07113 4 IDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 138 LEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGP------HHVQTLHEPIGVAGQIIPWNFPLVMFGWK 211
Cdd:cd07113 83 LETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPsmqgerYTAFTRREPVGVVAGIVPWNFSVMIAVWK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 212 VGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTaGAALCRHMDVDKLAFTGSTETGKIVLElSA 291
Cdd:cd07113 163 IGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGR-QA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 292 KSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAG 371
Cdd:cd07113 241 ASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 372 MEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPT--VFSDVKDDMLiaKDEIFGPVQTILKFKELDEV 449
Cdd:cd07113 321 VMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADSRLM--REETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939884057 450 IRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| OH_muco_semi_DH |
TIGR03216 |
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are ... |
58-524 |
8.83e-144 |
|
2-hydroxymuconic semialdehyde dehydrogenase; Members of this protein family are 2-hydroxymuconic semialdehyde dehydrogenase. Many aromatic compounds are catabolized by way of the catechol, via the meta-cleavage pathway, to pyruvate and acetyl-CoA. This enzyme performs the second of seven steps in that pathway for catechol degradation. [Energy metabolism, Other]
Pssm-ID: 132260 Cd Length: 481 Bit Score: 422.59 E-value: 8.83e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 58 INGQFVdaASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdEGPWPKMPAYERQKIMLRFADLVEKHNDEVAA 137
Cdd:TIGR03216 5 INGAFV--ESGKTFANINPVDGRVIARVHEAGAAEVDAAVAAARAAL-KGPWGKMTVAERADLLYAVADEIERRFDDFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 138 LEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWAdKIHGL----TIPADGPHHVQ-TLHEPIGVAGQIIPWNFPLVMFGWKV 212
Cdd:TIGR03216 82 AEVADTGKPRSLASHLDIPRGAANFRVFADVV-KNAPTecfeMATPDGKGALNyAVRKPLGVVGVISPWNLPLLLMTWKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 213 GPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGP-TAGAALCRHMDVDKLAFTGSTETGKIVLELSA 291
Cdd:TIGR03216 161 GPALACGNTVVVKPSEETPGTATLLGEVMNAVGVPKGVYNVVHGFGPdSAGEFLTRHPGVDAITFTGETRTGSAIMKAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 292 KSnLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAG 371
Cdd:TIGR03216 241 DG-VKPVSFELGGKNAAIVFADCDFDAAVAGILRSAFLNTGQVCLGTERVYVERPIFDRFVAALKARAESLKIGVPDDPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 372 MEQGPQVDADQFEKILKYIRSGAESGATLETGG-------DRLGtkGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFK 444
Cdd:TIGR03216 320 TNMGPLISAEHRDKVLSYYALAVEEGATVVTGGgvpdfgdALAG--GAWVQPTIWTGLPDSARVVTEEIFGPCCHIAPFD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 445 ELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:TIGR03216 398 SEEEVIALANDTPYGLAASVWTEDLSRAHRVARQMEVGIVWVNSWFLRDLRTPFGGSKLSGIGREGGVHSLEFYTELTNV 477
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
57-524 |
7.04e-143 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 421.02 E-value: 7.04e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 57 LINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDegPWPKMPAYERQKIMLRFADLVEKHNDEVA 136
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 137 ALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPH-HVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPA 215
Cdd:PLN02278 106 QLMTLEQGKPLKE-AIGEVAYGASFLEYFAEEAKRVYGDIIPSPFPDrRLLVLKQPVGVVGAITPWNFPLAMITRKVGPA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 216 LACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSnL 295
Cdd:PLN02278 185 LAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAAAT-V 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 296 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQG 375
Cdd:PLN02278 264 KRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 376 PQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANN 455
Cdd:PLN02278 344 PLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAND 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939884057 456 SSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:PLN02278 424 TEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
60-524 |
4.50e-137 |
|
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: 404.76 E-value: 4.50e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 60 GQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALE 139
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKE--WAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 140 AWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGP---HHVqtLHEPIGVAGQIIPWNFPLVMFGWKVGPAL 216
Cdd:cd07151 79 IRESGSTRIK-ANIEWGAAMAITREAATFPLRMEGRILPSDVPgkeNRV--YREPLGVVGVISPWNFPLHLSMRSVAPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 217 ACGNSVVLKTAEQTPLSA-LLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNL 295
Cdd:cd07151 156 ALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAGR-HL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 296 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQG 375
Cdd:cd07151 235 KKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 376 PQVDADQFEKILKYIRSGAESGATLETGGDRLGTkgyYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANN 455
Cdd:cd07151 315 PLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELAND 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 456 SSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAA-IPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07151 392 TEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
56-524 |
3.46e-136 |
|
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: 404.30 E-value: 3.46e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 56 LLINGQFVDaaSGKTFPTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:cd07124 35 LVIGGKEVR--TEEKIESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGP 214
Cdd:cd07124 111 LAAWMVLEVGKNWAE-ADADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTTA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 215 ALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAK-- 292
Cdd:cd07124 190 ALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAKvq 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 293 ---SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFK 369
Cdd:cd07124 270 pgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPED 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 370 AGMEQGPQVDADQFEKILKYIRSGaESGATLETGGDRLG--TKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELD 447
Cdd:cd07124 350 PEVYMGPVIDKGARDRIRRYIEIG-KSEGRLLLGGEVLElaAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFD 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 448 EVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTfdAAI----PFGGYKMSGIG-REKGEYSLKNYLQVK 522
Cdd:cd07124 429 EALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKIT--GALvgrqPFGGFKMSGTGsKAGGPDYLLQFMQPK 506
|
..
gi 1939884057 523 AV 524
Cdd:cd07124 507 TV 508
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
57-524 |
3.70e-134 |
|
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: 398.09 E-value: 3.70e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 57 LINGQFVDAAsGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVA 136
Cdd:cd07086 2 VIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE--WRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 137 ALEAWDSGKPYEQCaQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQ-TLHEPIGVAGQIIPWNFPLVMFGWKVGPA 215
Cdd:cd07086 79 RLVSLEMGKILPEG-LGEVQEMIDICDYAVGLSRMLYGLTIPSERPGHRLmEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 216 LACGNSVVLKTAEQTPLSALLVSKLFHEA----GLPEGVLNIVSGFGPtAGAALCRHMDVDKLAFTGSTETGKIVLELSA 291
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGD-GGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 292 KSNlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAG 371
Cdd:cd07086 237 RRF-GRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 372 MEQGPQVDADQFEKILKYIRSGAESGATLETGGDRL--GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEV 449
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939884057 450 IRRANNSSYGLAAGVFTQNLDTANTMMRALR--AGTVWINcFDTFDAAI--PFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAFRWLGPKGsdCGIVNVN-IPTSGAEIggAFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
71-525 |
9.67e-133 |
|
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: 393.64 E-value: 9.67e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 71 FPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQC 150
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 151 aQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHH-----VQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLK 225
Cdd:cd07145 79 -RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYnerriAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 226 TAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKSNLKPVTLELGGK 305
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIAS-KAGGTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 306 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEK 385
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 386 ILKYIRSGAESGATLETGGDRlgTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVF 465
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGKR--DEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939884057 466 TQNLDTANTMMRALRAGTVWINCFDTF--DaAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINDSTRFrwD-NLPFGGFKKSGIGREGVRYTMLEMTEEKTIV 455
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
74-526 |
7.82e-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: 380.80 E-value: 7.82e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 74 LDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQV 153
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRA--WAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRAD-AGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 154 EIPMFVRLFRYYAGWADKI---HGLTIPADGPHHVQTL-HEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQ 229
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVlapRKVPTGLLMPNKKATVeYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 230 TPLSALLVSKLFHEAGLPEGVLNIVSGFGPTaGAALCRHMdVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFI 309
Cdd:cd07099 158 TPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAAE-RLIPVVLELGGKDPMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 310 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEK--AKARALKrtVGDPFKAGMEQGPQVDADQFEKIL 387
Cdd:cd07099 235 VLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARlvAKARALR--PGADDIGDADIGPMTTARQLDIVR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 388 KYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQ 467
Cdd:cd07099 313 RHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSR 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1939884057 468 NLDTANTMMRALRAGTVWINCFDTFDA--AIPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07099 393 DLARAEAIARRLEAGAVSINDVLLTAGipALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
73-525 |
8.03e-127 |
|
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: 378.22 E-value: 8.03e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAyERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQ 152
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDPR-LRARVLLELADAFEANAERLARLLALENGKILGE-AR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 153 VEIPMFVRLFRYYAGWADKIHGLTI-PADGPHHVqTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTP 231
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIePEPGSFSL-VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 232 LSALLVSKLFHEA-GLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIV 310
Cdd:cd07120 158 QINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAAP-TLKRLGLELGGKTPCIV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 311 CEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYI 390
Cdd:cd07120 237 FDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 391 RSGAESGAT----LETGGDRLgTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFT 466
Cdd:cd07120 317 ERAIAAGAEvvlrGGPVTEGL-AKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWT 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1939884057 467 QNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07120 396 RDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIY 454
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
93-526 |
2.15e-125 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 373.72 E-value: 2.15e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 93 INRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAgwaDKI 172
Cdd:cd07100 1 IEAALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAE-ARAEVEKCAWICRYYA---ENA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 173 HGL----TIPADGPH-HVQtlHEPIGVAGQIIPWNFPLvmfgWKV----GPALACGNSVVLKTAEQTPLSALLVSKLFHE 243
Cdd:cd07100 75 EAFladePIETDAGKaYVR--YEPLGVVLGIMPWNFPF----WQVfrfaAPNLMAGNTVLLKHASNVPGCALAIEELFRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 244 AGLPEGVL-NIVSGFGPTAgaALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVEL 322
Cdd:cd07100 149 AGFPEGVFqNLLIDSDQVE--AIIADPRVRGVTLTGSERAGRAVAAEAGK-NLKKSVLELGGSDPFIVLDDADLDKAVKT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 323 AHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLET 402
Cdd:cd07100 226 AVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 403 GGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAG 482
Cdd:cd07100 306 GGKRPDGPGAFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAG 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1939884057 483 TVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07100 386 MVFINGMVKSDPRLPFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
75-525 |
2.13e-121 |
|
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: 364.45 E-value: 2.13e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 75 DPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQVE 154
Cdd:cd07094 5 NPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKD-ARVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 155 IPMFVRLFRYYAGWADKIHGLTIPAD-----GPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQ 229
Cdd:cd07094 82 VDRAIDTLRLAAEEAERIRGEEIPLDatqgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 230 TPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKivlELSAKSNLKPVTLELGGKSPFI 309
Cdd:cd07094 162 TPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGE---ALRANAGGKRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 310 VCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKY 389
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 390 IRSGAESGATLETGGDRlgtKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNL 469
Cdd:cd07094 319 VEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939884057 470 DTANTMMRALRAGTVWINCFDTFDA-AIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07094 396 NVAFKAAEKLEVGGVMVNDSSAFRTdWMPFGGVKESGVGREGVPYAMEEMTEEKTVV 452
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
92-524 |
7.12e-119 |
|
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: 357.27 E-value: 7.12e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 92 DINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPyEQCAQVEIPMFVRLFRYYAGWADK 171
Cdd:cd07105 1 DADQAVEAAAAAFPA--WSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGAT-AAWAGFNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 172 IHGLTIPADGPHHVQ-TLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGV 250
Cdd:cd07105 78 IIGGSIPSDKPGTLAmVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 251 LNIVSGF---GPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFAL 327
Cdd:cd07105 158 LNVVTHSpedAPEVVEALIAHPAVRKVNFTGSTRVGRIIAETAAK-HLKPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 328 FFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKagmeqGPQVDADQFEKILKYIRSGAESGATLETGG-DR 406
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGPVVL-----GSLVSAAAADRVKELVDDALSKGAKLVVGGlAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 407 LGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWI 486
Cdd:cd07105 312 ESPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHI 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 1939884057 487 NCFDTFD-AAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07105 392 NGMTVHDePTLPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
63-526 |
7.13e-119 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 360.35 E-value: 7.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 63 VDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAfdEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWD 142
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 143 SGK----PYEQCAQVEIPMfvrlfRYYAGWADKI-----HGLTIPadGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVG 213
Cdd:PRK09407 104 TGKarrhAFEEVLDVALTA-----RYYARRAPKLlaprrRAGALP--VLTKTTELRQPKGVVGVISPWNYPLTLAVSDAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 214 PALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHmdVDKLAFTGSTETGKIVLELSAkS 293
Cdd:PRK09407 177 PALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG-R 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 294 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGME 373
Cdd:PRK09407 254 RLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSAD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 374 QGPQVDADQFEKILKYIRSGAESGATLETGGDR---LGTkgYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:PRK09407 334 MGSLISEAQLETVSAHVDDAVAKGATVLAGGKArpdLGP--LFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcfDTFDAA-----IPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:PRK09407 412 ERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVN--EGYAAAwgsvdAPMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
.
gi 1939884057 526 T 526
Cdd:PRK09407 490 T 490
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
56-524 |
1.59e-118 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 359.25 E-value: 1.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 56 LLINGQFVDAAsgKTFPTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:PRK03137 39 LIIGGERITTE--DKIVSINPaNKSEVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYA----GWADKIHGLTIPADgphHVQTLHEPIGVAGQIIPWNFPL-VMFG 209
Cdd:PRK03137 115 FSAWLVKEAGKPWAE-ADADTAEAIDFLEYYArqmlKLADGKPVESRPGE---HNRYFYIPLGVGVVISPWNFPFaIMAG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 210 WKVGPaLACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLEL 289
Cdd:PRK03137 191 MTLAA-IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYER 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 290 SAKSN-----LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTV 364
Cdd:PRK03137 270 AAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTV 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 365 GDPFK-AGMeqGPQVDADQFEKILKYIRSGAESGaTLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKF 443
Cdd:PRK03137 350 GNPEDnAYM--GPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 444 KELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWIN--CFDTFDAAIPFGGYKMSGIGREKG--EYsLKNYL 519
Cdd:PRK03137 427 KDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTDSKAGgpDY-LLLFL 505
|
....*
gi 1939884057 520 QVKAV 524
Cdd:PRK03137 506 QAKTV 510
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
79-507 |
2.14e-118 |
|
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: 356.22 E-value: 2.14e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 79 GEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSG----KpyeqcAQVE 154
Cdd:cd07152 1 GAVLGEVGVADAADVDRAAARAAAAQRA--WAATPPRERAAVLRRAADLLEEHADEIADWIVRESGsirpK-----AGFE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 155 IPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSA 234
Cdd:cd07152 74 VGAAIGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 235 -LLVSKLFHEAGLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCED 313
Cdd:cd07152 154 gVVIARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAGR-HLKKVSLELGGKNALIVLDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 314 ADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSG 393
Cdd:cd07152 232 ADLDLAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 394 AESGATLETGGDRlgtKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTAN 473
Cdd:cd07152 312 VAAGARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAM 388
|
410 420 430
....*....|....*....|....*....|....*
gi 1939884057 474 TMMRALRAGTVWINCFDTFDAAI-PFGGYKMSGIG 507
Cdd:cd07152 389 ALADRLRTGMLHINDQTVNDEPHnPFGGMGASGNG 423
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
57-522 |
2.21e-118 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 357.68 E-value: 2.21e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 57 LINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDegPWPKMPAYERQKIMLRFADLVEKHNDEVA 136
Cdd:PRK11241 14 LINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQDDLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 137 ALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGP-HHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPA 215
Cdd:PRK11241 92 RLMTLEQGKPLAE-AKGEISYAASFIEWFAEEGKRIYGDTIPGHQAdKRLIVIKQPIGVTAAITPWNFPAAMITRKAGPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 216 LACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKsNL 295
Cdd:PRK11241 171 LAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQCAK-DI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 296 KPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQG 375
Cdd:PRK11241 250 KKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 376 PQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANN 455
Cdd:PRK11241 330 PLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQAND 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939884057 456 SSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVK 522
Cdd:PRK11241 410 TEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIK 476
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
75-526 |
2.01e-116 |
|
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: 351.61 E-value: 2.01e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 75 DPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGK----PYEQC 150
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarrhAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 151 AQVEIPMfvrlfRYYAGWADKI-----HGLTIPadGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLK 225
Cdd:cd07101 80 LDVAIVA-----RYYARRAERLlkprrRRGAIP--VLTRTTVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 226 TAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHmdVDKLAFTGSTETGKIVLElSAKSNLKPVTLELGGK 305
Cdd:cd07101 153 PDSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDN--ADYVMFTGSTATGRVVAE-RAGRRLIGCSLELGGK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 306 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEK 385
Cdd:cd07101 230 NPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 386 ILKYIRSGAESGATLETGGDR---LGTkgYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAA 462
Cdd:cd07101 310 VTAHVDDAVAKGATVLAGGRArpdLGP--YFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1939884057 463 GVFTQNLDTANTMMRALRAGTVWINcfDTFDAA-----IPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07101 388 SVWTRDGARGRRIAARLRAGTVNVN--EGYAAAwasidAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
55-526 |
5.17e-115 |
|
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: 348.79 E-value: 5.17e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAaSGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdEGPWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:cd07082 3 KYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQTL-----HEPIGVAGQIIPWNFPLVMFG 209
Cdd:cd07082 81 VANLLMWEIGKTLKD-ALKEVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGKiaqvrREPLGVVLAIGPFNYPLNLTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 210 WKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLEL 289
Cdd:cd07082 160 SKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKKQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 290 SAKsnlKPVTLELGGKSPFIVCEDADVDKAV-ELAHFALFFNqGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPF 368
Cdd:cd07082 240 HPM---KRLVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 369 KAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGtkGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDE 448
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGGREG--GNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 449 VIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCF-----DTFdaaiPFGGYKMSGIGREKGEYSLKNYLQVKA 523
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKcqrgpDHF----PFLGRKDSGIGTQGIGDALRSMTRRKG 469
|
...
gi 1939884057 524 VVT 526
Cdd:cd07082 470 IVI 472
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
74-525 |
2.28e-112 |
|
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: 341.26 E-value: 2.28e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 74 LDPRSGEVIAHVAEGDAEDINRAVAAARkafdeGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQV 153
Cdd:cd07146 4 RNPYTGEVVGTVPAGTEEALREALALAA-----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKD-TRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 154 EIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQ-----TLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAE 228
Cdd:cd07146 78 EVGRAADVLRFAAAEALRDDGESFSCDLTANGKarkifTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 229 QTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVlelSAKSNLKPVTLELGGKSPF 308
Cdd:cd07146 158 KTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 309 IVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEK--AKARALKrtVGDPFKAGMEQGPQVD---ADQF 383
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLlvEKSAALV--VGDPMDPATDMGTVIDeeaAIQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 384 EKIlkyIRSGAESGATLETGGDRlgtKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAG 463
Cdd:cd07146 313 ENR---VEEAIAQGARVLLGNQR---QGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939884057 464 VFTQNLDTANTMMRALRAGTVWINCFDTFDAA-IPFGGYKMSGIG-REKGEYSLKNYLQVKAVV 525
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGgKEGVREAMKEMTNVKTYS 450
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
121-524 |
6.68e-111 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 335.94 E-value: 6.68e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 121 MLRFADLVEKHNDEVAALEAWDSGKPyEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGP-HHVQTLHEPIGVAGQII 199
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKI-QQLAEVEVAFTADYIDYMAEWARRYEGEIIQSDRPgENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 200 PWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGS 279
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 280 TETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARA 359
Cdd:PRK10090 160 VSAGEKIMAAAAK-NITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 360 LKRTVGDPFKAG-MEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQ 438
Cdd:PRK10090 239 QAVQFGNPAERNdIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFGPVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 439 TILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcFDTFDAAIPF-GGYKMSGIGREKGEYSLKN 517
Cdd:PRK10090 319 PVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN-RENFEAMQGFhAGWRKSGIGGADGKHGLHE 397
|
....*..
gi 1939884057 518 YLQVKAV 524
Cdd:PRK10090 398 YLQTQVV 404
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
76-524 |
2.92e-108 |
|
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: 2.92e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 76 PRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQvEI 155
Cdd:cd07102 3 PIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGG-EI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 156 PMFVRLFRYYAGWADK-IHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSA 234
Cdd:cd07102 80 RGMLERARYMISIAEEaLADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 235 LLVSKLFHEAGLPEGVLNIVSGFGPTaGAALCRHMDVDKLAFTGSTETGKIVlELSAKSNLKPVTLELGGKSPFIVCEDA 314
Cdd:cd07102 160 ERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAI-QRAAAGRFIKVGLELGGKDPAYVRPDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 315 DVDKAVE-LAHFAlFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSG 393
Cdd:cd07102 238 DLDAAAEsLVDGA-FFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 394 AESGATLETGGDRLGT---KGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLD 470
Cdd:cd07102 317 IAKGARALIDGALFPEdkaGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1939884057 471 TANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07102 397 RAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
71-525 |
1.95e-106 |
|
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: 325.74 E-value: 1.95e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 71 FPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDegPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQc 150
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 151 AQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQ-----TLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLK 225
Cdd:cd07147 78 ARGEVARAIDTFRIAAEEATRIYGEVLPLDISARGEgrqglVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 226 TAEQTPLSALLVSKLFHEAGLPEGVLNIVSGfgPTAGAA-LCRHMDVDKLAFTGSTETGkivLELSAKSNLKPVTLELGG 304
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADlLVTDERIKLLSFTGSPAVG---WDLKARAGKKKVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 305 KSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEK--AKARALKrtVGDPFKAGMEQGPQVDADQ 382
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRlvARVKALK--TGDPKDDATDVGPMISESE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 383 FEKILKYIRSGAESGATLETGGDRlgtKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAA 462
Cdd:cd07147 311 AERVEGWVNEAVDAGAKLLTGGKR---DGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1939884057 463 GVFTQNLDTANTMMRALRAGTVWINCFDTFDA-AIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07147 388 GVFTRDLEKALRAWDELEVGGVVINDVPTFRVdHMPYGGVKDSGIGREGVRYAIEEMTEPRLLV 451
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
55-507 |
9.15e-106 |
|
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: 324.86 E-value: 9.15e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHH-VQTLHEPIGVAGQIIPWNFPLVMFGWKVG 213
Cdd:cd07085 80 LARLITLEHGKTLAD-ARGDVLRGLEVVEFACSIPHLLKGEYLENVARGIdTYSYRQPLGVVAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 214 PALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKS 293
Cdd:cd07085 159 MAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 294 NlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGME 373
Cdd:cd07085 238 G-KRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 374 QGPQVDADQFEKILKYIRSGAESGATLETGGDRL----GTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEV 449
Cdd:cd07085 317 MGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEA 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939884057 450 IRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcfdtfdAAIP-------FGGYKMSGIG 507
Cdd:cd07085 397 IAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN------VPIPvplaffsFGGWKGSFFG 455
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
75-526 |
5.37e-93 |
|
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: 291.51 E-value: 5.37e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 75 DPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVE 154
Cdd:cd07098 2 DPATGQHLGSVPADTPEDVDEAIAAARAAQRE--WAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 155 IpmFVRLfryyagwaDKIHGLTipADGPHHVQT---------------LH-EPIGVAGQIIPWNFPLVMFGWKVGPALAC 218
Cdd:cd07098 80 I--LVTC--------EKIRWTL--KHGEKALRPesrpggllmfykrarVEyEPLGVVGAIVSWNYPFHNLLGPIIAALFA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 219 GNSVVLKTAEQTPLSAL----LVSKLFHEAGLPEGVLNIVSGFGPTaGAALCRHMDVDKLAFTGSTETGKIVLELSAKSn 294
Cdd:cd07098 148 GNAIVVKVSEQVAWSSGfflsIIRECLAACGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVGKKVMAAAAES- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 LKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQ 374
Cdd:cd07098 226 LTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 375 GPQVDADQFEKILKYIRSGAESGATLETGGDR----LGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:cd07098 306 GAMISPARFDRLEELVADAVEKGARLLAGGKRyphpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAV 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTF--DAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07098 386 EIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
59-518 |
5.48e-92 |
|
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: 289.49 E-value: 5.48e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 59 NGQFVdaASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAAL 138
Cdd:cd07130 4 DGEWG--GGGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRDVPAPKRGEIVRQIGDALRKKKEALGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 139 EAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVqtLHE---PIGVAGQIIPWNFPLVMFGWKVGPA 215
Cdd:cd07130 80 VSLEMGKILPE-GLGEVQEMIDICDFAVGLSRQLYGLTIPSERPGHR--MMEqwnPLGVVGVITAFNFPVAVWGWNAAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 216 LACGNSVVLKTAEQTPLSAL----LVSKLFHEAGLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSA 291
Cdd:cd07130 157 LVCGNVVVWKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 292 KsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKaRALKR-TVGDPFKA 370
Cdd:cd07130 236 A-RFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLK-KAYKQvRIGDPLDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 371 GMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSdVKDDMLIAKDEIFGPVQTILKFKELDEVI 450
Cdd:cd07130 314 GTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939884057 451 RRANNSSYGLAAGVFTQNLDTANTMMRALRA--GTVWINcFDTFDAAI--PFGGYKMSGIGREKGEYSLKNY 518
Cdd:cd07130 393 AWNNEVPQGLSSSIFTTDLRNAFRWLGPKGSdcGIVNVN-IGTSGAEIggAFGGEKETGGGRESGSDAWKQY 463
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
73-524 |
1.15e-90 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 285.48 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQ 152
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLAS-AK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 153 VEIPMFVRLFRYYAGwadkiHGLTIPADGPHHVQTL--------HEPIGVAGQIIPWNFPLvmfgWKV----GPALACGN 220
Cdd:PRK09406 82 AEALKCAKGFRYYAE-----HAEALLADEPADAAAVgasrayvrYQPLGVVLAVMPWNFPL----WQVvrfaAPALMAGN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 221 SVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSgFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELsAKSNLKPVTL 300
Cdd:PRK09406 153 VGLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAI-AGDEIKKTVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 301 ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEK--AKARALKrtVGDPFKAGMEQGPQV 378
Cdd:PRK09406 231 ELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKfvARMAALR--VGDPTDPDTDVGPLA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 379 DADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSY 458
Cdd:PRK09406 309 TEQGRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTF 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 459 GLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:PRK09406 389 GLGSNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
56-511 |
5.00e-83 |
|
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: 266.75 E-value: 5.00e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 56 LLINGQFVDAASGKTfpTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKT--WKDWPQEDRARLLLKAADLLRRRRRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHG--LTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKV 212
Cdd:cd07083 97 LIATLTYEVGKNWVE-AIDDVAEAIDFIRYYARAALRLRYpaVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 213 GPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAK 292
Cdd:cd07083 176 VAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 293 -----SNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDP 367
Cdd:cd07083 256 lapgqTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 368 FKAGMEQGPQVDADQFEKILKYIRSGAESGaTLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFK--E 445
Cdd:cd07083 336 EENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKddD 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 446 LDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcfDTFDAAI----PFGGYKMSGIGREKG 511
Cdd:cd07083 415 FAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYIN--RKITGALvgvqPFGGFKLSGTNAKTG 482
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
38-520 |
6.49e-82 |
|
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: 264.44 E-value: 6.49e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 38 AAALEEPIKPPVSVQYDKL-LINGQfvDAASGKTFPTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAY 115
Cdd:cd07125 16 LEALADALKAFDEKEWEAIpIINGE--ETETGEGAPVIDPaDHERTIGEVSLADAEDVDAALAIAAAAFAG--WSATPVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 116 ERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKiHGLTIPADGPH-HVQTLH-EPIG 193
Cdd:cd07125 92 ERAEILEKAADLLEANRGELIALAAAEAGKTLAD-ADAEVREAIDFCRYYAAQARE-LFSDPELPGPTgELNGLElHGRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 194 VAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDK 273
Cdd:cd07125 170 VFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 274 LAFTGSTETGKIVLELSAKSNLKPVTL--ELGGKSPFIVCEDADVDKAV-ELAHFAlFFNQGQCCCAGSRTFVHEKVYDE 350
Cdd:cd07125 250 VIFTGSTETAKLINRALAERDGPILPLiaETGGKNAMIVDSTALPEQAVkDVVQSA-FGSAGQRCSALRLLYLQEEIAER 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 351 FVEKAK--ARALKrtVGDPFKAGMEQGPQVDADQFEKILKYI-RSGAESGATLETGGDRlgTKGYYIQPTVFSDVKDDML 427
Cdd:cd07125 329 FIEMLKgaMASLK--VGDPWDLSTDVGPLIDKPAGKLLRAHTeLMRGEAWLIAPAPLDD--GNGYFVAPGIIEIVGIFDL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 428 iaKDEIFGPVQTILKFK--ELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTfdAAI----PFGGY 501
Cdd:cd07125 405 --TTEVFGPILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYINRNIT--GAIvgrqPFGGW 480
|
490
....*....|....*....
gi 1939884057 502 KMSGIGREKGEYslkNYLQ 520
Cdd:cd07125 481 GLSGTGPKAGGP---NYLL 496
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
96-526 |
3.62e-78 |
|
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: 251.68 E-value: 3.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 96 AVAAARKAFDEGpwpKMPAYE-RQKIMLRFADLVEKHNDE-VAALEAwDSGKPYEQCAQVEIPMFVRLFRYY----AGWA 169
Cdd:cd07087 3 LVARLRETFLTG---KTRSLEwRKAQLKALKRMLTENEEEiAAALYA-DLGKPPAEAYLTEIAVVLGEIDHAlkhlKKWM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 170 DKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVM-FGWKVGpALACGNSVVLKTAEQTPLSALLVSKLFHEAgLPE 248
Cdd:cd07087 79 KPRRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLaLAPLIG-AIAAGNTVVLKPSELAPATSALLAKLIPKY-FDP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 249 GVLNIVSGFGPTAgAALCRHmDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALF 328
Cdd:cd07087 157 EAVAVVEGGVEVA-TALLAE-PFDHIFFTGSPAVGKIVMEAAAK-HLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 329 FNQGQCCCAGSRTFVHEKVYDEFVEKAKaRALKRTVGDPFKAGMEQGPQVDADQFEKILKYIrsgaeSGATLETGGDRlG 408
Cdd:cd07087 234 LNAGQTCIAPDYVLVHESIKDELIEELK-KAIKEFYGEDPKESPDYGRIINERHFDRLASLL-----DDGKVVIGGQV-D 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 409 TKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINc 488
Cdd:cd07087 307 KEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN- 385
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1939884057 489 fDT-FDAAI---PFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07087 386 -DVlLHAAIpnlPFGGVGNSGMGAYHGKAGFDTFSHLKSVLK 426
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
74-525 |
7.30e-78 |
|
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: 251.95 E-value: 7.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 74 LDPRSGEVIAHVAEGDAEDINRAVAAARKAF-DEGPWpkMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPY----- 147
Cdd:cd07148 4 VNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLvdakv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 148 ---------EQCAQ-------VEIPMfvrlfryyagwadkihGLTiPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWK 211
Cdd:cd07148 82 evtraidgvELAADelgqlggREIPM----------------GLT-PASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 212 VGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAgAALCRHMDVDKLAFTGSTETGkivleLSA 291
Cdd:cd07148 145 VAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVA-EKLVTDPRVAFFSFIGSARVG-----WML 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 292 KSNLKPVT---LELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPF 368
Cdd:cd07148 219 RSKLAPGTrcaLEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 369 KAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGYyiQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDE 448
Cdd:cd07148 299 DPDTEVGPLIRPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDE 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939884057 449 VIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAA-IPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:cd07148 377 AIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYGTGGIPYTMHDMTQEKMAV 454
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
92-513 |
1.65e-77 |
|
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: 250.27 E-value: 1.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 92 DINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKP-YEqcAQVEIpmfvrlfryyAGWAD 170
Cdd:cd07095 1 QVDAAVAAARAAFPG--WAALSLEERAAILRRFAELLKANKEELARLISRETGKPlWE--AQTEV----------AAMAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 171 KIhGLTIPA----------DGPHHVQTL-HEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSK 239
Cdd:cd07095 67 KI-DISIKAyhertgeratPMAQGRAVLrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 240 LFHEAGLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSNLKPVTLELGGKSPFIVCEDADVDKA 319
Cdd:cd07095 146 LWEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 320 VELAHFALFFNQGQCCCAGSRTFVHEK-VYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGA 398
Cdd:cd07095 225 AYLIVQSAFLTAGQRCTCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 399 TLETGGDRLGTKGYYIQPTVFsDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRA 478
Cdd:cd07095 305 EPLLAMERLVAGTAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLAR 383
|
410 420 430
....*....|....*....|....*....|....*.
gi 1939884057 479 LRAGTVWINCFDTFDA-AIPFGGYKMSGIGREKGEY 513
Cdd:cd07095 384 IRAGIVNWNRPTTGASsTAPFGGVGLSGNHRPSAYY 419
|
|
| MMSDH |
TIGR01722 |
methylmalonic acid semialdehyde dehydrogenase; Involved in valine catabolism, ... |
55-526 |
2.97e-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: 250.95 E-value: 2.97e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdeGPWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:TIGR01722 2 NHWIGGKFAEGASGTYIPVTNPATNEVTTKVAFASVDEVDAAVASARETF--LTWGQTSLAQRTSVLLRYQALLKEHRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIPADGPH-HVQTLHEPIGVAGQIIPWNFPLVMFGWKVG 213
Cdd:TIGR01722 80 IAELITAEHGKTHSD-ALGDVARGLEVVEHACGVNSLLKGETSTQVATRvDVYSIRQPLGVCAGITPFNFPAMIPLWMFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 214 PALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVLElSAKS 293
Cdd:TIGR01722 159 IAIACGNTFVLKPSEKVPSAAVKLAELFSEAGAPDGVLNVVHG-DKEAVDRLLEHPDVKAVSFVGSTPIGRYIHT-TGSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 294 NLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSrTFVHEKVYDEFVEKAKARALKRTVGDPFKAGME 373
Cdd:TIGR01722 237 HGKRVQALGGAKNHMVVMPDADKDAAADALVGAAYGAAGQRCMAIS-AAVLVGAADEWVPEIRERAEKIRIGPGDDPGAE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 374 QGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGY----YIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEV 449
Cdd:TIGR01722 316 MGPLITPQAKDRVASLIAGGAAEGAEVLLDGRGYKVDGYeegnWVGPTLLERVPPTMKAYQEEIFGPVLCVLEADTLEEA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 450 IRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcfdtfdAAIP-------FGGYKMSGIGREK--GEYSLKNYLQ 520
Cdd:TIGR01722 396 IALINASPYGNGTAIFTRDGAAARRFQHEIEVGQVGVN------VPIPvplpyfsFTGWKDSFFGDHHiyGKQGTHFYTR 469
|
....*.
gi 1939884057 521 VKAVVT 526
Cdd:TIGR01722 470 GKTVTT 475
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
73-524 |
7.04e-71 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 233.99 E-value: 7.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 73 TLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQ 152
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQ-AR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 153 VEIPMFVRLFRYYAGwadkiHGLTIPADGPHHVQT-----LHEPIGVAGQIIPWNFPLvmfgWKV----GPALACGNSVV 223
Cdd:PRK13968 88 AEVAKSANLCDWYAE-----HGPAMLKAEPTLVENqqaviEYRPLGTILAIMPWNFPL----WQVmrgaVPILLAGNGYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 224 LKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGfgptAGAALCRHMDVDKLA---FTGSTETGKiVLELSAKSNLKPVTL 300
Cdd:PRK13968 159 LKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNA----DNDGVSQMINDSRIAavtVTGSVRAGA-AIGAQAGAALKKCVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 301 ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEK--AKARALKrtVGDPFKAGMEQGPQV 378
Cdd:PRK13968 234 ELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERfvAAAAALK--MGDPRDEENALGPMA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 379 DADQFEKILKYIRSGAESGATLETGGDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSY 458
Cdd:PRK13968 312 RFDLRDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEF 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1939884057 459 GLAAGVFTQNLDTANTMMRALRAGTVWINCFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:PRK13968 392 GLSATIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
63-507 |
7.52e-69 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 239.33 E-value: 7.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 63 VDAASGKTFPTLDPRSGE-VIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAAL--- 138
Cdd:PRK11904 556 IINGEGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAELIALcvr 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 139 EAwdsGKPYeQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGP---HHVQTLHePIGVAGQIIPWNFPLVMFGWKVGPA 215
Cdd:PRK11904 634 EA---GKTL-QDAIAEVREAVDFCRYYAAQARRLFGAPEKLPGPtgeSNELRLH-GRGVFVCISPWNFPLAIFLGQVAAA 708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 216 LACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIV-LELSAKSN 294
Cdd:PRK11904 709 LAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIInRTLAARDG 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 295 lKPVTL--ELGGKSPFIVceDAD------VDKAVELAhfalFFNQGQCCCAGSRTFVHEKVYDEFVE--KAKARALKrtV 364
Cdd:PRK11904 789 -PIVPLiaETGGQNAMIV--DSTalpeqvVDDVVTSA----FRSAGQRCSALRVLFVQEDIADRVIEmlKGAMAELK--V 859
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 365 GDPFKAGMEQGPQVDADQFEKILKYI---RSGAESGATLETGGDrlGTKGYYIQPTVF--SDVKDdmliAKDEIFGPVQT 439
Cdd:PRK11904 860 GDPRLLSTDVGPVIDAEAKANLDAHIermKREARLLAQLPLPAG--TENGHFVAPTAFeiDSISQ----LEREVFGPILH 933
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1939884057 440 ILKFK--ELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcFDTFDAAI---PFGGYKMSGIG 507
Cdd:PRK11904 934 VIRYKasDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYVN-RNQIGAVVgvqPFGGQGLSGTG 1005
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
56-505 |
1.18e-68 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 228.69 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 56 LLINGQFVdAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEV 135
Cdd:PRK09457 3 LWINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 136 AALEAWDSGKPYEQcAQVEIpmfvrlfryyAGWADKIhGLTIPAdgpHHVQT--------------LHEPIGVAGQIIPW 201
Cdd:PRK09457 80 AEVIARETGKPLWE-AATEV----------TAMINKI-AISIQA---YHERTgekrsemadgaavlRHRPHGVVAVFGPY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 202 NFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTE 281
Cdd:PRK09457 145 NFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSAN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 282 TGKIVLELSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVY-DEFVEKAKARAL 360
Cdd:PRK09457 224 TGYLLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 361 KRTVGDPFKAG---MeqGPQVDADQFEKILK----YIRSGAES--GATLETGGDRLGTKGyYIQPTVFSDVKDdmliakD 431
Cdd:PRK09457 304 RLTVGRWDAEPqpfM--GAVISEQAAQGLVAaqaqLLALGGKSllEMTQLQAGTGLLTPG-IIDVTGVAELPD------E 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939884057 432 EIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTV-WINCFDTFDAAIPFGGYKMSG 505
Cdd:PRK09457 375 EYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASG 449
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
57-522 |
8.52e-68 |
|
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: 227.10 E-value: 8.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 57 LINGQFVDAASGKtfPTLDPRS-GEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEV 135
Cdd:TIGR01238 41 IIGHSYKADGEAQ--PVTNPADrRDIVGQVFHANLAHVQAAIDSAQQAFPT--WNATPAKERAAKLDRLADLLELHMPEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 136 AALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGltipadgphhvQTLHEPIGVAGQIIPWNFPLVMFGWKVGPA 215
Cdd:TIGR01238 117 MALCVREAGKTIHN-AIAEVREAVDFCRYYAKQVRDVLG-----------EFSVESRGVFVCISPWNFPLAIFTGQISAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 216 LACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSNL 295
Cdd:TIGR01238 185 LAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQRED 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 296 KPVTL--ELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGME 373
Cdd:TIGR01238 265 APVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 374 QGPQVDADQFEKILKYI---RSGAESGATLETGGDRLGTKGYYIQPTVFSdvKDDMLIAKDEIFGPVQTILKFK--ELDE 448
Cdd:TIGR01238 345 VGPVIDAEAKQNLLAHIehmSQTQKKIAQLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKarELDQ 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1939884057 449 VIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcFDTFDAAI---PFGGYKMSGIG-REKGEYSLKNYLQVK 522
Cdd:TIGR01238 423 IVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVN-RNQVGAVVgvqPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
95-524 |
1.04e-67 |
|
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: 224.80 E-value: 1.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 95 RAVAAARKAFDegpwpkmpAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEI------------------- 155
Cdd:cd07134 8 QAHALALRAST--------AAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEIlpvlseinhaikhlkkwmk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 156 PMFVRLFRYYAGWADKIHgltipadgphhvqtlHEPIGVAGQIIPWNFPlvmFGWKVGP---ALACGNSVVLKTAEQTPL 232
Cdd:cd07134 80 PKRVRTPLLLFGTKSKIR---------------YEPKGVCLIISPWNYP---FNLAFGPlvsAIAAGNTAILKPSELTPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 233 SALLVSKLFHEAGLPEGVlNIVSGFGPTAGAALcrHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCE 312
Cdd:cd07134 142 TSAVIAKIIREAFDEDEV-AVFEGDAEVAQALL--ELPFDHIFFTGSPAVGKIVMAAAAK-HLASVTLELGGKSPTIVDE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 313 DADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKArALKRTVGDpfKAGMEQGPQ----VDADQFEKILK 388
Cdd:cd07134 218 TADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKDAFVEHLKA-EIEKFYGK--DAARKASPDlariVNDRHFDRLKG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 389 YIRSGAESGATLETGGDrLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQN 468
Cdd:cd07134 295 LLDDAVAKGAKVEFGGQ-FDAAQRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKD 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 469 LDTANTMMRALRAGTVWINcfDTF----DAAIPFGGYKMSGIGREKGEYSLKNYLQVKAV 524
Cdd:cd07134 374 KANVNKVLARTSSGGVVVN--DVVlhflNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
190-534 |
1.37e-65 |
|
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: 219.68 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 190 EPIGVAGQIIPWNFP--LVMfgwkvGP---ALACGNSVVLKTAEQTPLSALLVSKLFHEAgLPEGVLNIVSGFGPTAGAA 264
Cdd:cd07136 99 EPYGVVLIIAPWNYPfqLAL-----APligAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEGGVEENQEL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 265 LcrHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVH 344
Cdd:cd07136 173 L--DQKFDYIFFTGSVRVGKIVMEAAAK-HLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 345 EKVYDEFVEkakarALKRTVGDPFKAGMEQGPQ----VDADQFEKILKYIRSGaesgaTLETGG--DRlgtKGYYIQPTV 418
Cdd:cd07136 250 ESVKEKFIK-----ELKEEIKKFYGEDPLESPDygriINEKHFDRLAGLLDNG-----KIVFGGntDR---ETLYIEPTI 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 419 FSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcfDTfdaaI-- 496
Cdd:cd07136 317 LDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN--DT----Imh 390
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1939884057 497 ------PFGGYKMSGIGREKGEYSLKNYLQVKAVVtalKNPAWL 534
Cdd:cd07136 391 lanpylPFGGVGNSGMGSYHGKYSFDTFSHKKSIL---KKSTWF 431
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
189-526 |
3.19e-65 |
|
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: 218.24 E-value: 3.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 189 HEPIGVAGQIIPWNFPLVMfgwKVGP---ALACGNSVVLKTAEQTPLSALLVSKLFHEAgLPEGVLNIVSGFGPTAGAAL 265
Cdd:cd07135 106 KEPLGVVLIIGPWNYPVLL---ALSPlvgAIAAGCTVVLKPSELTPHTAALLAELVPKY-LDPDAFQVVQGGVPETTALL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 266 CRHMDvdKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHE 345
Cdd:cd07135 182 EQKFD--KIFYTGSGRVGRIIAEAAAK-HLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVLVDP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 346 KVYDEFVEKAKaRALKRTVGDPFKAGMEQGPQVDADQFEKILKYIrsgAESGATLETGGDRLGTKgYYIQPTVFSDVKDD 425
Cdd:cd07135 259 SVYDEFVEELK-KVLDEFYPGGANASPDYTRIVNPRHFNRLKSLL---DTTKGKVVIGGEMDEAT-RFIPPTIVSDVSWD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 426 MLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcfDTFDAA----IPFGGY 501
Cdd:cd07135 334 DSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVIN--DTLIHVgvdnAPFGGV 411
|
330 340
....*....|....*....|....*
gi 1939884057 502 KMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07135 412 GDSGYGAYHGKYGFDTFTHERTVVK 436
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
55-533 |
6.90e-64 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 216.55 E-value: 6.90e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 55 KLLINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAfdEGPWPKMPAYERQKIMLRFADLVEKHNDE 134
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 135 VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYA-------GWADKIHGLTIPADGPHHVQTLHE-PIGVAGQIIPWNFPLV 206
Cdd:PLN00412 95 IAECLVKEIAKPAKD-AVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNERNKYCLTSKiPLGVVLAIPPFNYPVN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 207 MFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGStETGkiv 286
Cdd:PLN00412 174 LAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTG--- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 287 LELSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGD 366
Cdd:PLN00412 250 IAISKKAGMVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 367 PfKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRlgtKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKEL 446
Cdd:PLN00412 330 P-EDDCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKR---EGNLIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 447 DEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCF-----DTFdaaiPFGGYKMSGIGREKGEYSLKNYLQV 521
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApargpDHF----PFQGLKDSGIGSQGITNSINMMTKV 481
|
490
....*....|..
gi 1939884057 522 KAVVTALKNPAW 533
Cdd:PLN00412 482 KSTVINLPKPSY 493
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
101-526 |
5.36e-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: 212.35 E-value: 5.36e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 101 RKAFDEGPWPkmPAYERQKIMLRFADLVEKHNDE-VAALEAWDSGKPYEQCAQVEIPMFVRLFRYY----AGW--ADKIH 173
Cdd:cd07133 8 KAAFLANPPP--SLEERRDRLDRLKALLLDNQDAlAEAISADFGHRSRHETLLAEILPSIAGIKHArkhlKKWmkPSRRH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 174 -GLTIPadgPHHVQTLHEPIGVAGQIIPWNFPLVMfgwKVGP---ALACGNSVVLKTAEQTPLSALLVSKLFHEAgLPEG 249
Cdd:cd07133 86 vGLLFL---PAKAEVEYQPLGVVGIIVPWNYPLYL---ALGPliaALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDED 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 250 VLNIVSGfGPTAGAALCRhMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFF 329
Cdd:cd07133 159 EVAVVTG-GADVAAAFSS-LPFDHLLFTGSTAVGRHVMRAAAE-NLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 330 NQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRtvgdpFKAGMEqGPQ----VDADQFEKILKYIRSGAESGATLET--G 403
Cdd:cd07133 236 NAGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-----YPTLAD-NPDytsiINERHYARLQGLLEDARAKGARVIElnP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 404 GDRLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGT 483
Cdd:cd07133 310 AGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1939884057 484 VWINcfDT-FDAA---IPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07133 390 VTIN--DTlLHVAqddLPFGGVGASGMGAYHGKEGFLTFSHAKPVFK 434
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
36-507 |
2.62e-62 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 221.28 E-value: 2.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 36 AAAAALEEPIKPPVSVQYD-KLLINGqfvDAASGKTFPTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMP 113
Cdd:PRK11905 536 ATLAALDEALNAFAAKTWHaAPLLAG---GDVDGGTRPVLNPaDHDDVVGTVTEASAEDVERALAAAQAAFPE--WSATP 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 114 AYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYeQCAQVEIPMFVRLFRYYAGWADKIhgltiPADGPHhvqtlhEPIG 193
Cdd:PRK11905 611 AAERAAILERAADLMEAHMPELFALAVREAGKTL-ANAIAEVREAVDFLRYYAAQARRL-----LNGPGH------KPLG 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 194 VAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDK 273
Cdd:PRK11905 679 PVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAG 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 274 LAFTGSTETGKIVLELSAKSNLKPVTL--ELGGKSPFIV-----CEDAdVDKAVELAhfalFFNQGQCCCAGSRTFVHEK 346
Cdd:PRK11905 759 VMFTGSTEVARLIQRTLAKRSGPPVPLiaETGGQNAMIVdssalPEQV-VADVIASA----FDSAGQRCSALRVLCLQED 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 347 VYDEFVEKAKArALK-RTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGT-KGYYIQPTVFS-DVK 423
Cdd:PRK11905 834 VADRVLTMLKG-AMDeLRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLPLPAETeKGTFVAPTLIEiDSI 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 424 DDMliaKDEIFGPVQTILKFK--ELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcFDTFDAAI---PF 498
Cdd:PRK11905 913 SDL---EREVFGPVLHVVRFKadELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVN-RNIIGAVVgvqPF 988
|
....*....
gi 1939884057 499 GGYKMSGIG 507
Cdd:PRK11905 989 GGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
36-507 |
3.79e-61 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 217.88 E-value: 3.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 36 AAAAALEEPIKPPVSVQYDKL-LINGQfvdAASGKTFPTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFDEgpWPKMP 113
Cdd:COG4230 539 AVLAALSAALAAAAEKQWQAApLIAGE---AASGEARPVRNPaDHSDVVGTVVEATAADVEAALAAAQAAFPA--WSATP 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 114 AYERQKIMLRFADLVEKHNDEVAAL---EAwdsGKPYeQCAQVEIPMFVRLFRYYAGWADKIhgltipADGPhhvqTLHE 190
Cdd:COG4230 614 VEERAAILERAADLLEAHRAELMALlvrEA---GKTL-PDAIAEVREAVDFCRYYAAQARRL------FAAP----TVLR 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 191 PIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMD 270
Cdd:COG4230 680 GRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGVPADVLQLLPGDGETVGAALVADPR 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 271 VDKLAFTGSTETGKIV-LELSAKSNlKPVTL--ELGGKSPFIV-----CEDAdVDKAVELAhfalFFNQGQCCCAGSRTF 342
Cdd:COG4230 760 IAGVAFTGSTETARLInRTLAARDG-PIVPLiaETGGQNAMIVdssalPEQV-VDDVLASA----FDSAGQRCSALRVLC 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 343 VHEKVYDEFVE--KAKARALKrtVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATL-ETGGDRLGTKGYYIQPTVF 419
Cdd:COG4230 834 VQEDIADRVLEmlKGAMAELR--VGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLVhQLPLPEECANGTFVAPTLI 911
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 420 --SDVKDdmLiaKDEIFGPVQTILKFK--ELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINcFDTFDAA 495
Cdd:COG4230 912 eiDSISD--L--EREVFGPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN-RNIIGAV 986
|
490
....*....|....*
gi 1939884057 496 I---PFGGYKMSGIG 507
Cdd:COG4230 987 VgvqPFGGEGLSGTG 1001
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
57-530 |
4.75e-61 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 211.53 E-value: 4.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 57 LINGQFVDAASGKTFPTLDPRSGEVIAHVAEGDAEDINRAVAAARKAFdegP-WPKMPAYERQKIMLRFADLVEKHNDEV 135
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAF---PlWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 136 AALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGWADKIHGLTIP--ADGPHhVQTLHEPIGVAGQIIPWNFPLVMFGWKVG 213
Cdd:PLN02419 194 AMNITTEQGKTLKD-SHGDIFRGLEVVEHACGMATLQMGEYLPnvSNGVD-TYSIREPLGVCAGICPFNFPAMIPLWMFP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 214 PALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGaALCRHMDVDKLAFTGSTETGKIVLELSAKS 293
Cdd:PLN02419 272 VAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAAAK 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 294 NlKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSR-TFVHEKVY--DEFVEKAKarALKRTVGDPFKA 370
Cdd:PLN02419 351 G-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDAKSweDKLVERAK--ALKVTCGSEPDA 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 371 GMeqGPQVDADQFEKILKYIRSGAESGATLETGGDRLGTKGY----YIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKEL 446
Cdd:PLN02419 428 DL--GPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSF 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 447 DEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGTVWINCfdTFDAAIP---FGGYKMSGIGREK--GEYSLKNYLQV 521
Cdd:PLN02419 506 DEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPffsFTGNKASFAGDLNfyGKAGVDFFTQI 583
|
....*....
gi 1939884057 522 KAVVTALKN 530
Cdd:PLN02419 584 KLVTQKQKD 592
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
66-520 |
2.28e-60 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 207.38 E-value: 2.28e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 66 ASGKTFPTLDPRSGEVIAHVAEGDAEDIN---RAVAAARKAfdegpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWD 142
Cdd:PLN02315 31 ANGPLVSSVNPANNQPIAEVVEASLEDYEeglRACEEAAKI-----WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 143 SGKPYEQCAQvEIPMFVRLFRYYAGWADKIHGLTIPADGPHHVQT-LHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNS 221
Cdd:PLN02315 106 MGKILAEGIG-EVQEIIDMCDFAVGLSRQLNGSIIPSERPNHMMMeVWNPLGIVGVITAFNFPCAVLGWNACIALVCGNC 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 222 VVLKTAEQTPLSALLVSKLFHEA----GLPEGVLNIVSGfGPTAGAALCRHMDVDKLAFTGSTETGKIVlELSAKSNLKP 297
Cdd:PLN02315 185 VVWKGAPTTPLITIAMTKLVAEVleknNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMV-QQTVNARFGK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 298 VTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGP- 376
Cdd:PLN02315 263 CLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPl 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 377 --QVDADQFEKILKYIRSgaeSGATLETGGDRLGTKGYYIQPTVFsDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRAN 454
Cdd:PLN02315 343 htPESKKNFEKGIEIIKS---QGGKILTGGSAIESEGNFVQPTIV-EISPDADVVKEELFGPVLYVMKFKTLEEAIEINN 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 455 NSSYGLAAGVFTQNLDTANTMMRALRA--GTVWINcFDTFDAAI--PFGGYKMSGIGREKGEYSLKNYLQ 520
Cdd:PLN02315 419 SVPQGLSSSIFTRNPETIFKWIGPLGSdcGIVNVN-IPTNGAEIggAFGGEKATGGGREAGSDSWKQYMR 487
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
31-505 |
1.72e-58 |
|
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: 202.82 E-value: 1.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 31 YRYGTAAAAALEEPIK----PPVSVQydkLLINGQFVDaaSGKTFPTLDP-RSGEVIAHVAEGDAEDINRAVAAARKAFD 105
Cdd:cd07123 9 YAPGSPERAKLQEALAelksLTVEIP---LVIGGKEVR--TGNTGKQVMPhDHAHVLATYHYADAALVEKAIEAALEARK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 106 EgpWPKMPAYERQKIMLRFADLVE-KHNDEVAALEAWDSGKpyeQCAQVEIPMFVRL---FRYYAGWADKIHgltipadg 181
Cdd:cd07123 84 E--WARMPFEDRAAIFLKAADLLSgKYRYELNAATMLGQGK---NVWQAEIDAACELidfLRFNVKYAEELY-------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 182 phHVQTLHEPIGVAGQ------------IIPWNFPLVMFGWKVGPALAcGNSVVLKTAEQTPLSALLVSKLFHEAGLPEG 249
Cdd:cd07123 151 --AQQPLSSPAGVWNRleyrplegfvyaVSPFNFTAIGGNLAGAPALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 250 VLNIVSGFGPTAGAALCRHMDVDKLAFTGSTET-----GKIVLELSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAH 324
Cdd:cd07123 228 VINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTfkslwKQIGENLDRYRTYPRIVGETGGKNFHLVHPSADVDSLVTATV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 325 FALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYI-RSGAESGATLETG 403
Cdd:cd07123 308 RGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIdHAKSDPEAEIIAG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 404 GDRLGTKGYYIQPTVF--SDVKDDMLiaKDEIFGPVQTILKF--KELDEVIRRANNSS-YGLAAGVFTQNLDTANTMMRA 478
Cdd:cd07123 388 GKCDDSVGYFVEPTVIetTDPKHKLM--TEEIFGPVLTVYVYpdSDFEETLELVDTTSpYALTGAIFAQDRKAIREATDA 465
|
490 500 510
....*....|....*....|....*....|...
gi 1939884057 479 LR--AGTVWINCFDTfdAAI----PFGGYKMSG 505
Cdd:cd07123 466 LRnaAGNFYINDKPT--GAVvgqqPFGGARASG 496
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
89-525 |
5.63e-58 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 200.64 E-value: 5.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 89 DAEDINRAVAAARKAFDEGPWPKMPAYERQ-KIMLRFadLVEKHNDEVAALEAwDSGKPYEQCAQVEIPMFV-------- 159
Cdd:PTZ00381 5 NPEIIPPIVKKLKESFLTGKTRPLEFRKQQlRNLLRM--LEENKQEFSEAVHK-DLGRHPFETKMTEVLLTVaeiehllk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 160 RLFRYYAGWADKIHGLTIPADGphhvQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSK 239
Cdd:PTZ00381 82 HLDEYLKPEKVDTVGVFGPGKS----YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 240 LFHEAgLPEGVLNIVSGfGPTAGAALCRHmDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKA 319
Cdd:PTZ00381 158 LLTKY-LDPSYVRVIEG-GVEVTTELLKE-PFDHIFFTGSPRVGKLVMQAAAE-NLTPCTLELGGKSPVIVDKSCNLKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 320 VELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKaRALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRsgaESGAT 399
Cdd:PTZ00381 234 ARRIAWGKFLNAGQTCVAPDYVLVHRSIKDKFIEALK-EAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIK---DHGGK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 400 LETGGDrLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRAL 479
Cdd:PTZ00381 310 VVYGGE-VDIENKYVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENT 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1939884057 480 RAGTVWIN--CFDTFDAAIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:PTZ00381 389 SSGAVVINdcVFHLLNPNLPFGGVGNSGMGAYHGKYGFDTFSHPKPVL 436
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
96-514 |
4.97e-52 |
|
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: 183.19 E-value: 4.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 96 AVAAARKAFDEGpwpKMPAYE-RQKIMLRFADLVEKHNDE-VAALEAwDSGKPYEQCAQVEIpMFVR-----LFRYYAGW 168
Cdd:cd07132 3 AVRRAREAFSSG---KTRPLEfRIQQLEALLRMLEENEDEiVEALAK-DLRKPKFEAVLSEI-LLVKneikyAISNLPEW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 169 ADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPL-VMFGWKVGpALACGNSVVLKTAEQTPLSALLVSKLfheagLP 247
Cdd:cd07132 78 MKPEPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLqLTLVPLVG-AIAAGNCVVIKPSEVSPATAKLLAEL-----IP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 248 EGVLN----IVSGfGPTAGAALCRHmDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELA 323
Cdd:cd07132 152 KYLDKecypVVLG-GVEETTELLKQ-RFDYIFYTGSTSVGKIVMQAAAK-HLTPVTLELGGKSPCYVDKSCDIDVAARRI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 324 HFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKaRALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGaesgaTLETG 403
Cdd:cd07132 229 AWGKFINAGQTCIAPDYVLCTPEVQEKFVEALK-KTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGG-----KVAIG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 404 GDrLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAGT 483
Cdd:cd07132 303 GQ-TDEKERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGG 381
|
410 420 430
....*....|....*....|....*....|....*
gi 1939884057 484 VWINcfDTFDAAI----PFGGYKMSGIGREKGEYS 514
Cdd:cd07132 382 VCVN--DTIMHYTldslPFGGVGNSGMGAYHGKYS 414
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
75-511 |
4.58e-48 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 179.78 E-value: 4.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 75 DPRsgEVIAHVAEGDAEDINRAVAAARKAfdeGP-WPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQcAQV 153
Cdd:PRK11809 668 DPR--DIVGYVREATPAEVEQALESAVNA---APiWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSN-AIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 154 EIPMFVRLFRYYAGWADkihgltipadgPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLS 233
Cdd:PRK11809 742 EVREAVDFLRYYAGQVR-----------DDFDNDTHRPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 234 ALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLE-----LSAKSNLKPVTLELGGKSPF 308
Cdd:PRK11809 811 AAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRnlagrLDPQGRPIPLIAETGGQNAM 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 309 IVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILK 388
Cdd:PRK11809 891 IVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIER 970
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 389 YIRSGAESGATL------ETGGDRLGTkgyYIQPTVFS-DVKDDMliaKDEIFGPVQTILKFK--ELDEVIRRANNSSYG 459
Cdd:PRK11809 971 HIQAMRAKGRPVfqaareNSEDWQSGT---FVPPTLIElDSFDEL---KREVFGPVLHVVRYNrnQLDELIEQINASGYG 1044
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1939884057 460 LAAGVFTQNLDTANTMMRALRAGTVWINcFDTFDAAI---PFGGYKMSGIGREKG 511
Cdd:PRK11809 1045 LTLGVHTRIDETIAQVTGSAHVGNLYVN-RNMVGAVVgvqPFGGEGLSGTGPKAG 1098
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
95-526 |
1.39e-46 |
|
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: 168.36 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 95 RAVAAARKAFDEGpwpKMPAYERQKIMLR-FADLVEKHNDE-VAALEAwDSGKPYEQCAQVEIPMFVR--------LFRY 164
Cdd:cd07137 3 RLVRELRETFRSG---RTRSAEWRKSQLKgLLRLVDENEDDiFAALRQ-DLGKPSAESFRDEVSVLVSscklaikeLKKW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 165 YAGWADKIHGLTIPADGphhvQTLHEPIGVAGQIIPWNFPlvmFGWKVGP---ALACGNSVVLKTAEQTPLSALLVSKLF 241
Cdd:cd07137 79 MAPEKVKTPLTTFPAKA----EIVSEPLGVVLVISAWNFP---FLLSLEPvigAIAAGNAVVLKPSELAPATSALLAKLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 242 hEAGLPEGVLNIVSGfGPTAGAALCRHmDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVceDADVDKAVE 321
Cdd:cd07137 152 -PEYLDTKAIKVIEG-GVPETTALLEQ-KWDKIFFTGSPRVGRIIMAAAAK-HLTPVTLELGGKCPVIV--DSTVDLKVA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 322 LAHFAL---FFNQGQCCCAGSRTFVHEKVYDEFVEKAKaRALKRTVGDPFKAGMEQGPQVDADQFEKiLKYIRSGAESGA 398
Cdd:cd07137 226 VRRIAGgkwGCNNGQACIAPDYVLVEESFAPTLIDALK-NTLEKFFGENPKESKDLSRIVNSHHFQR-LSRLLDDPSVAD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 399 TLETGGDRlGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRA 478
Cdd:cd07137 304 KIVHGGER-DEKNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAE 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1939884057 479 LRAGTVWINcfdtfDAAI-------PFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:cd07137 383 TSSGGVTFN-----DTVVqyaidtlPFGGVGESGFGAYHGKFSFDAFSHKKAVLY 432
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
90-525 |
1.24e-33 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 133.25 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 90 AEDINRAVAAARKAFDEGpwpKMPAYE-RQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEIPMF---VRL-FRY 164
Cdd:PLN02174 9 AADASILVTELRRSFDDG---VTRGYEwRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLrnsIKLaLKQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 165 YAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFhEA 244
Cdd:PLN02174 86 LKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 245 GLPEGVLNIVSGFGPTAGAALcrHMDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAH 324
Cdd:PLN02174 165 YLDSSAVRVVEGAVTETTALL--EQKWDKIFYTGSSKIGRVIMAAAAK-HLTPVVLELGGKSPVVVDSDTDLKVTVRRII 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 325 FALF-FNQGQCCCAGSRTFVHEKVYDEFVEKAKARALKRTVGDPFKAgMEQGPQVDADQFEKILKYIRSGAESGATLETG 403
Cdd:PLN02174 242 AGKWgCNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMES-KDMSRIVNSTHFDRLSKLLDEKEVSDKIVYGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 404 -GDRLGTKgyyIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRALRAG 482
Cdd:PLN02174 321 eKDRENLK---IAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAG 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1939884057 483 TVWINCFDTFDA--AIPFGGYKMSGIGREKGEYSLKNYLQVKAVV 525
Cdd:PLN02174 398 GIVVNDIAVHLAlhTLPFGGVGESGMGAYHGKFSFDAFSHKKAVL 442
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
86-526 |
6.19e-33 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 131.39 E-value: 6.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 86 AEGDAEDINRAVAAARKAFDEGPWPKMPAYERQ-KIMLRFadLVEKHNDEVAALEAwDSGKPYEQCAQVEIPMFVRLFRY 164
Cdd:PLN02203 1 EEAPGETLEGSVAELRETYESGRTRSLEWRKSQlKGLLRL--LKDNEEAIFKALHQ-DLGKHRVEAYRDEVGVLTKSANL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 165 ----YAGWADKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPlvmFGWKVGP---ALACGNSVVLKTAEQTPLSALLV 237
Cdd:PLN02203 78 alsnLKKWMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFP---IGLSLEPligAIAAGNAVVLKPSELAPATSAFL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 238 SKLFhEAGLPEGVLNIVSGfGPTAGAALCRHmDVDKLAFTGSTETGKIVLELSAKsNLKPVTLELGGKSPFIV-CEDADV 316
Cdd:PLN02203 155 AANI-PKYLDSKAVKVIEG-GPAVGEQLLQH-KWDKIFFTGSPRVGRIIMTAAAK-HLTPVALELGGKCPCIVdSLSSSR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 317 DKAVEL-----AHFALFfnQGQCCCAGSRTFVHEKVYDEFVEKAKArALKRTVGDPFKAGMEQGPQVDADQFEKILKYIR 391
Cdd:PLN02203 231 DTKVAVnrivgGKWGSC--AGQACIAIDYVLVEERFAPILIELLKS-TIKKFFGENPRESKSMARILNKKHFQRLSNLLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 392 SGAESGATLETGGdrLGTKGYYIQPTVFSDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDT 471
Cdd:PLN02203 308 DPRVAASIVHGGS--IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1939884057 472 ANTMMRALRAGTVWINcfdtfDA-------AIPFGGYKMSGIGREKGEYSLKNYLQVKAVVT 526
Cdd:PLN02203 386 KRRILSETSSGSVTFN-----DAiiqyacdSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLR 442
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
94-487 |
2.62e-30 |
|
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: 123.12 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 94 NRAVAAARKafDEGPWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEIPMFVRLFRYYAGWADKIH 173
Cdd:cd07084 2 ERALLAADI--STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVIYSYRIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 174 GLTIPADGPHHVQTLHE---PIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAG-LPEG 249
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 250 VLNIVSGFGPTaGAALCRHMDVDKLAFTGSTETGKivlELSAKSNLKPVTLELGGKSPFIVCEDADVDKAV--ELAhFAL 327
Cdd:cd07084 160 DVTLINGDGKT-MQALLLHPNPKMVLFTGSSRVAE---KLALDAKQARIYLELAGFNWKVLGPDAQAVDYVawQCV-QDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 328 FFNQGQCCCAGSRTFVHEKVYDE-FVEKAKARALKRTVGDPFkagmeqgpqVDADQFEKILKYIRS-GAESGATLETGG- 404
Cdd:cd07084 235 TACSGQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLL---------LGPVQTFTTLAMIAHmENLLGSVLLFSGk 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 405 -----DRLGTKGYYIQPTVF--SDVKDDMLIAKD-EIFGPVQTILKFKE-----LDEVIRRANNSsygLAAGVFTQNLDT 471
Cdd:cd07084 306 elknhSIPSIYGACVASALFvpIDEILKTYELVTeEIFGPFAIVVEYKKdqlalVLELLERMHGS---LTAAIYSNDPIF 382
|
410
....*....|....*..
gi 1939884057 472 ANTMMRAL-RAGTVWIN 487
Cdd:cd07084 383 LQELIGNLwVAGRTYAI 399
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
58-466 |
1.40e-29 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 122.12 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 58 INGQFVdAASGKTFPTLDPRSGEVIAHVaEGDAEDINRAVAAARKafDEGPWPKMPAYERQKIMLR-FADLVEKHNDEVA 136
Cdd:PRK11903 9 VAGRWQ-AGSGAGTPLFDPVTGEELVRV-SATGLDLAAAFAFARE--QGGAALRALTYAQRAALLAaIVKVLQANRDAYY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 137 ALEAWDSGKpYEQCAQVEIPMFVRLFRYYAGWADKIHGLTIPADGP------------HHVQTlhePI-GVAGQIIPWNF 203
Cdd:PRK11903 85 DIATANSGT-TRNDSAVDIDGGIFTLGYYAKLGAALGDARLLRDGEavqlgkdpafqgQHVLV---PTrGVALFINAFNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 204 PlvmfGW----KVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAG-LPEGVLNIVSGfgptAGAALCRHMD-VDKLAFT 277
Cdd:PRK11903 161 P----AWglweKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCG----SSAGLLDHLQpFDVVSFT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 278 GSTETGKI------VLELSAKSNLKPVTLELGgkspfIVCEDADVDKAVelahFALFFNQ---------GQCCCAGSRTF 342
Cdd:PRK11903 233 GSAETAAVlrshpaVVQRSVRVNVEADSLNSA-----LLGPDAAPGSEA----FDLFVKEvvremtvksGQKCTAIRRIF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 343 VHEKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGG-----DRLGTKGYYIQPT 417
Cdd:PRK11903 304 VPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLFDGGgfalvDADPAVAACVGPT 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1939884057 418 VF--SDVKDDMLIAKDEIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFT 466
Cdd:PRK11903 384 LLgaSDPDAATAVHDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYS 434
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
58-479 |
8.98e-28 |
|
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: 116.60 E-value: 8.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 58 INGQFVdAASGKTFPTLDPRSGEVIAHVAeGDAEDINRAVAAARKafDEGP-WPKMPAYERQKIMLRFADLVEKHNDEVA 136
Cdd:cd07128 5 VAGQWH-AGTGDGRTLHDAVTGEVVARVS-SEGLDFAAAVAYARE--KGGPaLRALTFHERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 137 ALEAWDSGKPYEQCAQVEIPMFVrLFrYYAGWADK-IHGLTIPADGP------------HHVQTlhePI-GVAGQIIPWN 202
Cdd:cd07128 81 ALSAATGATRRDSWIDIDGGIGT-LF-AYASLGRReLPNAHFLVEGDveplskdgtfvgQHILT---PRrGVAVHINAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 203 FPLvmfgW----KVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAG-LPEGVLNIVSGfgpTAGAALCRHMDVDKLAFT 277
Cdd:cd07128 156 FPV----WgmleKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICG---SVGDLLDHLGEQDVVAFT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 278 GSTETGKIvleLSAKSNLK----PVTLELGGKSPFIVCEDADVDKAvelaHFALFFNQ---------GQCCCAGSRTFVH 344
Cdd:cd07128 229 GSAATAAK---LRAHPNIVarsiRFNAEADSLNAAILGPDATPGTP----EFDLFVKEvaremtvkaGQKCTAIRRAFVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 345 EKVYDEFVEKAKARALKRTVGDPFKAGMEQGPQVDADQFEKILKYIRSGAESGATLETGGDRLGT------KGYYIQPTV 418
Cdd:cd07128 302 EARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVvgadaeKGAFFPPTL 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1939884057 419 FsdVKDDMLIAKD----EIFGPVQTILKFKELDEVIRRANNSSYGLAAGVFTQNLDTANTMMRAL 479
Cdd:cd07128 382 L--LCDDPDAATAvhdvEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGA 444
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
57-475 |
6.53e-16 |
|
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: 80.23 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 57 LINGQFVDAASGKTFptLDPRSGEVIAHVAEGDAEDINRAVAAARKAFDEGPWPKMPAYERQ----KIMLRFADLVEKHN 132
Cdd:cd07126 2 LVAGKWKGASNYTTL--LDPLNGDKFISVPDTDEDEINEFVDSLRQCPKSGLHNPLKNPERYllygDVSHRVAHELRKPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 133 DE--VAALEAWDSGKPYEQcAQVEIPMFVRLFRYYAGwaDKIH----GLTIPADgpHHVQTLHE---PIGVAGQIIPWNF 203
Cdd:cd07126 80 VEdfFARLIQRVAPKSDAQ-ALGEVVVTRKFLENFAG--DQVRflarSFNVPGD--HQGQQSSGyrwPYGPVAIITPFNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 204 PLVMFGWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRhMDVDKLAFTGSTETG 283
Cdd:cd07126 155 PLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-ANPRMTLFTGSSKVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 284 -KIVLELSAKsnlkpVTLELGGKSPFIVCED-ADVDKAVELAHFALFFNQGQCCCAGSRTFVHEK-VYDEFVEKAKARAL 360
Cdd:cd07126 234 eRLALELHGK-----VKLEDAGFDWKILGPDvSDVDYVAWQCDQDAYACSGQKCSAQSILFAHENwVQAGILDKLKALAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 361 KRTVGDpfkagMEQGPQVDADQfEKILKYIRS-GAESGATLETGGDRLgtKGYYI-------QPT-VF-----SDVKDDM 426
Cdd:cd07126 309 QRKLED-----LTIGPVLTWTT-ERILDHVDKlLAIPGAKVLFGGKPL--TNHSIpsiygayEPTaVFvpleeIAIEENF 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1939884057 427 LIAKDEIFGPVQTILKFK--ELDEVIRRANNSSYGLAAGV------FTQNLdTANTM 475
Cdd:cd07126 381 ELVTTEVFGPFQVVTEYKdeQLPLVLEALERMHAHLTAAVvsndirFLQEV-LANTV 436
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
93-454 |
2.60e-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: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 93 INRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKPyEQCAQVEIP-------MFVRLFRyy 165
Cdd:cd07129 1 VDAAAAAAAAAFES--YRALSPARRAAFLEAIADEIEALGDELVARAHAETGLP-EARLQGELGrttgqlrLFADLVR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 166 AGWAdkiHGLTI--------PADGPHHVQtLHEPIGVAGQIIPWNFPLVmF---GWKVGPALACGNSVVLK-------TA 227
Cdd:cd07129 76 EGSW---LDARIdpadpdrqPLPRPDLRR-MLVPLGPVAVFGASNFPLA-FsvaGGDTASALAAGCPVVVKahpahpgTS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 228 EqtpLSALLVSKLFHEAGLPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGSTETGKIVLELSAKSNL-KPVTLELGGKS 306
Cdd:cd07129 151 E---LVARAIRAALRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 307 PFIVCEDADVDKAVELAH-FA--LFFNQGQ-CCCAGSRTFVHEKVYDEFVEKAkARALKRTVGDP-FKAGMEQGPQVDAD 381
Cdd:cd07129 228 PVFILPGALAERGEAIAQgFVgsLTLGAGQfCTNPGLVLVPAGPAGDAFIAAL-AEALAAAPAQTmLTPGIAEAYRQGVE 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1939884057 382 QFEkilkyirsgAESGATLETGGDrLGTKGYYIQPTVFSdVKDDMLIAKD----EIFGPVQTILKFKELDEVIRRAN 454
Cdd:cd07129 307 ALA---------AAPGVRVLAGGA-AAEGGNQAAPTLFK-VDAAAFLADPalqeEVFGPASLVVRYDDAAELLAVAE 372
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
115-356 |
5.10e-15 |
|
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: 76.88 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 115 YERQKIMLRFADLVEKHNDEVAALEAWDSGKPYEQCAQVEIPMFVRL----------FRYYAGWADKIHGLTIPADGPHH 184
Cdd:cd07077 16 EQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIANWIAMMGCSesklyknidtERGITASVGHIQDVLLPDNGETY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 185 VQTlhEPIGVAGQIIPWNFPLVMFgWKVGPALACGNSVVLKTAEQTPLSALLVSKLFHEA---GLPEGVLNIVSGFGPTA 261
Cdd:cd07077 96 VRA--FPIGVTMHILPSTNPLSGI-TSALRGIATRNQCIFRPHPSAPFTNRALALLFQAAdaaHGPKILVLYVPHPSDEL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 262 GAALCRHMDVDKLAFTGSTEtgkIVLELSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQgQCCCAGSRT 341
Cdd:cd07077 173 AEELLSHPKIDLIVATGGRD---AVDAAVKHSPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFDQ-NACASEQNL 248
|
250
....*....|....*
gi 1939884057 342 FVHEKVYDEFVEKAK 356
Cdd:cd07077 249 YVVDDVLDPLYEEFK 263
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
93-358 |
1.63e-08 |
|
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: 56.89 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 93 INRAVAAARKAFDEgpWPKMPAYERQKIMLRFADLVEKHNDEVAALEAWDSGKpyeqcAQVEIPMFVRLF--RY-YAGWA 169
Cdd:cd07081 1 LDDAVAAAKVAQQG--LSCKSQEMVDLIFRAAAEAAEDARIDLAKLAVSETGM-----GRVEDKVIKNHFaaEYiYNVYK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 170 DKIHGLTIPADGPHHVQTLHEPIGVAGQIIPWNFPLVMFGWKVGPALACGNSVVL----KTAEQTPLSALLVSKLFHEAG 245
Cdd:cd07081 74 DEKTCGVLTGDENGGTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFsphpRAKKVTQRAATLLLQAAVAAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 246 LPEGVLNIVSGFGPTAGAALCRHMDVDKLAFTGstetGKIVLElSAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHF 325
Cdd:cd07081 154 APENLIGWIDNPSIELAQRLMKFPGIGLLLATG----GPAVVK-AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVK 228
|
250 260 270
....*....|....*....|....*....|...
gi 1939884057 326 ALFFNQGQCCCAGSRTFVHEKVYDEFVEKAKAR 358
Cdd:cd07081 229 SKTFDNGVICASEQSVIVVDSVYDEVMRLFEGQ 261
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
190-358 |
8.54e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143440 [Multi-domain] Cd Length: 436 Bit Score: 48.26 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 190 EPIGVAGQIIPWNFPL--VMFgwKVGPALACGNSVVL----KTAEQTPLSALLVSKLFHEAGLPEGVLNIVSGfgPT--A 261
Cdd:cd07122 94 EPVGVIAALIPSTNPTstAIF--KALIALKTRNAIIFsphpRAKKCSIEAAKIMREAAVAAGAPEGLIQWIEE--PSieL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1939884057 262 GAALCRHMDVDKLAFTGSTETGKivlelSAKSNLKPVtleLG---GKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAG 338
Cdd:cd07122 170 TQELMKHPDVDLILATGGPGMVK-----AAYSSGKPA---IGvgpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASE 241
|
170 180
....*....|....*....|
gi 1939884057 339 SRTFVHEKVYDEFVEKAKAR 358
Cdd:cd07122 242 QSVIVDDEIYDEVRAELKRR 261
|
|
| |
