|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
1-500 |
0e+00 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 933.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 1 MDNLSINGDSFIKIPTIKFKKLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPG 80
Cdd:PLN02766 2 GSNGNCGGASGVKVPEIKFTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 81 AERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGV 160
Cdd:PLN02766 82 FERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 161 VGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAV 240
Cdd:PLN02766 162 VGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDKV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 241 SFTGSTETGRRVMQAAALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKK 320
Cdd:PLN02766 242 SFTGSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 321 VLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIF 400
Cdd:PLN02766 322 LVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 401 GPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEA 480
Cdd:PLN02766 402 GPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDA 481
|
490 500
....*....|....*....|
gi 357500467 481 LHKYLQVKSVATPIYNSPWL 500
Cdd:PLN02766 482 LDKYLQVKSVVTPLYNSPWL 501
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
17-492 |
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: 765.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 17 IKFKKLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATLIEQ 96
Cdd:cd07142 1 VKHTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 97 NQEEIAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFA 176
Cdd:cd07142 81 HADELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLLMFAW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 177 KAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAA 256
Cdd:cd07142 161 KVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 257 ALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDP 336
Cdd:cd07142 241 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 337 KVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGI 416
Cdd:cd07142 321 GVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357500467 417 KKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVAT 492
Cdd:cd07142 401 KRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAVVM 476
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
14-490 |
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: 752.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 14 IPTikfkKLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATL 93
Cdd:cd07091 2 QPT----GLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 94 IEQNQEEIAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIM 173
Cdd:cd07091 78 IERDRDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPIDGNFLAYTRREPIGVCGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 174 FFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVM 253
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 254 QAAALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDP 333
Cdd:cd07091 238 EAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 334 FDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIE 413
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTED 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 414 EGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07091 398 EVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
15-490 |
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: 686.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 15 PTIKFKKLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNG-PWPRMPGAERAKIMVKWATL 93
Cdd:cd07141 2 PEIKYTKIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 94 IEQNQEEIAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIM 173
Cdd:cd07141 82 IERDRAYLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMDGDFFTYTRHEPVGVCGQIIPWNFPLLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 174 FFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVM 253
Cdd:cd07141 162 AAWKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 254 QAAALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDP 333
Cdd:cd07141 242 QAAGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 334 FDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIE 413
Cdd:cd07141 322 FDPKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTID 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 414 EGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTV 478
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
17-500 |
0e+00 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 675.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 17 IKFKKLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATLIEQ 96
Cdd:PLN02466 55 VSYTQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLLEK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 97 NQEEIAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFA 176
Cdd:PLN02466 135 HNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLLMFAW 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 177 KAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAA 256
Cdd:PLN02466 215 KVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGKIVLELA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 257 ALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDP 336
Cdd:PLN02466 295 AKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 337 KVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGI 416
Cdd:PLN02466 375 GVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVI 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 417 KKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVATPIYN 496
Cdd:PLN02466 455 RRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAVVTPLKN 534
|
....
gi 357500467 497 SPWL 500
Cdd:PLN02466 535 PAWL 538
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
21-491 |
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: 637.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:COG1012 7 PLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLLEERREE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKtVDVPEAANILRYYAGAADKVHGEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAA 179
Cdd:COG1012 85 LAALLTLETGKPLAEAR-GEVDRAADFLRYYAGEARRLYGETIPSDApGTRAYVRREPLGVVGAITPWNFPLALAAWKLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 180 PCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlS 259
Cdd:COG1012 164 PALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGRRIAAAAA-E 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 260 NLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQ 339
Cdd:COG1012 243 NLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 340 QGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV-GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKK 418
Cdd:COG1012 323 MGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPdGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIAL 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 419 ANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAF-DIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVA 491
Cdd:COG1012 403 ANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGaVPQAPFGGVKQSGIGREGGREGLEEYTETKTVT 476
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
28-490 |
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: 630.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 28 FVDSvSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDngPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTI 107
Cdd:pfam00171 1 WVDS-ESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 108 DGGKLYSWCKTvDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCT 187
Cdd:pfam00171 78 ENGKPLAEARG-EVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 188 MVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLE 267
Cdd:pfam00171 157 VVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKRVTLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 268 LGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKA 347
Cdd:pfam00171 236 LGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 348 QFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLA 427
Cdd:pfam00171 316 QLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 428 AGIVTKNLDIANTVSRSIRAGIIWINCYFAFDID-CPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:pfam00171 396 AGVFTSDLERALRVARRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
34-490 |
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: 627.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 34 GKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLY 113
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 114 SWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPA 193
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPTGPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVVLKPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 194 EQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSNLKPVSLELGGKSP 273
Cdd:cd07112 161 EQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECGGKSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 274 VLIFD-DADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKI 352
Cdd:cd07112 241 NIVFAdAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAHFDKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 353 LSYIKHGKNEGATLLTGGKQV--GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGI 430
Cdd:cd07112 321 LGYIESGKAEGARLVAGGKRVltETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 431 VTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07112 401 WTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
22-490 |
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: 606.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFdNGPWPR-MPGAERAKIMVKWATLIEQNQEE 100
Cdd:cd07143 9 LFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAF-ETDWGLkVSGSKRGRCLSKLADLMERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:cd07143 88 LASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKKLTYTRHEPIGVCGQIIPWNFPLLMCAWKIAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSN 260
Cdd:cd07143 168 ALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQ 340
Cdd:cd07143 248 LKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 341 GPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKAN 420
Cdd:cd07143 328 GPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRAN 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 421 NTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07143 408 DSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAV 477
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
21-490 |
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: 602.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgPWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:cd07144 9 GLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLVEKNRDL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:cd07144 88 LAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTSPNKLAYTLHEPYGVCGQIIPWNYPLAMAAWKLAP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSN 260
Cdd:cd07144 168 ALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRLVMKAAA-QN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAK-NWVVGDPFDPKVQ 339
Cdd:cd07144 247 LKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKqNYKVGSPFDDDTV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 340 QGPQTSKAQFDKILSYIKHGKNEGATLLTGG---KQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGI 416
Cdd:cd07144 327 VGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAI 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 417 KKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07144 407 KKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAV 480
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
39-490 |
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: 569.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKT 118
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 vDVPEAANILRYYAGAADKVHGEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFPtIMFFA-KAAPCLAAGCTMVLKPAEQT 196
Cdd:cd07114 81 -QVRYLAEWYRYYAGLADKIEGAVIPVDKgDYLNFTRREPLGVVAAITPWNSP-LLLLAkKLAPALAAGNTVVLKPSEHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 197 PLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLI 276
Cdd:cd07114 159 PASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-ENLAPVTLELGGKSPNIV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 277 FDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYI 356
Cdd:cd07114 238 FDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVERYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 357 KHGKNEGATLLTGGKQVG----NKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVT 432
Cdd:cd07114 318 ARAREEGARVLTGGERPSgadlGAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWT 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 357500467 433 KNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07114 398 RDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
39-490 |
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: 564.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDngPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKT 118
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFE--AWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 VDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPL 198
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPVRGPFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 199 SSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFD 278
Cdd:cd07115 159 SALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAA-GNLKRVSLELGGKSANIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 279 DADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKH 358
Cdd:cd07115 238 DADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLDYVDV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 359 GKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIA 438
Cdd:cd07115 318 GREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 357500467 439 NTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07115 398 HRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
60-490 |
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: 554.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 60 DIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWcKTVDVPEAANILRYYAGAADKVH 139
Cdd:cd07078 1 DAAVAAARAAFKA--WAALPPAERAAILRKLADLLEERREELAALETLETGKPIEE-ALGEVARAADTFRYYAGLARRLH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 140 GEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLN 218
Cdd:cd07078 78 GEVIPSPDpGELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 219 VLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKG 298
Cdd:cd07078 158 VVTGDGDEVGAALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 299 EICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGK-QVGNKG 377
Cdd:cd07078 237 QVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKrLEGGKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 378 YYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFA 457
Cdd:cd07078 317 YFVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSV 396
|
410 420 430
....*....|....*....|....*....|....
gi 357500467 458 FDID-CPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07078 397 GAEPsAPFGGVKQSGIGREGGPYGLEEYTEPKTV 430
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
39-491 |
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: 552.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKT 118
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPG--WSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 VDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPL 198
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSEWTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 199 SSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFD 278
Cdd:cd07093 159 TAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRAAA-PNLKPVSLELGGKNPNIVFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 279 DADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKH 358
Cdd:cd07093 238 DADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGYVEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 359 GKNEGATLLTGGKQVG----NKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKN 434
Cdd:cd07093 318 ARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 435 LDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVA 491
Cdd:cd07093 398 LGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVC 454
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
23-490 |
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: 547.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATLIEQNQEEIA 102
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 103 ALDTIDGGKLYSWCKTvDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCL 182
Cdd:cd07119 81 RLETLNTGKTLRESEI-DIDDVANCFRYYAGLATKETGEVYDVPPHVISRTVREPVGVCGLITPWNYPLLQAAWKLAPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 183 AAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLK 262
Cdd:cd07119 160 AAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA-GNVK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 263 PVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGP 342
Cdd:cd07119 239 KVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 343 QTSKAQFDKILSYIKHGKNEGATLLTGGKQ-VGN---KGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKK 418
Cdd:cd07119 319 LVSAEHREKVLSYIQLGKEEGARLVCGGKRpTGDelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357500467 419 ANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07119 399 ANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
12-490 |
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: 527.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 12 IKIPTikfkKLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWA 91
Cdd:cd07140 2 LKMPH----QLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 92 TLIEQNQEEIAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVF-----KTSRNLhMYTLMEPIGVVGHIIP 166
Cdd:cd07140 78 DLMEEHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIpinqaRPNRNL-TLTKREPIGVCGIVIP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 167 WNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGST 246
Cdd:cd07140 157 WNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGST 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 247 ETGRRVMQAAALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAK 326
Cdd:cd07140 237 PIGKHIMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 327 NWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMAL 406
Cdd:cd07140 317 KMKIGDPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 407 SKFKT--IEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKY 484
Cdd:cd07140 397 SKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEY 476
|
....*.
gi 357500467 485 LQVKSV 490
Cdd:cd07140 477 LKTKTV 482
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
21-490 |
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: 516.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:cd07559 2 DNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:cd07559 80 LAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDEDTLSYHFHEPLGVVGQIIPWNFPLLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAgIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSN 260
Cdd:cd07559 160 ALAAGNTVVLKPASQTPLSILVLMELIGDL-LPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQYAA-EN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDDADVDKAVDL-----ALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFD 335
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAMDADDDFDdkaeeGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 336 PKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV----GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKT 411
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLtlggLDKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357500467 412 IEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHYQQTKNI 476
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
42-490 |
1.36e-179 |
|
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: 511.50 E-value: 1.36e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 42 PRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKTvDV 121
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARG-EI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 122 PEAANILRYYAGAADKVHGEVFKT--SRNLHMyTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLS 199
Cdd:cd07118 83 EGAADLWRYAASLARTLHGDSYNNlgDDMLGL-VLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 200 SLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDD 279
Cdd:cd07118 162 TLMLAELLIEAGLPAGVVNIVTGYGATVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQIVFAD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 280 ADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHG 359
Cdd:cd07118 241 ADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 360 KNEGATLLTGGKQV-GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIA 438
Cdd:cd07118 321 RAEGATLLLGGERLaSAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 357500467 439 NTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07118 401 LTVARRIRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
21-490 |
2.60e-178 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 509.42 E-value: 2.60e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:PRK13252 8 SLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQ--KIWAAMTAMERSRILRRAVDILRERNDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:PRK13252 86 LAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGGSFVYTRREPLGVCAGIGAWNYPIQIACWKSAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTaGAAITSHMDIDAVSFTGSTETGRRVMQAAALSn 260
Cdd:PRK13252 166 ALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTGKKVMAAAAAS- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQ 340
Cdd:PRK13252 244 LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 341 GPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGN----KGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGI 416
Cdd:PRK13252 324 GPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 417 KKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:PRK13252 404 ARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSV 477
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
22-490 |
3.63e-176 |
|
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: 503.26 E-value: 3.63e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:cd07139 1 LFIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNL-HMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:cd07139 81 ARLWTAENGMPISWSRRAQGPGPAALLRYYAALARDFPFEERRPGSGGgHVLVRREPVGVVAAIVPWNAPLFLAALKIAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGfGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSN 260
Cdd:cd07139 161 ALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCG-ER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQ 340
Cdd:cd07139 239 LARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 341 GPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVG--NKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKK 418
Cdd:cd07139 319 GPLASARQRERVEGYIAKGRAEGARLVTGGGRPAglDRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRI 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357500467 419 ANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINcYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07139 399 ANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN-GFRLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSI 469
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
39-490 |
1.84e-174 |
|
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: 498.41 E-value: 1.84e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLY---SW 115
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPR--WKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLdeaAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 116 cktvDVPEAANILRYYAGAADKVHGevfKTSRNLHM-------YTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTM 188
Cdd:cd07110 79 ----DVDDVAGCFEYYADLAEQLDA---KAERAVPLpsedfkaRVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 189 VLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLEL 268
Cdd:cd07110 152 VLKPSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSLEL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 269 GGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQ 348
Cdd:cd07110 231 GGKSPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 349 FDKILSYIKHGKNEGATLLTGGK--QVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGL 426
Cdd:cd07110 311 YEKVLSFIARGKEEGARLLCGGRrpAHLEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 427 AAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07110 391 AAAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
22-491 |
4.99e-173 |
|
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: 495.10 E-value: 4.99e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDngPWPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:cd07138 1 FYIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVH-GEVFKTSRnlhmyTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:cd07138 79 AQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEfEERRGNSL-----VVREPIGVCGLITPWNWPLNQIVLKVAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSN 260
Cdd:cd07138 154 ALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRVAEAAA-DT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQ 340
Cdd:cd07138 233 VKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 341 GPQTSKAQFDKILSYIKHGKNEGATLLTGG--KQVG-NKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIK 417
Cdd:cd07138 313 GPLASAAQFDRVQGYIQKGIEEGARLVAGGpgRPEGlERGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIA 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 418 KANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINcYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVA 491
Cdd:cd07138 393 IANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
40-491 |
5.99e-173 |
|
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: 494.26 E-value: 5.99e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFDngPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKtV 119
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEAR-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 120 DVPEAANILRYYAGAADKVHGEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPL 198
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIPSPApGKRILVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 199 SSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFD 278
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFIVFD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 279 DADVdkavDLALFGILHNK----GEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILS 354
Cdd:cd07103 238 DADL----DKAVDGAIASKfrnaGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 355 YIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKN 434
Cdd:cd07103 314 LVEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRD 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 435 LDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVA 491
Cdd:cd07103 394 LARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVS 450
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
40-491 |
9.75e-173 |
|
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: 494.06 E-value: 9.75e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFDnGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKTv 119
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFE-SGWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 120 DVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLS 199
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPGYFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 200 SLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDD 279
Cdd:cd07109 160 ALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQIVFAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 280 ADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPF-DPKVqqGPQTSKAQFDKILSYIKH 358
Cdd:cd07109 239 ADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLeDPDL--GPLISAKQLDRVEGFVAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 359 GKNEGATLLTGGKQVGN---KGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNL 435
Cdd:cd07109 317 ARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 436 DIANTVSRSIRAGIIWINCYFAF-DIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVA 491
Cdd:cd07109 397 DRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKGLEALYNYTQTKTVA 453
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
12-499 |
3.99e-170 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 489.24 E-value: 3.99e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 12 IKIPTikfKKLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAF---DNGPWPRMPGAERAKIMV 88
Cdd:PLN02467 3 IPVPR---RQLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 89 KWATLIEQNQEEIAALDTIDGGKLY---SWcktvDVPEAANILRYYAGAADKVHG----------EVFKTsrnlhmYTLM 155
Cdd:PLN02467 80 AIAAKITERKSELAKLETLDCGKPLdeaAW----DMDDVAGCFEYYADLAEALDAkqkapvslpmETFKG------YVLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 156 EPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHM 235
Cdd:PLN02467 150 EPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 236 DIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYD 315
Cdd:PLN02467 230 GVDKIAFTGSTATGRKIMTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIAS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 316 EFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGK--QVGNKGYYIEPTIFTNVKDDML 393
Cdd:PLN02467 309 EFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 394 IAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYG 473
Cdd:PLN02467 389 IWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFG 468
|
490 500
....*....|....*....|....*.
gi 357500467 474 RDYGLEALHKYLQVKSVATPIYNSPW 499
Cdd:PLN02467 469 RELGEWGLENYLSVKQVTKYISDEPW 494
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
39-490 |
1.55e-169 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 486.04 E-value: 1.55e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSwCKT 118
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKE--WSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIE-EAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 VDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPL 198
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 199 SSLFFAHLAKEAGIPDGVLNVLPGFGSTaGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFD 278
Cdd:cd07090 158 TALLLAEILTEAGLPDGVFNVVQGGGET-GQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPLIIFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 279 DADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKH 358
Cdd:cd07090 236 DADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 359 GKNEGATLLTGG--KQVGNK---GYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTK 433
Cdd:cd07090 316 AKQEGAKVLCGGerVVPEDGlenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTR 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 434 NLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07090 396 DLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTV 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
40-491 |
2.90e-167 |
|
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: 480.20 E-value: 2.90e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWpRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKTV 119
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 120 DVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLM-----EPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAE 194
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEFDLPVPALRGGPGRrvvrrEPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 195 QTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPV 274
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 275 LIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILS 354
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 355 YIKHGKNEGATLLTGGKQV--GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVT 432
Cdd:cd07089 320 YIARGRDEGARLVTGGGRPagLDKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 357500467 433 KNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVA 491
Cdd:cd07089 400 ADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIA 458
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
23-488 |
1.56e-163 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 471.22 E-value: 1.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEEIA 102
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 103 ALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCL 182
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPLGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 183 AAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLK 262
Cdd:TIGR01804 159 AAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAAAA-GHLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 263 PVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGP 342
Cdd:TIGR01804 238 HVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEATEMGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 343 QTSKAQFDKILSYIKHGKNEGATLLTGGKQVGN----KGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKK 418
Cdd:TIGR01804 318 LISAAHRDKVLSYIEKGKAEGATLATGGGRPENvglqNGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIAR 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 419 ANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVK 488
Cdd:TIGR01804 398 ANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
21-490 |
3.37e-160 |
|
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: 463.08 E-value: 3.37e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:cd07117 2 GLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:cd07117 80 LAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDEDTLSIVLREPIGVVGQIIPWNFPFLMAAWKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAgIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSN 260
Cdd:cd07117 160 ALAAGNTVVIKPSSTTSLSLLELAKIIQDV-LPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIAAA-KK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQ 340
Cdd:cd07117 238 LIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 341 GPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVG----NKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGI 416
Cdd:cd07117 318 GAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTenglDKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 417 KKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07117 398 DMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKNI 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
21-490 |
1.81e-158 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 458.60 E-value: 1.81e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSvSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:PRK13473 4 KLLINGELVAG-EGEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFPE--WSQTTPKERAEALLKLADAIEENADE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVfkTSRNLHMYTLM---EPIGVVGHIIPWNFPTIMFFAK 177
Cdd:PRK13473 81 FARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGKA--AGEYLEGHTSMirrDPVGVVASIAPWNYPLMMAAWK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 178 AAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAgIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAA 257
Cdd:PRK13473 159 LAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSLTGSIATGKHVLSAAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 258 lSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPK 337
Cdd:PRK13473 238 -DSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDED 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 338 VQQGPQTSKAQFDKILSYIKHGKNEG-ATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGI 416
Cdd:PRK13473 317 TELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 417 KKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:PRK13473 397 RWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
40-492 |
8.37e-155 |
|
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: 448.31 E-value: 8.37e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKTV 119
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 120 DVPEAANILRYYAGAADKVHGEVfkTSRNLHMYTLM---EPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQT 196
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPA--AGEYLPGHTSMirrEPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 197 PLSSLFFAHLAKEaGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLI 276
Cdd:cd07092 158 PLTTLLLAELAAE-VLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARAAA-DTLKRVHLELGGKAPVIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 277 FDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYI 356
Cdd:cd07092 236 FDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 357 KHGKnEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLD 436
Cdd:cd07092 316 ERAP-AHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVG 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 357500467 437 IANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVAT 492
Cdd:cd07092 395 RAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
21-490 |
9.14e-155 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 449.73 E-value: 9.14e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:PRK09847 21 RLFINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:PRK09847 101 LALLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSN 260
Cdd:PRK09847 181 ALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDD-ADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQ 339
Cdd:PRK09847 261 MKRVWLEAGGKSANIVFADcPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 340 QGPQTSKAQFDKILSYIKHGKNEGaTLLTGGKQVGNKGyYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKA 419
Cdd:PRK09847 341 MGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLA 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357500467 420 NNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:PRK09847 419 NDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTI 489
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
23-490 |
2.56e-152 |
|
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: 442.84 E-value: 2.56e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSVSGKtfETVDP-RTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPsDTSDVVGKYARASAEDADAAIAAAAAAFPA--WRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKlyswckTV-----DVPEAANILRYYAGAADKVHGEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFPTIMFF 175
Cdd:cd07097 80 ARLLTREEGK------TLpeargEVTRAGQIFRYYAGEALRLSGETLPSTRpGVEVETTREPLGVVGLITPWNFPIAIPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 176 AKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVmQA 255
Cdd:cd07097 154 WKIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRI-AA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 256 AALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFD 335
Cdd:cd07097 233 AAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 336 PKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV--GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIE 413
Cdd:cd07097 313 EGVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLkrPDEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYD 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357500467 414 EGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFA-FDIDCPFGGYKMSGYG-RDYGLEALHKYLQVKSV 490
Cdd:cd07097 393 EALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNLPTAgVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
23-490 |
8.84e-151 |
|
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: 438.62 E-value: 8.84e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIA 102
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKA--WERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 103 ALDTIDGGKLYSWCKtVDVPEAANILRYYAGAADKVHGEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPC 181
Cdd:cd07088 79 KLIVEEQGKTLSLAR-VEVEFTADYIDYMAEWARRIEGEIIPSDRpNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 182 LAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNL 261
Cdd:cd07088 158 LVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAA-ENI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 262 KPVSLELGGKSPVLIFddadVDKAVDLALFGILH----NKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPK 337
Cdd:cd07088 237 TKVSLELGGKAPAIVM----KDADLDLAVKAIVDsriiNCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 338 VQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV-GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGI 416
Cdd:cd07088 313 TDMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPeGEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAI 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357500467 417 KKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCyFAFDIDCPF-GGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07088 393 ELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINR-ENFEAMQGFhAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
22-485 |
1.85e-146 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 428.35 E-value: 1.85e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:cd07111 24 HFINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEvfktsrnLHMYtlmEPIGVVGHIIPWNFPTIMFFAKAAPC 181
Cdd:cd07111 102 AVLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLDTE-------LAGW---KPVGVVGQIVPWNFPLLMLAWKICPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 182 LAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTaGAAITSHMDIDAVSFTGSTETGRRVMQAAALSNl 261
Cdd:cd07111 172 LAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGSF-GSALANHPGVDKVAFTGSTEVGRALRRATAGTG- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 262 KPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQG 341
Cdd:cd07111 250 KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 342 PQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANN 421
Cdd:cd07111 330 AIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANN 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 422 TKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYL 485
Cdd:cd07111 410 TPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
64-490 |
9.05e-146 |
|
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: 422.02 E-value: 9.05e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 64 KAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYsWCKTVDVPEAANILRYYAGAADKVHGEVF 143
Cdd:cd06534 1 AAARAAFKA--WAALPPAERAAILRKIADLLEERREELAALETLETGKPI-EEALGEVARAIDTFRYAAGLADKLGGPEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 144 K-TSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPG 222
Cdd:cd06534 78 PsPDPGGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 223 FGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICV 302
Cdd:cd06534 158 GGDEVGAALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 303 AYSRVFVQEGIYDEFEKKVLekaknwvvgdpfdpkvqqgpqtskaqfdkilsyikhgknegatlltggkqvgnkgyyiep 382
Cdd:cd06534 237 AASRLLVHESIYDEFVEKLV------------------------------------------------------------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 383 TIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDID- 461
Cdd:cd06534 257 TVLVDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGPe 336
|
410 420
....*....|....*....|....*....
gi 357500467 462 CPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd06534 337 APFGGVKNSGIGREGGPYGLEEYTRTKTV 365
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
23-490 |
1.76e-145 |
|
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: 425.61 E-value: 1.76e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSVSGKTFETVDP-RTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPaDLEEVVGTFPLSTASDVDAAVEAAREAFPE--WRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKLYSWCKTvDVPEAANILRYYAGAADKVHGEVFKTS-RNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:cd07131 80 ARLVTREMGKPLAEGRG-DVQEAIDMAQYAAGEGRRLFGETVPSElPNKDAMTRRQPIGVVALITPWNFPVAIPSWKIFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSN 260
Cdd:cd07131 159 ALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCARPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 lKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQ 340
Cdd:cd07131 239 -KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 341 GPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV----GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGI 416
Cdd:cd07131 318 GPLINEAQLEKVLNYNEIGKEEGATLLLGGERLtgggYEKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 417 KKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN--CYFAfDIDCPFGGYKMSGYG-RDYGLEALHKYLQVKSV 490
Cdd:cd07131 398 EIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVNapTIGA-EVHLPFGGVKKSGNGhREAGTTALDAFTEWKAV 473
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
40-490 |
8.25e-144 |
|
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: 420.01 E-value: 8.25e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKlYSWCKTV 119
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPG--WSATPLEERRAALLAIADAIEANAEELARLLTLEQGK-PLAEAQF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 120 DVPEAANILRYYAGAADKVhgEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLS 199
Cdd:cd07106 79 EVGGAVAWLRYTASLDLPD--EVIEDDDTRRVELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 200 SLFFAHLAKEAgIPDGVLNVLPGfGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDD 279
Cdd:cd07106 157 TLKLGELAQEV-LPPGVLNVVSG-GDELGPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 280 ADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHG 359
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 360 KNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIAN 439
Cdd:cd07106 314 KAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 357500467 440 TVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07106 394 AVARRLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
39-490 |
1.74e-143 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 419.86 E-value: 1.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSwcKT 118
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPE--WRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS--AM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 V-DVPEAANILRYYAGAADKVHGEVFKTS-RNLHmYTLMEPIGVVGHIIPWNFPtIMFFA-KAAPCLAAGCTMVLKPAEQ 195
Cdd:cd07107 77 LgDVMVAAALLDYFAGLVTELKGETIPVGgRNLH-YTLREPYGVVARIVAFNHP-LMFAAaKIAAPLAAGNTVVVKPPEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 196 TPLSSLFFAHLAKEAgIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVL 275
Cdd:cd07107 155 APLSALRLAELAREV-LPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRAAA-EGIKHVTLELGGKNALI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 276 IFDDADVDKAVDLALFGI-LHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILS 354
Cdd:cd07107 233 VFPDADPEAAADAAVAGMnFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVMH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 355 YIKHGKNEGATLLTGGKQ----VGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGI 430
Cdd:cd07107 313 YIDSAKREGARLVTGGGRpegpALEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAI 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 431 VTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07107 393 WTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNV 452
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
23-490 |
5.40e-142 |
|
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: 416.85 E-value: 5.40e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIA 102
Cdd:cd07116 4 FIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKEA--WGKTSVAERANILNKIADRMEANLEMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 103 ALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCL 182
Cdd:cd07116 82 VAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEIDENTVAYHFHEPLGVVGQIIPWNFPLLMATWKLAPAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 183 AAGCTMVLKPAEQTPLSSLFFAHLAKEAgIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLK 262
Cdd:cd07116 162 AAGNCVVLKPAEQTPASILVLMELIGDL-LPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQYAS-ENII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 263 PVSLELGGKSPVLIFDDADVDKAVDL-------ALFGIlhNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFD 335
Cdd:cd07116 240 PVTLELGGKSPNIFFADVMDADDAFFdkalegfVMFAL--NQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 336 PKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQ-----VGNKGYYIEPTIFTNvkDDMLIAQDEIFGPVMALSKFK 410
Cdd:cd07116 318 TETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERnelggLLGGGYYVPTTFKGG--NKMRIFQEEIFGPVLAVTTFK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 411 TIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07116 396 DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNL 475
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
22-490 |
9.15e-141 |
|
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: 413.38 E-value: 9.15e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDnGPWPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:cd07113 2 HFIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKLYSWCKTVDVPEAANILRYYAGAADKVHGEVFKTS---RNLHMY---TLMEPIGVVGHIIPWNFPTIMFF 175
Cdd:cd07113 81 AQLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSipsMQGERYtafTRREPVGVVAGIVPWNFSVMIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 176 AKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTaGAAITSHMDIDAVSFTGSTETGRRVmQA 255
Cdd:cd07113 161 WKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKI-GR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 256 AALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFD 335
Cdd:cd07113 239 QAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 336 PKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEG 415
Cdd:cd07113 319 ESVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEEL 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357500467 416 IKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07113 399 IQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSV 473
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
23-490 |
7.71e-139 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 409.47 E-value: 7.71e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDngPWPRMPGAERAKIMVKWATLIEQNQEEIA 102
Cdd:PLN02278 28 LIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKEDLA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 103 ALDTIDGGKlySWCKTV-DVPEAANILRYYAGAADKVHGEVFKT-SRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAP 180
Cdd:PLN02278 106 QLMTLEQGK--PLKEAIgEVAYGASFLEYFAEEAKRVYGDIIPSpFPDRRLLVLKQPVGVVGAITPWNFPLAMITRKVGP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 181 CLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSN 260
Cdd:PLN02278 184 ALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAGAA-AT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 261 LKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQ 340
Cdd:PLN02278 263 VKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 341 GPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKAN 420
Cdd:PLN02278 343 GPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIAN 422
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 421 NTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:PLN02278 423 DTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYV 492
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
39-490 |
2.69e-136 |
|
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: 401.35 E-value: 2.69e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYswcKT 118
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGNAL---RT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 VDVPEA---ANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQ 195
Cdd:cd07108 76 QARPEAavlADLFRYFGGLAGELKGETLPFGPDVLTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 196 TPLSSLFFAHLAKEAgIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVL 275
Cdd:cd07108 156 APLAVLLLAEILAQV-LPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRAAA-DRLIPVSLELGGKSPMI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 276 IFDDADVDKAVDLALFGI-LHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILS 354
Cdd:cd07108 234 VFPDADLDDAVDGAIAGMrFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEKQFAKVCG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 355 YIKHGKNE-GATLLTGGKQ----VGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAG 429
Cdd:cd07108 314 YIDLGLSTsGATVLRGGPLpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAY 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357500467 430 IVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEA-LHKYLQVKSV 490
Cdd:cd07108 394 VWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGmLEHFTQKKTV 455
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
39-490 |
1.84e-128 |
|
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: 381.31 E-value: 1.84e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPWPRMPgAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKt 118
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDWAHDP-RLRARVLLELADAFEANAERLARLLALENGKILGEAR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 VDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPL 198
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMIEPEPGSFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 199 -SSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIF 277
Cdd:cd07120 159 iNAAIIRILAEIPSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTPCIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 278 DDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIK 357
Cdd:cd07120 238 DDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVDRMVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 358 HGKNEGAT-LLTGGKQVG--NKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKN 434
Cdd:cd07120 318 RAIAAGAEvVLRGGPVTEglAKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRD 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 357500467 435 LDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07120 398 LARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHI 453
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
58-488 |
7.77e-128 |
|
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: 378.80 E-value: 7.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 58 DVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSwcK-TVDVPEAANILRYYAGAAD 136
Cdd:cd07104 1 DVDRAYAAAAAAQ--KAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRP--KaAFEVGAAIAILREAAGLPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 137 KVHGEVFKTSRNLHM-YTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSS-LFFAHLAKEAGIPD 214
Cdd:cd07104 77 RPEGEILPSDVPGKEsMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGgLLIAEIFEEAGLPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 215 GVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGI- 293
Cdd:cd07104 157 GVLNVVPGGGSEIGDALVEHPRVRMISFTGSTAVGRHIGELAG-RHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAf 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 294 LHNkGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV 373
Cdd:cd07104 236 LHQ-GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGGTYE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 374 GNkgyYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN 453
Cdd:cd07104 315 GL---FYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIN 391
|
410 420 430
....*....|....*....|....*....|....*.
gi 357500467 454 CYFAFD-IDCPFGGYKMSGYGRDYGLEALHKYLQVK 488
Cdd:cd07104 392 DQTVNDePHVPFGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
22-491 |
3.91e-125 |
|
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: 374.64 E-value: 3.91e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSvsGKTFETVDP-RTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:cd07124 35 LVIGGKEVRT--EEKIESRNPaDPSEVLGTVQKATKEEAEAAVQAARAAFPT--WRRTPPEERARLLLRAAALLRRRRFE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKlySWCKTV-DVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAA 179
Cdd:cd07124 111 LAAWMVLEVGK--NWAEADaDVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPLAILAGMTT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 180 PCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAA-- 257
Cdd:cd07124 189 AALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYERAAkv 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 258 ---LSNLKPVSLELGGKSPVLIfddaDVDKAVDLALFGILHN----KGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVV 330
Cdd:cd07124 269 qpgQKWLKRVIAEMGGKNAIIV----DEDADLDEAAEGIVRSafgfQGQKCSACSRVIVHESVYDEFLERLVERTKALKV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 331 GDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGaTLLTGGK--QVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSK 408
Cdd:cd07124 345 GDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 409 FKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN--CYFAFDIDCPFGGYKMSGY-----GRDYgleaL 481
Cdd:cd07124 424 AKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANrkITGALVGRQPFGGFKMSGTgskagGPDY----L 499
|
490
....*....|
gi 357500467 482 HKYLQVKSVA 491
Cdd:cd07124 500 LQFMQPKTVT 509
|
|
| SSADH |
TIGR01780 |
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three ... |
40-488 |
5.06e-125 |
|
succinate-semialdehyde dehydrogenase; Succinic semialdehyde dehydrogenase is one of three enzymes constituting 4-aminobutyrate (GABA) degradation in both prokaryotes and eukaryotes, catalyzing the (NAD(P)+)-dependent catabolism reaction of succinic semialdehyde to succinate for metabolism by the citric acid cycle. The EC number depends on the cofactor: 1.2.1.24 for NAD only, 1.2.1.79 for NADP only, and 1.2.1.16 if both can be used. In Escherichia coli, succinic semialdehyde dehydrogenase is located in an unidirectionally transcribed gene cluster encoding enzymes for GABA degradation and is suggested to be cotranscribed with succinic semialdehyde transaminase from a common promoter upstream of SSADH. Similar gene arrangements can be found in characterized Ralstonia eutropha and the genome analysis of Bacillus subtilis. Prokaryotic succinic semialdehyde dehydrogenases (1.2.1.16) share high sequence homology to characterized succinic semialdehyde dehydrogenases from rat and human (1.2.1.24), exhibiting conservation of proposed cofactor binding residues, and putative active sites (G-237 _ G-242, C-293 _ G-259 respectively of rat SSADH). Eukaryotic SSADH enzymes exclusively utilize NAD+ as a cofactor, exhibiting little to no NADP+ activity. While a NADP+ preference has been detected in prokaryotes in addition to both NADP+- and NAD+-dependencies as in E.coli, Pseudomonas, and Klebsiella pneumoniae. The function of this alternative SSADH currently is unknown, but has been suggested to play a possible role in 4-hydroxyphenylacetic degradation. Just outside the scope of this model, are several sequences belonging to clades scoring between trusted and noise. These sequences may be actual SSADH enzymes, but lack sufficiently close characterized homologs to make a definitive assignment at this time. SSADH enzyme belongs to the aldehyde dehydrogenase family (pfam00171), sharing a common evolutionary origin and enzymatic mechanism with lactaldehyde dehydrogenase. Like in lactaldehyde dehydrogenase and succinate semialdehyde dehydrogenase, the mammalian catalytic glutamic acid and cysteine residues are conserved in all the enzymes of this family (PS00687, PS00070). [Central intermediary metabolism, Other]
Pssm-ID: 188167 Cd Length: 448 Bit Score: 372.15 E-value: 5.06e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKTv 119
Cdd:TIGR01780 2 YNPATGEIIGSVPDQGVDETEAAIRAAYEAFKT--WRATTAKERSSLLRKWYNLMMENKDDLARLITLENGKPLKEAKG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 120 DVPEAANILRYYAGAADKVHGEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPL 198
Cdd:TIGR01780 79 EILYAASFLEWFAEEAKRVYGDTIPSPQsDKRLIVIKQPVGVCAAITPWNFPAAMITRKAGAALAAGCTVVVKPAEQTPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 199 SSLFFAHLAKEAGIPDGVLNVLPG-FGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIF 277
Cdd:TIGR01780 159 SALALARLAEQAGIPKGVLNVITGsRAKEVGNVLTTSPLVRKISFTGSTNVGKILMKQSA-STVKKVSMELGGNAPFIVF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 278 DDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIK 357
Cdd:TIGR01780 238 DDADLDQAVEGAMASKFRNAGQTCVCANRLYVHDGIYDEFAKKLAEAVKKLKVGNGLDEGVTQGPLINEKAVEKVEKHIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 358 HGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDI 437
Cdd:TIGR01780 318 DAVEKGAKVVTGGKRHELGGNFFEPTVLSNVTADMLVSKEETFGPLAPVFKFDDEEEVIAIANDTEVGLAAYFFSRDLSR 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 357500467 438 ANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVK 488
Cdd:TIGR01780 398 IWRVAEALEYGMVGINTGLISNVVAPFGGVKQSGLGREGSKYGIEEYLETK 448
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
37-491 |
3.10e-124 |
|
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: 370.51 E-value: 3.10e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 37 FETVDPRTEEVITKIAEATKDDVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLY--S 114
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAF--PAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYgkA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 115 WCKTVDVPeaaNILRYYAGAADKVHGEVFKTSRNLHM-YTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPA 193
Cdd:cd07150 79 WFETTFTP---ELLRAAAGECRRVRGETLPSDSPGTVsMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 194 EQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSP 273
Cdd:cd07150 156 EETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAG-RHLKKITLELGGKNP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 274 VLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKIL 353
Cdd:cd07150 235 LIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 354 SYIKHGKNEGATLLTGGKQVGNkgyYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTK 433
Cdd:cd07150 315 RQVEDAVAKGAKLLTGGKYDGN---FYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTN 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 357500467 434 NLDIANTVSRSIRAGIIWINCYFAFD-IDCPFGGYKMSGYGRDYGLEALHKYLQVKSVA 491
Cdd:cd07150 392 DLQRAFKLAERLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWIT 450
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
37-474 |
7.19e-124 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 369.62 E-value: 7.19e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 37 FETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNGPwpRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWC 116
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMK--SLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 117 KtVDVPEAANILRYYAGAADKVHGEVF-----KTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLK 191
Cdd:cd07149 79 R-KEVDRAIETLRLSAEEAKRLAGETIpfdasPGGEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 192 PAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALsnlKPVSLELGGK 271
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARKAGL---KKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 272 SPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDK 351
Cdd:cd07149 235 AAVIVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 352 ILSYIKHGKNEGATLLTGGKQVGNkgyYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIV 431
Cdd:cd07149 315 IEEWVEEAVEGGARLLTGGKRDGA---ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVF 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 357500467 432 TKNLDIANTVSRSIRAGIIWINCYFAFDID-CPFGGYKMSGYGR 474
Cdd:cd07149 392 TNDLQKALKAARELEVGGVMINDSSTFRVDhMPYGGVKESGTGR 435
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
40-492 |
1.72e-118 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 355.76 E-value: 1.72e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSwCKTV 119
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQ--RAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRA-DAGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 120 DVPEAANILRYYAGAADKV-------HGEVFKTSRNLHMYtlmEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKP 192
Cdd:cd07099 78 EVLLALEAIDWAARNAPRVlaprkvpTGLLMPNKKATVEY---RPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 193 AEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTaGAAITSHMdIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKS 272
Cdd:cd07099 155 SEVTPLVGELLAEAWAAAGPPQGVLQVVTGDGAT-GAALIDAG-VDKVAFTGSVATGRKVMAAAA-ERLIPVVLELGGKD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 273 PVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKI 352
Cdd:cd07099 232 PMIVLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 353 LSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVT 432
Cdd:cd07099 312 RRHVDDAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFS 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357500467 433 KNLDIANTVSRSIRAGIIWINC--YFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVAT 492
Cdd:cd07099 392 RDLARAEAIARRLEAGAVSINDvlLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
23-484 |
3.07e-118 |
|
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: 355.72 E-value: 3.07e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSvSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIA 102
Cdd:cd07086 2 VIGGEWVGS-GGETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKE--WRKVPAPRRGEIVRQIGEALRKKKEALG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 103 ALDTIDGGKLYSWCKTvDVPEAANILRYYAGAADKVHGEVFKTSRNLH-MYTLMEPIGVVGHIIPWNFPTIMFFAKAAPC 181
Cdd:cd07086 79 RLVSLEMGKILPEGLG-EVQEMIDICDYAVGLSRMLYGLTIPSERPGHrLMEQWNPLGVVGVITAFNFPVAVPGWNAAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 182 LAAGCTMVLKPAEQTPLSSL----FFAHLAKEAGIPDGVLNVLPGFGsTAGAAITSHMDIDAVSFTGSTETGRRVMQAAA 257
Cdd:cd07086 158 LVCGNTVVWKPSETTPLTAIavtkILAEVLEKNGLPPGVVNLVTGGG-DGGELLVHDPRVPLVSFTGSTEVGRRVGETVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 258 lSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPK 337
Cdd:cd07086 237 -RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 338 VQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV--GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEG 415
Cdd:cd07086 316 TLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIdgGEPGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEA 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357500467 416 IKKANNTKYGLAAGIVTKNLDIANtvsRSIR-----AGIIWIN--CYFAfDIDCPFGGYKMSGYGRDYGLEALHKY 484
Cdd:cd07086 396 IAINNDVPQGLSSSIFTEDLREAF---RWLGpkgsdCGIVNVNipTSGA-EIGGAFGGEKETGGGRESGSDAWKQY 467
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
37-475 |
5.17e-113 |
|
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: 341.64 E-value: 5.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 37 FETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWC 116
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 117 KtVDVPEAANILRYYAGAADKVHGEVFKT-----SRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLK 191
Cdd:cd07145 79 R-VEVERTIRLFKLAAEEAKVLRGETIPVdayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 192 PAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGK 271
Cdd:cd07145 158 PSSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASKAG-GTGKKVALELGGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 272 SPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDK 351
Cdd:cd07145 237 DPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVER 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 352 ILSYIKHGKNEGATLLTGGKqvGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIV 431
Cdd:cd07145 317 MENLVNDAVEKGGKILYGGK--RDEGSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVF 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 357500467 432 TKNLDIANTVSRSIRAGIIWINCYFAFDID-CPFGGYKMSGYGRD 475
Cdd:cd07145 395 TNDINRALKVARELEAGGVVINDSTRFRWDnLPFGGFKKSGIGRE 439
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
26-490 |
3.76e-112 |
|
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: 339.67 E-value: 3.76e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 26 GGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAfdNGPWPRMPGAERAKIMVKWATLIEQNQEEIAALD 105
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 106 TIDGGKLYSwcK-TVDVPEAANILRYYAGAADKVHGEVF------KTSRnlhMYTlmEPIGVVGHIIPWNFPTIMFFAKA 178
Cdd:cd07151 79 IRESGSTRI--KaNIEWGAAMAITREAATFPLRMEGRILpsdvpgKENR---VYR--EPLGVVGVISPWNFPLHLSMRSV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 179 APCLAAGCTMVLKPAEQTPLSS-LFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAA 257
Cdd:cd07151 152 APALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 258 lSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPK 337
Cdd:cd07151 232 -RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 338 VQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNkgyYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIK 417
Cdd:cd07151 311 TVVGPLINESQVDGLLDKIEQAVEEGATLLVGGEAEGN---VLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357500467 418 KANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINcyfafDI------DCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07151 388 LANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHIN-----DQpvndepHVPFGGEKNSGLGRFNGEWALEEFTTDKWI 461
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
21-490 |
4.15e-110 |
|
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: 334.87 E-value: 4.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:cd07085 2 KLFINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFPA--WSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCK-----TVDVPEAAnilryyAGAADKVHGE-VFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMF 174
Cdd:cd07085 80 LARLITLEHGKTLADARgdvlrGLEVVEFA------CSIPHLLKGEyLENVARGIDTYSYRQPLGVVAGITPFNFPAMIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 175 FAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGfGSTAGAAITSHMDIDAVSFTGSTETGRRVMQ 254
Cdd:cd07085 154 LWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 255 AAAlSNLKPVSLELGGKSPVLIF---DDADVDKAVDLALFGilhNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVG 331
Cdd:cd07085 233 RAA-ANGKRVQALGGAKNHAVVMpdaDLEQTANALVGAAFG---AAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 332 DPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV----GNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALS 407
Cdd:cd07085 309 AGDDPGADMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVkvpgYENGNFVGPTILDNVTPDMKIYKEEIFGPVLSIV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 408 KFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINC-------YFafdidcPFGGYKMSGYGrD---YG 477
Cdd:cd07085 389 RVDTLDEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGINVpipvplaFF------SFGGWKGSFFG-DlhfYG 461
|
490
....*....|...
gi 357500467 478 LEALHKYLQVKSV 490
Cdd:cd07085 462 KDGVRFYTQTKTV 474
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
59-490 |
1.77e-109 |
|
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: 331.73 E-value: 1.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 59 VDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKTvDVPEAANILRYYA-GAADK 137
Cdd:cd07100 1 IEAALDRAHAAFLA--WRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARA-EVEKCAWICRYYAeNAEAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 138 VHGEVFKTSrNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVL 217
Cdd:cd07100 78 LADEPIETD-AGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 218 NVLPGFGSTAGAAItSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNK 297
Cdd:cd07100 157 QNLLIDSDQVEAII-ADPRVRGVTLTGSERAGRAVAAEAG-KNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 298 GEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKG 377
Cdd:cd07100 235 GQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 378 YYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFA 457
Cdd:cd07100 315 AFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVK 394
|
410 420 430
....*....|....*....|....*....|...
gi 357500467 458 FDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07100 395 SDPRLPFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
22-491 |
2.51e-109 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 334.21 E-value: 2.51e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSvsGKTFETVDP-RTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:PRK03137 39 LIIGGERITT--EDKIVSINPaNKSEVVGRVSKATKELAEKAMQAALEAFET--WKKWSPEDRARILLRAAAIIRRRKHE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKlySWCKT-VDVPEAANILRYYAGAADKVHGEVFKTSR----NLHMYtlmEPIGVVGHIIPWNFPT-IMF 174
Cdd:PRK03137 115 FSAWLVKEAGK--PWAEAdADTAEAIDFLEYYARQMLKLADGKPVESRpgehNRYFY---IPLGVGVVISPWNFPFaIMA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 175 FAKAAPcLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQ 254
Cdd:PRK03137 190 GMTLAA-IVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRIYE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 255 AAALSN-----LKPVSLELGGKSPVLIfddaDVDKAVDLALFGILHN----KGEICVAYSRVFVQEGIYDEFEKKVLEKA 325
Cdd:PRK03137 269 RAAKVQpgqiwLKRVIAEMGGKDAIVV----DEDADLDLAAESIVASafgfSGQKCSACSRAIVHEDVYDEVLEKVVELT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 326 KNWVVGDPFDPKVqQGPQTSKAQFDKILSYIKHGKNEGaTLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMA 405
Cdd:PRK03137 345 KELTVGNPEDNAY-MGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVA 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 406 LSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN--CYFAFDIDCPFGGYKMSGY-----GRDYgl 478
Cdd:PRK03137 423 FIKAKDFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVGNLYFNrgCTGAIVGYHPFGGFNMSGTdskagGPDY-- 500
|
490
....*....|...
gi 357500467 479 eaLHKYLQVKSVA 491
Cdd:PRK03137 501 --LLLFLQAKTVS 511
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
29-500 |
5.62e-109 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 333.77 E-value: 5.62e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 29 VDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAfdNGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTID 108
Cdd:PRK09407 26 VDGAAGPTREVTAPFTGEPLATVPVSTAADVEAAFARARAA--QRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 109 GGK--LYSWCKTVDVPEAAnilRYYAGAADKVHGE--------VFKTSRNLHmytlmEPIGVVGHIIPWNFPTIMFFAKA 178
Cdd:PRK09407 104 TGKarRHAFEEVLDVALTA---RYYARRAPKLLAPrrragalpVLTKTTELR-----QPKGVVGVISPWNYPLTLAVSDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 179 APCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHmdIDAVSFTGSTETGRRVMQAAAl 258
Cdd:PRK09407 176 IPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVTGPGPVVGTALVDN--ADYLMFTGSTATGRVLAEQAG- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 259 SNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKV 338
Cdd:PRK09407 253 RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 339 QQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKG-YYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIK 417
Cdd:PRK09407 333 DMGSLISEAQLETVSAHVDDAVAKGATVLAGGKARPDLGpLFYEPTVLTGVTPDMELAREETFGPVVSVYPVADVDEAVE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 418 KANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAF---DIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVAT-- 492
Cdd:PRK09407 413 RANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAAawgSVDAPMGGMKDSGLGRRHGAEGLLKYTESQTIATqr 492
|
490
....*....|
gi 357500467 493 --PIYNSPWL 500
Cdd:PRK09407 493 vlPLAPPPGM 502
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
41-492 |
9.00e-108 |
|
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: 328.11 E-value: 9.00e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 41 DPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGK--LYSWCKT 118
Cdd:cd07101 2 APFTGEPLGELPQSTPADVEAAFARARAAQRA--WAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKarRHAFEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 VDVpeaANILRYYAGAADKV------HGEVFKTSRNLHMYTlmePIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKP 192
Cdd:cd07101 80 LDV---AIVARYYARRAERLlkprrrRGAIPVLTRTTVNRR---PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 193 AEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIdaVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKS 272
Cdd:cd07101 154 DSQTALTALWAVELLIEAGLPRDLWQVVTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGGKN 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 273 PVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKI 352
Cdd:cd07101 231 PMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 353 LSYIKHGKNEGATLLTGGKQVGNKG-YYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIV 431
Cdd:cd07101 311 TAHVDDAVAKGATVLAGGRARPDLGpYFYEPTVLTGVTEDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVW 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357500467 432 TKNLDIANTVSRSIRAGIIWINCYFAF---DIDCPFGGYKMSGYGRDYGLEALHKYLQVKSVAT 492
Cdd:cd07101 391 TRDGARGRRIAARLRAGTVNVNEGYAAawaSIDAPMGGMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
46-477 |
3.96e-106 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 323.48 E-value: 3.96e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 46 EVITKIAEATKDDVDIAVKAAREAfdNGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSwcKT-VDVPEA 124
Cdd:cd07152 2 AVLGEVGVADAADVDRAAARAAAA--QRAWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRP--KAgFEVGAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 125 ANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSS-LFF 203
Cdd:cd07152 78 IGELHEAAGLPTQPQGEILPSAPGRLSLARRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgVVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 204 AHLAKEAGIPDGVLNVLPGfGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVD 283
Cdd:cd07152 158 ARLFEEAGLPAGVLHVLPG-GADAGEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVLDDADLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 284 KAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEG 363
Cdd:cd07152 236 LAASNGAWGAFLHQGQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 364 ATLLTGGKQvgnKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSR 443
Cdd:cd07152 316 ARLEAGGTY---DGLFYRPTVLSGVKPGMPAFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALAD 392
|
410 420 430
....*....|....*....|....*....|....*.
gi 357500467 444 SIRAGIIWINCYFAFDiDC--PFGGYKMSGYGRDYG 477
Cdd:cd07152 393 RLRTGMLHINDQTVND-EPhnPFGGMGASGNGSRFG 427
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
12-488 |
7.91e-104 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 319.16 E-value: 7.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 12 IKIPTIKFKKLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDngPWPRMPGAERAKIMVKWA 91
Cdd:PRK11241 3 LNDSTLFRQQALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 92 TLIEQNQEEIAALDTIDGGKLYSWCKTvDVPEAANILRYYAGAADKVHGEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFP 170
Cdd:PRK11241 81 NLMMEHQDDLARLMTLEQGKPLAEAKG-EISYAASFIEWFAEEGKRIYGDTIPGHQaDKRLIVIKQPIGVTAAITPWNFP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 171 TIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGR 250
Cdd:PRK11241 160 AAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 251 RVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVV 330
Cdd:PRK11241 240 QLMEQCA-KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 331 GDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFK 410
Cdd:PRK11241 319 GDGLEKGVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 411 TIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRD---YGLEalhKYLQV 487
Cdd:PRK11241 399 DEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREgskYGIE---DYLEI 475
|
.
gi 357500467 488 K 488
Cdd:PRK11241 476 K 476
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
38-490 |
1.10e-103 |
|
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: 317.84 E-value: 1.10e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 38 ETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCK 117
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 118 tVDVPEAANILRYYAGAADKVHGEV-----FKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKP 192
Cdd:cd07094 80 -VEVDRAIDTLRLAAEEAERIRGEEipldaTQGSDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 193 AEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlsnLKPVSLELGGKS 272
Cdd:cd07094 159 ASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALRANAG---GKRIALELGGNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 273 PVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKI 352
Cdd:cd07094 236 PVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 353 LSYIKHGKNEGATLLTGGKQvgnKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVT 432
Cdd:cd07094 316 ERWVEEAVEAGARLLCGGER---DGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFT 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 357500467 433 KNLDIANTVSRSIRAGIIWINCYFAFDID-CPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07094 393 RDLNVAFKAAEKLEVGGVMVNDSSAFRTDwMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
58-490 |
1.72e-102 |
|
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: 313.74 E-value: 1.72e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 58 DVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKtVDVPEAANILRYYAGAADK 137
Cdd:cd07105 1 DADQAVEAAAAAF--PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAG-FNVDLAAGMLREAASLITQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 138 VHGEVFKTSR-NLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGV 216
Cdd:cd07105 78 IIGGSIPSDKpGTLAMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 217 LNVLPGFGSTAGA---AITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGI 293
Cdd:cd07105 158 LNVVTHSPEDAPEvveALIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAANAALFGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 294 LHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDpfdpkVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQV 373
Cdd:cd07105 237 FLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLAD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 374 GNK-GYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWI 452
Cdd:cd07105 312 ESPsGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHI 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 357500467 453 NCYFAFDIDC-PFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07105 392 NGMTVHDEPTlPHGGVKSSGYGRFNGKWGIDEFTETKWI 430
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
20-492 |
3.68e-102 |
|
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: 314.51 E-value: 3.68e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 20 KKLFINGGFVDSvSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFdNGPWPRMPGAERAKIMVKWATLIEQNQE 99
Cdd:cd07082 2 FKYLINGEWKES-SGKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 100 EIAALDTIDGGKLYSWCKTvDVPEAANILRYYAGAADKVHGEV-----FKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMF 174
Cdd:cd07082 80 EVANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSlpgdwFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 175 FAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQ 254
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 255 AAAlsnLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPF 334
Cdd:cd07082 239 QHP---MKRLVLELGGKDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 335 DPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKqvGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEE 414
Cdd:cd07082 316 DNGVDITPLIDPKSADFVEGLIDDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 415 GIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDC-PFGGYKMSGYGRD---YGLEALHKYlqvKSV 490
Cdd:cd07082 394 AIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQRGPDHfPFLGRKDSGIGTQgigDALRSMTRR---KGI 470
|
..
gi 357500467 491 AT 492
Cdd:cd07082 471 VI 472
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
87-490 |
1.03e-98 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 303.58 E-value: 1.03e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 87 MVKWATLIEQNQEEIAALDTIDGGKLYSWCKtVDVPEAANILRYYAGAADKVHGEVFKTSR-NLHMYTLMEPIGVVGHII 165
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAE-VEVAFTADYIDYMAEWARRYEGEIIQSDRpGENILLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 166 PWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGS 245
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSMTGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 246 TETGRRVMQAAAlSNLKPVSLELGGKSPVLIFddadVDKAVDLALFGILH----NKGEICVAYSRVFVQEGIYDEFEKKV 321
Cdd:PRK10090 160 VSAGEKIMAAAA-KNITKVCLELGGKAPAIVM----DDADLDLAVKAIVDsrviNSGQVCNCAERVYVQKGIYDQFVNRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 322 LEKAKNWVVGDPFD-PKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIF 400
Cdd:PRK10090 235 GEAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 401 GPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINcYFAFDIDCPF-GGYKMSGYGRDYGLE 479
Cdd:PRK10090 315 GPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYIN-RENFEAMQGFhAGWRKSGIGGADGKH 393
|
410
....*....|.
gi 357500467 480 ALHKYLQVKSV 490
Cdd:PRK10090 394 GLHEYLQTQVV 404
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
37-474 |
1.57e-98 |
|
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: 304.55 E-value: 1.57e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 37 FETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDngPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWC 116
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 117 KtVDVPEAANILRYYAGAADKVHGEVFK---TSRNLHMYTLME--PIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLK 191
Cdd:cd07147 79 R-GEVARAIDTFRIAAEEATRIYGEVLPldiSARGEGRQGLVRrfPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 192 PAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGfgSTAGAAI-TSHMDIDAVSFTGSTETGRRVMQAAALsnlKPVSLELGG 270
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLPC--SRDDADLlVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 271 KSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFD 350
Cdd:cd07147 233 NAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 351 KILSYIKHGKNEGATLLTGGKQVGNkgyYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGI 430
Cdd:cd07147 313 RVEGWVNEAVDAGAKLLTGGKRDGA---LLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGV 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 357500467 431 VTKNLDIANTVSRSIRAGIIWINCYFAFDID-CPFGGYKMSGYGR 474
Cdd:cd07147 390 FTRDLEKALRAWDELEVGGVVINDVPTFRVDhMPYGGVKDSGIGR 434
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
38-490 |
1.60e-92 |
|
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: 288.87 E-value: 1.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 38 ETVDPRTEEVITKIAEATKDDVDIAVKAAReafdnGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKlyswCK 117
Cdd:cd07146 2 EVRNPYTGEVVGTVPAGTEEALREALALAA-----SYRSTLTRYQRSAILNKAAALLEARREEFARLITLESGL----CL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 118 T---VDVPEAANILRYYAGAADKVHGEVFKTSRNLH-----MYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMV 189
Cdd:cd07146 73 KdtrYEVGRAADVLRFAAAEALRDDGESFSCDLTANgkarkIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 190 LKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVmqaAALSNLKPVSLELG 269
Cdd:cd07146 153 LKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEIGDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 270 GKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQF 349
Cdd:cd07146 230 GNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 350 DKILSYIKHGKNEGATLLTGGKQVGNKgYYiePTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAG 429
Cdd:cd07146 310 IQIENRVEEAIAQGARVLLGNQRQGAL-YA--PTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357500467 430 IVTKNLDIANTVSRSIRAGIIWINCYFAFDID-CPFGGYKMSGYGRDYG-LEALHKYLQVKSV 490
Cdd:cd07146 387 VCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPFGGVKDSGLGGKEGvREAMKEMTNVKTY 449
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
40-490 |
4.87e-90 |
|
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: 282.60 E-value: 4.87e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCK-- 117
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKG--WRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGge 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 118 TVDVPEAAnilRYYAG-AADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQT 196
Cdd:cd07102 79 IRGMLERA---RYMISiAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 197 PLSSLFFAHLAKEAGIPDGVLNVLPGFGSTaGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLI 276
Cdd:cd07102 156 PLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAA-GRFIKVGLELGGKDPAYV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 277 FDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYI 356
Cdd:cd07102 234 RPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 357 KHGKNEGATLLTGGK---QVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTK 433
Cdd:cd07102 314 ADAIAKGARALIDGAlfpEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 434 NLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:cd07102 394 DIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
40-492 |
3.17e-87 |
|
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: 275.72 E-value: 3.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 40 VDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMvkwATLIEQ---NQEEIAALDTIDGGKLY--- 113
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQRE--WAKTSFAERRKVL---RSLLKYileNQEEICRVACRDTGKTMvda 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 114 ------------SWckTVDVPEAA--------NILRYYAGAadKVHgevfktsrnlhmytlMEPIGVVGHIIPWNFPTIM 173
Cdd:cd07098 76 slgeilvtcekiRW--TLKHGEKAlrpesrpgGLLMFYKRA--RVE---------------YEPLGVVGAIVSWNYPFHN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 174 FFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEA----GIPDGVLNVLPGFGSTaGAAITSHMDIDAVSFTGSTETG 249
Cdd:cd07098 137 LLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacGHDPDLVQLVTCLPET-AEALTSHPVIDHITFIGSPPVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 250 RRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWV 329
Cdd:cd07098 216 KKVMAAAA-ESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 330 VGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGN----KGYYIEPTIFTNVKDDMLIAQDEIFGPVMA 405
Cdd:cd07098 295 QGPPLDGDVDVGAMISPARFDRLEELVADAVEKGARLLAGGKRYPHpeypQGHYFPPTLLVDVTPDMKIAQEEVFGPVMV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 406 LSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDC--PFGGYKMSGYGRDYGLEALHK 483
Cdd:cd07098 375 VMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMVAINDFGVNYYVQqlPFGGVKGSGFGRFAGEEGLRG 454
|
....*....
gi 357500467 484 YLQVKSVAT 492
Cdd:cd07098 455 LCNPKSVTE 463
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
22-491 |
7.23e-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: 265.60 E-value: 7.23e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSVSGKTfeTVDP-RTEEVITKIAEATKDDVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:cd07083 21 LVIGGEWVDTKERMV--SVSPfAPSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRRRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKlySWCKTVD-VPEAANILRYYAGAADKVHG---EVFKTSRNLHMyTLMEPIGVVGHIIPWNFPTIMFFA 176
Cdd:cd07083 97 LIATLTYEVGK--NWVEAIDdVAEAIDFIRYYARAALRLRYpavEVVPYPGEDNE-SFYVGLGAGVVISPWNFPVAIFTG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 177 KAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAA 256
Cdd:cd07083 174 MIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 257 A-----LSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVG 331
Cdd:cd07083 254 ArlapgQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 332 DPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGaTLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKT 411
Cdd:cd07083 334 PPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 412 IE--EGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDI--DCPFGGYKMSGYG-RDYGLEALHKYLQ 486
Cdd:cd07083 413 DDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALvgVQPFGGFKLSGTNaKTGGPHYLRRFLE 492
|
....*
gi 357500467 487 VKSVA 491
Cdd:cd07083 493 MKAVA 497
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
23-473 |
2.25e-80 |
|
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: 259.44 E-value: 2.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSvsGKTFETVDP-RTEEVITKIAEATKDDVDIAVKAAREAFdnGPWPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:cd07125 36 IINGEETET--GEGAPVIDPaDHERTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKlyswckTV-----DVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTL-MEPIGVVGHIIPWNFPTIMFF 175
Cdd:cd07125 112 IALAAAEAGK------TLadadaEVREAIDFCRYYAAQARELFSDPELPGPTGELNGLeLHGRGVFVCISPWNFPLAIFT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 176 AKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQ- 254
Cdd:cd07125 186 GQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINRa 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 255 -AAALSNLKPVSLELGGKSPVLIfddadvdkaVDLAL------------FGilhNKGEICVAYSRVFVQEGIYDEFEKKV 321
Cdd:cd07125 266 lAERDGPILPLIAETGGKNAMIV---------DSTALpeqavkdvvqsaFG---SAGQRCSALRLLYLQEEIAERFIEML 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 322 LEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEgATLLTGGKQVGNKGYYIEPTIFTNVKDDMLiaQDEIFG 401
Cdd:cd07125 334 KGAMASLKVGDPWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIVGIFDL--TTEVFG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 402 PVMALSKFK--TIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGiiwiNCYFAFDIDC------PFGGYKMSGYG 473
Cdd:cd07125 411 PILHVIRFKaeDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAG----NLYINRNITGaivgrqPFGGWGLSGTG 486
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
39-490 |
1.03e-77 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 250.81 E-value: 1.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKT 118
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 vDVPEAANILRYYAGaadkvHGEVF-----------KTSRNLHMYtlmEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCT 187
Cdd:PRK09406 83 -EALKCAKGFRYYAE-----HAEALladepadaaavGASRAYVRY---QPLGVVLAVMPWNFPLWQVVRFAAPALMAGNV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 188 MVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPgFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLE 267
Cdd:PRK09406 154 GLLKHASNVPQTALYLADLFRRAGFPDGCFQTLL-VGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAG-DEIKKTVLE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 268 LGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKA 347
Cdd:PRK09406 232 LGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 348 QFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLA 427
Cdd:PRK09406 312 GRDEVEKQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLG 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357500467 428 AGIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:PRK09406 392 SNAWTRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
38-473 |
8.72e-73 |
|
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: 237.70 E-value: 8.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 38 ETVDPRTEEVITKIAEATKDDVDIAVKAAREAF-DNGPWprMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWC 116
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFlDRNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 117 KtVDVPEAANILRYYAGAADKVHGE-----VFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLK 191
Cdd:cd07148 80 K-VEVTRAIDGVELAADELGQLGGReipmgLTPASAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 192 PAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMdIDAVSFTGSTETGRRVMqaaalSNLKP---VSLEL 268
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPR-VAFFSFIGSARVGWMLR-----SKLAPgtrCALEH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 269 GGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQ 348
Cdd:cd07148 233 GGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 349 FDKILSYIKHGKNEGATLLTGGKQVGNKGYyiEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAA 428
Cdd:cd07148 313 VDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQA 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 357500467 429 GIVTKNLDIANTVSRSIRAGIIWINCYFAFDID-CPFGGYKMSGYG 473
Cdd:cd07148 391 AVFTKDLDVALKAVRRLDATAVMVNDHTAFRVDwMPFAGRRQSGYG 436
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
33-435 |
9.28e-70 |
|
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: 230.17 E-value: 9.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 33 SGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKL 112
Cdd:cd07130 10 GGGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFKE--WRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 113 YSWCKTvDVPEAANILRYYAGAADKVHGEVFKTSRNLHMytLME---PIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMV 189
Cdd:cd07130 88 LPEGLG-EVQEMIDICDFAVGLSRQLYGLTIPSERPGHR--MMEqwnPLGVVGVITAFNFPVAVWGWNAAIALVCGNVVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 190 LKPAEQTPLSSL----FFAHLAKEAGIPDGVLNVLPGfGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVS 265
Cdd:cd07130 165 WKPSPTTPLTAIavtkIVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVA-ARFGRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 266 LELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTS 345
Cdd:cd07130 243 LELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 346 KAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTnVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYG 425
Cdd:cd07130 323 KAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQG 401
|
410
....*....|
gi 357500467 426 LAAGIVTKNL 435
Cdd:cd07130 402 LSSSIFTTDL 411
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
39-490 |
3.09e-65 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 218.19 E-value: 3.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 39 TVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKT 118
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRD--WRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 119 vDVPEAANILRYYAGaadkvHGEVFKTSRNlhmyTLME---------PIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMV 189
Cdd:PRK13968 89 -EVAKSANLCDWYAE-----HGPAMLKAEP----TLVEnqqavieyrPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 190 LKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMdIDAVSFTGSTETGRRV-MQAAALsnLKPVSLEL 268
Cdd:PRK13968 159 LKHAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSR-IAAVTVTGSVRAGAAIgAQAGAA--LKKCVLEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 269 GGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQ 348
Cdd:PRK13968 236 GGSDPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 349 FDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAA 428
Cdd:PRK13968 316 RDELHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357500467 429 GIVTKNLDIANTVSRSIRAGIIWINCYFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQVKSV 490
Cdd:PRK13968 396 TIFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
23-490 |
1.02e-63 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 217.69 E-value: 1.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFdngP-WPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAF---PlWRNTPITTRQRVMLKFQELIRKNMDKL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKLYSWCKTvDVPEAANILRYYAGAADKVHGEVF-KTSRNLHMYTLMEPIGVVGHIIPWNFPTIM---FFAK 177
Cdd:PLN02419 194 AMNITTEQGKTLKDSHG-DIFRGLEVVEHACGMATLQMGEYLpNVSNGVDTYSIREPLGVCAGICPFNFPAMIplwMFPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 178 AAPClaaGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGaAITSHMDIDAVSFTGSTETGRRVMQAAA 257
Cdd:PLN02419 273 AVTC---GNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVN-AICDDEDIRAVSFVGSNTAGMHIYARAA 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 258 LSNlKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVfVQEGIYDEFEKKVLEKAKNWVVGDPFDPK 337
Cdd:PLN02419 349 AKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTV-VFVGDAKSWEDKLVERAKALKVTCGSEPD 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 338 VQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGY----YIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIE 413
Cdd:PLN02419 427 ADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFD 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 414 EGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCyfAFDIDCP---FGGYKMSGYG--RDYGLEALHKYLQVK 488
Cdd:PLN02419 507 EAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPffsFTGNKASFAGdlNFYGKAGVDFFTQIK 584
|
..
gi 357500467 489 SV 490
Cdd:PLN02419 585 LV 586
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
29-473 |
4.54e-62 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 218.91 E-value: 4.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 29 VDSVSGKTFETVDP-RTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTI 107
Cdd:PRK11904 556 IINGEGEARPVVSPaDRRRVVGEVAFADAEQVEQALAAARAAFPA--WSRTPVEERAAILERAADLLEANRAELIALCVR 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 108 DGGKlyswckTVD-----VPEAANILRYYAGAADKVHGEVFK------TSRNLHMytlmEPIGVVGHIIPWNFPTIMFFA 176
Cdd:PRK11904 634 EAGK------TLQdaiaeVREAVDFCRYYAAQARRLFGAPEKlpgptgESNELRL----HGRGVFVCISPWNFPLAIFLG 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 177 KAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAA 256
Cdd:PRK11904 704 QVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTADPRIAGVAFTGSTETARIINRTL 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 257 ALSNLKPVSL--ELGGKSPVLIfddadvdkaVDLAL------------FGilhNKGEICVAYsRV-FVQEGIYDefekKV 321
Cdd:PRK11904 784 AARDGPIVPLiaETGGQNAMIV---------DSTALpeqvvddvvtsaFR---SAGQRCSAL-RVlFVQEDIAD----RV 846
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 322 LE----KAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEgATLLTGGK--QVGNKGYYIEPTIF--TNVKDdml 393
Cdd:PRK11904 847 IEmlkgAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKRE-ARLLAQLPlpAGTENGHFVAPTAFeiDSISQ--- 922
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 394 iAQDEIFGPVMALSKFKT--IEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGiiwiNCYFAFDI------DCPFG 465
Cdd:PRK11904 923 -LEREVFGPILHVIRYKAsdLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVG----NVYVNRNQigavvgVQPFG 997
|
....*...
gi 357500467 466 GYKMSGYG 473
Cdd:PRK11904 998 GQGLSGTG 1005
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
58-474 |
3.67e-60 |
|
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: 203.66 E-value: 3.67e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 58 DVDIAVKAAREAFDngPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSWCKT--------VDVPEAANILR 129
Cdd:cd07095 1 QVDAAVAAARAAFP--GWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTevaamagkIDISIKAYHER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 130 YYAGAADKVHGEVFKTSRnlhmytlmePIGVVGHIIPWNFPT------IMffakaaPCLAAGCTMVLKPAEQTPLSSLFF 203
Cdd:cd07095 79 TGERATPMAQGRAVLRHR---------PHGVMAVFGPFNFPGhlpnghIV------PALLAGNTVVFKPSELTPAVAELM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 204 AHLAKEAGIPDGVLNVLPGfGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSNLKPVSLELGGKSPVLIFDDADVD 283
Cdd:cd07095 144 VELWEEAGLPPGVLNLVQG-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 284 KAVDLALFGILHNKGEICVAYSRVFVQEGIY-DEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNE 362
Cdd:cd07095 223 AAAYLIVQSAFLTAGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 363 GATLLTGGKQVGNKGYYIEPTIF--TNVKDdmlIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANT 440
Cdd:cd07095 303 GGEPLLAMERLVAGTAFLSPGIIdvTDAAD---VPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFER 379
|
410 420 430
....*....|....*....|....*....|....*
gi 357500467 441 VSRSIRAGIIWINCYFAF-DIDCPFGGYKMSGYGR 474
Cdd:cd07095 380 FLARIRAGIVNWNRPTTGaSSTAPFGGVGLSGNHR 414
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
41-488 |
9.15e-60 |
|
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: 204.76 E-value: 9.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 41 DPRteEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSwCKTVD 120
Cdd:TIGR01238 60 DRR--DIVGQVFHANLAHVQAAIDSAQQAFPT--WNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIH-NAIAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 121 VPEAANILRYYAGAADKVHGEvfktsrnlhmyTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSS 200
Cdd:TIGR01238 135 VREAVDFCRYYAKQVRDVLGE-----------FSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 201 LFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSNLKPVSL--ELGGKSPVLIFD 278
Cdd:TIGR01238 204 YRAVELMQEAGFPAGTIQLLPGRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDS 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 279 DADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKH 358
Cdd:TIGR01238 284 TALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEH 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 359 GKNEGAT---LLTGGKQVGNKGYYIEPTIFTnvKDDMLIAQDEIFGPVMALSKFKT--IEEGIKKANNTKYGLAAGIVTK 433
Cdd:TIGR01238 364 MSQTQKKiaqLTLDDSRACQHGTFVAPTLFE--LDDIAELSEEVFGPVLHVVRYKAreLDQIVDQINQTGYGLTMGVHSR 441
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357500467 434 NLDIANTVSRSIRAGiiwiNCYFAFDIDC------PFGGYKMSGYG-RDYGLEALHKYLQVK 488
Cdd:TIGR01238 442 IETTYRWIEKHARVG----NCYVNRNQVGavvgvqPFGGQGLSGTGpKAGGPHYLYRLTQVQ 499
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
22-476 |
8.50e-59 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 201.73 E-value: 8.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 22 LFINGGFVDSvSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEI 101
Cdd:PRK09457 3 LWINGDWIAG-QGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPA--WARLSFEERQAIVERFAALLEENKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKLYsWCKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPC 181
Cdd:PRK09457 80 AEVIARETGKPL-WEAATEVTAMINKIAISIQAYHERTGEKRSEMADGAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 182 LAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGfGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSNL 261
Cdd:PRK09457 159 LLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGYLLHRQFAGQPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 262 KPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIY-DEFEKKVLEKAKNWVVGDPF-DPKVQ 339
Cdd:PRK09457 238 KILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDaEPQPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 340 QGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIF--TNVKDdmlIAQDEIFGPVMALSKFKTIEEGIK 417
Cdd:PRK09457 318 MGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGIIdvTGVAE---LPDEEYFGPLLQVVRYDDFDEAIR 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 418 KANNTKYGLAAGIVTKNLDIANTVSRSIRAGII-WINCYFAFDIDCPFGGYKMSG-------YGRDY 476
Cdd:PRK09457 395 LANNTRFGLSAGLLSDDREDYDQFLLEIRAGIVnWNKPLTGASSAAPFGGVGASGnhrpsayYAADY 461
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
21-473 |
2.03e-58 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 201.14 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 21 KLFINGGFVDSVSGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAfdNGPWPRMPGAERAKIMVKWATLIEQNQEE 100
Cdd:PLN00412 17 KYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAA--QKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 101 IAALDTIDGGKLYSWCKTvDVPEAANILRYYA-------GAADKVHGEVFK-TSRNLHMYTLMEPIGVVGHIIPWNFPTI 172
Cdd:PLN00412 95 IAECLVKEIAKPAKDAVT-EVVRSGDLISYTAeegvrilGEGKFLVSDSFPgNERNKYCLTSKIPLGVVLAIPPFNYPVN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 173 MFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGStETGRRV 252
Cdd:PLN00412 174 LAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGVNCISFTGG-DTGIAI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 253 MQAAALSnlkPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGD 332
Cdd:PLN00412 253 SKKAGMV---PLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 333 PFDpKVQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGKQVGNkgyYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTI 412
Cdd:PLN00412 330 PED-DCDITPVVSESSANFIEGLVMDAKEKGATFCQEWKREGN---LIWPLLLDNVRPDMRIAWEEPFGPVLPVIRINSV 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357500467 413 EEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFAFDID-CPFGGYKMSGYG 473
Cdd:PLN00412 406 EEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSAPARGPDhFPFQGLKDSGIG 467
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
62-490 |
2.28e-58 |
|
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: 198.90 E-value: 2.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 62 AVKAAREAFDNG-----PWprmpgaeRAKIMVKWATLIEQNQEEIAALDTIDGGK-----------------------LY 113
Cdd:cd07087 3 LVARLRETFLTGktrslEW-------RKAQLKALKRMLTENEEEIAAALYADLGKppaeaylteiavvlgeidhalkhLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 114 SWCKT--VDVPeaaniLRYYAGAAdkvhgevfktsrnlhmYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLK 191
Cdd:cd07087 76 KWMKPrrVSVP-----LLLQPAKA----------------YVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 192 PAEQTPLSSLFFAHLAKEAgIPDGVLNVLPGFGSTAgAAITSHmDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGK 271
Cdd:cd07087 135 PSELAPATSALLAKLIPKY-FDPEAVAVVEGGVEVA-TALLAE-PFDHIFFTGSPAVGKIVMEAAA-KHLTPVTLELGGK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 272 SPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKvLEKAKNWVVGDpfDPKVQQ--GPQTSKAQF 349
Cdd:cd07087 211 SPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELIEE-LKKAIKEFYGE--DPKESPdyGRIINERHF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 350 DKILSYIKHGKnegatLLTGGkQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAG 429
Cdd:cd07087 288 DRLASLLDDGK-----VVIGG-QVDKEERYIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALY 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 430 IVTKNLDIANTVSRSIRAGIIWIN--CYFAFDIDCPFGGYKMSGYGR---DYGLEAL-HKylqvKSV 490
Cdd:cd07087 362 LFSEDKAVQERVLAETSSGGVCVNdvLLHAAIPNLPFGGVGNSGMGAyhgKAGFDTFsHL----KSV 424
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
30-473 |
1.90e-55 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 200.48 E-value: 1.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 30 DSVSGKTFETVDP-RTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTID 108
Cdd:PRK11905 562 GDVDGGTRPVLNPaDHDDVVGTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPELFALAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 109 GGKlySWCKTVD-VPEAANILRYYAGAAdkvhgevfktsRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCT 187
Cdd:PRK11905 640 AGK--TLANAIAeVREAVDFLRYYAAQA-----------RRLLNGPGHKPLGPVVCISPWNFPLAIFTGQIAAALVAGNT 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 188 MVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSNLKPVSL- 266
Cdd:PRK11905 707 VLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAKRSGPPVPLi 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 267 -ELGGK------SPVLifddadvdkaVDLALFGILH----NKGEICVAYsRV-FVQEGIYDefekKVLEKAKN----WVV 330
Cdd:PRK11905 787 aETGGQnamivdSSAL----------PEQVVADVIAsafdSAGQRCSAL-RVlCLQEDVAD----RVLTMLKGamdeLRI 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 331 GDPFDPKVQQGPQ-TSKAQfDKILSYIKHGKNEGATLltggKQVG-----NKGYYIEPTIFtNVKD--DMliaQDEIFGP 402
Cdd:PRK11905 852 GDPWRLSTDVGPViDAEAQ-ANIEAHIEAMRAAGRLV----HQLPlpaetEKGTFVAPTLI-EIDSisDL---EREVFGP 922
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 357500467 403 VMALSKFKT--IEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINcyfaf--didcPFGGYKMSGYG 473
Cdd:PRK11905 923 VLHVVRFKAdeLDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAGNIYVNrniigavvgvqPFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
30-453 |
1.66e-54 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 197.47 E-value: 1.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 30 DSVSGKTFETVDP-RTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTID 108
Cdd:COG4230 565 EAASGEARPVRNPaDHSDVVGTVVEATAADVEAALAAAQAAFPA--WSATPVEERAAILERAADLLEAHRAELMALLVRE 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 109 GGKlyswckTVD-----VPEAANILRYYAGAAdkvhgevfktSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLA 183
Cdd:COG4230 643 AGK------TLPdaiaeVREAVDFCRYYAAQA----------RRLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALA 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 184 AGCTMVLKPAEQTPLsslfFAHLA----KEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALS 259
Cdd:COG4230 707 AGNTVLAKPAEQTPL----IAARAvrllHEAGVPADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAAR 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 260 NLKPVSL--ELGGK------SPVLI-----------FddadvdkavdlalfgilHNKGEICVAYsRV-FVQEGIYDefek 319
Cdd:COG4230 783 DGPIVPLiaETGGQnamivdSSALPeqvvddvlasaF-----------------DSAGQRCSAL-RVlCVQEDIAD---- 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 320 KVLE----KAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKNEGATLltggKQV-----GNKGYYIEPTIF--TNV 388
Cdd:COG4230 841 RVLEmlkgAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEGRLV----HQLplpeeCANGTFVAPTLIeiDSI 916
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 389 KDdmLiaQDEIFGPVMALSKFK--TIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN 453
Cdd:COG4230 917 SD--L--EREVFGPVLHVVRYKadELDKVIDAINATGYGLTLGVHSRIDETIDRVAARARVGNVYVN 979
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
57-477 |
1.23e-53 |
|
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: 186.66 E-value: 1.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 57 DDVDIAVKAAREAFDNGPwpRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKL--------YSWCKTvDVPEAANIL 128
Cdd:cd07135 5 DEIDSIHSRLRATFRSGK--TKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPpfetllteVSGVKN-DILHMLKNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 129 RYYAgaADKvhgevfKTSRNLHMYTLM------EPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLF 202
Cdd:cd07135 82 KKWA--KDE------KVKDGPLAFMFGkprirkEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 203 FAHLAKEAGIPDGVLNVLPGFGSTaGAAITSHMDidAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADV 282
Cdd:cd07135 154 LAELVPKYLDPDAFQVVQGGVPET-TALLEQKFD--KIFYTGSGRVGRIIAEAAA-KHLTPVTLELGGKSPVIVTKNADL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 283 DKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFekkvLEKAKNWVvgDPFDPKVQQGPQT-----SKAQFDKILSYIK 357
Cdd:cd07135 230 ELAAKRILWGKFGNAGQICVAPDYVLVDPSVYDEF----VEELKKVL--DEFYPGGANASPDytrivNPRHFNRLKSLLD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 358 HGKnegATLLTGGKQvGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDI 437
Cdd:cd07135 304 TTK---GKVVIGGEM-DEATRFIPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSE 379
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 357500467 438 ANTVSRSIRAGIIWIN-CYFAFDID-CPFGGYKMSGYGRDYG 477
Cdd:cd07135 380 IDHILTRTRSGGVVINdTLIHVGVDnAPFGGVGDSGYGAYHG 421
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
67-479 |
5.77e-52 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 181.91 E-value: 5.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 67 REAFDNGPWPRMpgAERAKIMVKWATLIEQNQEEIA-ALD------------------TIDGGK-----LYSWCKtvdvP 122
Cdd:cd07133 8 KAAFLANPPPSL--EERRDRLDRLKALLLDNQDALAeAISadfghrsrhetllaeilpSIAGIKharkhLKKWMK----P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 123 EaanilryyagaadKVH-GEVFKTSRNLHMYtlmEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSL 201
Cdd:cd07133 82 S-------------RRHvGLLFLPAKAEVEY---QPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 202 FFAHLAKEAGIPDGVLNVLpGfGSTAGAAItSHMDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDAD 281
Cdd:cd07133 146 LLAELLAEYFDEDEVAVVT-G-GADVAAAF-SSLPFDHLLFTGSTAVGRHVMRAAA-ENLTPVTLELGGKSPAIIAPDAD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 282 VDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFekkvLEKAKNWVVGdpFDPKVQQGPQ-TS---KAQFDKILSYIK 357
Cdd:cd07133 222 LAKAAERIAFGKLLNAGQTCVAPDYVLVPEDKLEEF----VAAAKAAVAK--MYPTLADNPDyTSiinERHYARLQGLLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 358 HGKNEGATL--LTGGKQVGNKGYYIEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNL 435
Cdd:cd07133 296 DARAKGARVieLNPAGEDFAATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDK 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 357500467 436 DIANTVSRSIRAGIIWIN---CYFAFDiDCPFGGYKMSGYGRDYGLE 479
Cdd:cd07133 376 AEQDRVLRRTHSGGVTINdtlLHVAQD-DLPFGGVGASGMGAYHGKE 421
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
32-471 |
6.79e-52 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 183.94 E-value: 6.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 32 VSGKTFETVDPRT-------EEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQN-QEEIAA 103
Cdd:cd07123 37 IGGKEVRTGNTGKqvmphdhAHVLATYHYADAALVEKAIEAALEARKE--WARMPFEDRAAIFLKAADLLSGKyRYELNA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 104 LDTIDGGKlYSWCKTVDVP-EAANILRYYAGAADKVHGE----VFKTSRNLHMYTLMEpiGVVGHIIPWNFPTIMFFAKA 178
Cdd:cd07123 115 ATMLGQGK-NVWQAEIDAAcELIDFLRFNVKYAEELYAQqplsSPAGVWNRLEYRPLE--GFVYAVSPFNFTAIGGNLAG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 179 APCLAaGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAAl 258
Cdd:cd07123 192 APALM-GNVVLWKPSDTAVLSNYLVYKILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIG- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 259 SNLK-----P-VSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGD 332
Cdd:cd07123 270 ENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 333 PFDPKVQQGPQTSKAQFDKILSYIKHGKNE-GATLLTGGKQVGNKGYYIEPTIF--TNVKDDMLiaQDEIFGPVMAL--- 406
Cdd:cd07123 350 PDDFSNFMGAVIDEKAFDRIKGYIDHAKSDpEAEIIAGGKCDDSVGYFVEPTVIetTDPKHKLM--TEEIFGPVLTVyvy 427
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 407 --SKFKTIEEGIKKAnnTKYGLAAGIVTKNLDIANTVSRSIR--AGIIWINCyfafdiDC--------PFGGYKMSG 471
Cdd:cd07123 428 pdSDFEETLELVDTT--SPYALTGAIFAQDRKAIREATDALRnaAGNFYIND------KPtgavvgqqPFGGARASG 496
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
156-477 |
2.95e-50 |
|
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: 177.42 E-value: 2.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 156 EPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGVlNVLPGFGSTAGAAITshM 235
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEV-AVFEGDAEVAQALLE--L 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 236 DIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYD 315
Cdd:cd07134 176 PFDHIFFTGSPAVGKIVMAAAA-KHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 316 EFE---KKVLEKaknwVVGDpfDPKVQQGPQ----TSKAQFDKILSYIKHGKNEGATLLTGGkQVGNKGYYIEPTIFTNV 388
Cdd:cd07134 255 AFVehlKAEIEK----FYGK--DAARKASPDlariVNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVLTNV 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 389 KDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINCYFA--FDIDCPFGG 466
Cdd:cd07134 328 TPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLhfLNPNLPFGG 407
|
330
....*....|.
gi 357500467 467 YKMSGYGRDYG 477
Cdd:cd07134 408 VNNSGIGSYHG 418
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
152-473 |
2.67e-46 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 168.28 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 152 YTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAgIPDGVLNVLPGfGSTAGAAI 231
Cdd:PTZ00381 104 YIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEG-GVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 232 TSHmDIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQE 311
Cdd:PTZ00381 182 LKE-PFDHIFFTGSPRVGKLVMQAAA-ENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVHR 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 312 GIYDEFEKKVLEKAKNWvVGDpfDPKVQQ--GPQTSKAQFDKILSYIkhgKNEGATLLTGGkQVGNKGYYIEPTIFTNVK 389
Cdd:PTZ00381 260 SIKDKFIEALKEAIKEF-FGE--DPKKSEdySRIVNEFHTKRLAELI---KDHGGKVVYGG-EVDIENKYVAPTIIVNPD 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 390 DDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN-CYFAF-DIDCPFGGY 467
Cdd:PTZ00381 333 LDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdCVFHLlNPNLPFGGV 412
|
....*.
gi 357500467 468 KMSGYG 473
Cdd:PTZ00381 413 GNSGMG 418
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
33-486 |
5.37e-45 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 165.01 E-value: 5.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 33 SGKTFETVDPRTEEVITKIAEATKDDVDIAVKAAREAFDNgpWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKL 112
Cdd:PLN02315 32 NGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 113 YSWcKTVDVPEAANILRYYAGAADKVHGEVFKTSRNLHMytLME---PIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMV 189
Cdd:PLN02315 110 LAE-GIGEVQEIIDMCDFAVGLSRQLNGSIIPSERPNHM--MMEvwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 190 LKPAEQTPLSSL----FFAHLAKEAGIPDGVLNVLPGfGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSNLKPVs 265
Cdd:PLN02315 187 WKGAPTTPLITIamtkLVAEVLEKNNLPGAIFTSFCG-GAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCL- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 266 LELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTS 345
Cdd:PLN02315 265 LELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 346 KAQFDKILSYIKHGKNEGATLLTGGKQVGNKGYYIEPTIfTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYG 425
Cdd:PLN02315 345 PESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQG 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357500467 426 LAAGIVTKNLDianTVSRSI-----RAGIIWINC-YFAFDIDCPFGGYKMSGYGRDYGLEALHKYLQ 486
Cdd:PLN02315 424 LSSSIFTRNPE---TIFKWIgplgsDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQYMR 487
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
152-477 |
2.96e-44 |
|
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: 161.52 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 152 YTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAgIPDGVLNVLPGfgstaGAAI 231
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDEEYVAVVEG-----GVEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 232 TSHM---DIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIfddaDVDKAVDLA----LFGILHNKGEICVAY 304
Cdd:cd07136 169 NQELldqKFDYIFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIV----DEDANLKLAakriVWGKFLNAGQTCVAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 305 SRVFVQEGIYDEFEKKVLEKAKNWVVGDPFD----PKVqqgpqTSKAQFDKILSYIKHGKnegatLLTGGKqvGNKG-YY 379
Cdd:cd07136 244 DYVLVHESVKEKFIKELKEEIKKFYGEDPLEspdyGRI-----INEKHFDRLAGLLDNGK-----IVFGGN--TDREtLY 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 380 IEPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWINcyfafd 459
Cdd:cd07136 312 IEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCIN------ 385
|
330 340
....*....|....*....|....*..
gi 357500467 460 iDC---------PFGGYKMSGYGRDYG 477
Cdd:cd07136 386 -DTimhlanpylPFGGVGNSGMGSYHG 411
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
41-473 |
1.58e-38 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 150.51 E-value: 1.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 41 DPRteEVITKIAEATKDDVDIAVKAAREAfdnGP-WPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKLYSwCKTV 119
Cdd:PRK11809 668 DPR--DIVGYVREATPAEVEQALESAVNA---APiWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFS-NAIA 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 120 DVPEAANILRYYAG-AADKVHGEvfkTSRnlhmytlmePIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPL 198
Cdd:PRK11809 742 EVREAVDFLRYYAGqVRDDFDND---THR---------PLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPL 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 199 SSLFFAHLAKEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQ--AAALSNL-KPVSL--ELGGKSP 273
Cdd:PRK11809 810 IAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADARVRGVMFTGSTEVARLLQRnlAGRLDPQgRPIPLiaETGGQNA 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 274 VLIFDDADVDKAVDLALFGILHNKGEICVAYSRVFVQEGIYDefekKVLEKAK----NWVVGDPFDPKVQQGPQTSKAQF 349
Cdd:PRK11809 890 MIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCLQDDVAD----RTLKMLRgamaECRMGNPDRLSTDIGPVIDAEAK 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 350 DKILSYIKHGKNEGAT---LLTGGKQVGNKGYYIEPT-IFTNVKDDMliaQDEIFGPVMALSKFK--TIEEGIKKANNTK 423
Cdd:PRK11809 966 ANIERHIQAMRAKGRPvfqAARENSEDWQSGTFVPPTlIELDSFDEL---KREVFGPVLHVVRYNrnQLDELIEQINASG 1042
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 357500467 424 YGLAAGIVTKnldIANTVSR---SIRAGiiwiNCYFAFDIDC------PFGGYKMSGYG 473
Cdd:PRK11809 1043 YGLTLGVHTR---IDETIAQvtgSAHVG----NLYVNRNMVGavvgvqPFGGEGLSGTG 1094
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
156-477 |
8.75e-38 |
|
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: 143.71 E-value: 8.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 156 EPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAgIPDGVLNVLPGfgstaGAAITSHM 235
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEY-LDTKAIKVIEG-----GVPETTAL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 236 ---DIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILH-NKGEICVAYSRVFVQE 311
Cdd:cd07137 174 leqKWDKIFFTGSPRVGRIIMAAAA-KHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGcNNGQACIAPDYVLVEE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 312 giydEFEKKVLEKAKNWV---VGDpfDPK-VQQGPQTSKAQFDKILSYIKHGKNEGATLLTGGkQVGNKGYYIEPTIFTN 387
Cdd:cd07137 253 ----SFAPTLIDALKNTLekfFGE--NPKeSKDLSRIVNSHHFQRLSRLLDDPSVADKIVHGG-ERDEKNLYIEPTILLD 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 388 VKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN-CYFAFDID-CPFG 465
Cdd:cd07137 326 PPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNdTVVQYAIDtLPFG 405
|
330
....*....|..
gi 357500467 466 GYKMSGYGRDYG 477
Cdd:cd07137 406 GVGESGFGAYHG 417
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
152-477 |
1.09e-32 |
|
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: 129.65 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 152 YTLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLakeagIPDGVLN----VLpgfgsTA 227
Cdd:cd07132 95 YIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAEL-----IPKYLDKecypVV-----LG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 228 GAAITSHM---DIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAY 304
Cdd:cd07132 165 GVEETTELlkqRFDYIFYTGSTSVGKIVMQAAA-KHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTCIAP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 305 SRVFVQEGIYDEFEKKVLEKAKNWvVGDpfDPKVQQ--GPQTSKAQFDKILSYIKHGKnegatLLTGGkQVGNKGYYIEP 382
Cdd:cd07132 244 DYVLCTPEVQEKFVEALKKTLKEF-YGE--DPKESPdyGRIINDRHFQRLKKLLSGGK-----VAIGG-QTDEKERYIAP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 383 TIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN---CYFAFD 459
Cdd:cd07132 315 TVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNdtiMHYTLD 394
|
330
....*....|....*...
gi 357500467 460 iDCPFGGYKMSGYGRDYG 477
Cdd:cd07132 395 -SLPFGGVGNSGMGAYHG 411
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
23-430 |
7.90e-30 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 122.51 E-value: 7.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSvSGKTFETVDPRTEEVITKiAEATKDDVDIAVKAAREafDNGPWPRMPG-AERAKIMVKWATLIEQNQEEI 101
Cdd:PRK11903 8 YVAGRWQAG-SGAGTPLFDPVTGEELVR-VSATGLDLAAAFAFARE--QGGAALRALTyAQRAALLAAIVKVLQANRDAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 102 AALDTIDGGKLYSWCKtVDVPEAANILRYYAGAADKVhGEVF-----------KTSRNLHMYTLMEPIGVVGHIIPWNFP 170
Cdd:PRK11903 84 YDIATANSGTTRNDSA-VDIDGGIFTLGYYAKLGAAL-GDARllrdgeavqlgKDPAFQGQHVLVPTRGVALFINAFNFP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 171 TIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGI-PDGVLNVLPGfgstAGAAITSHMD-IDAVSFTGSTET 248
Cdd:PRK11903 162 AWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGIlPAGALSVVCG----SSAGLLDHLQpFDVVSFTGSAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 249 GRR------VMQAAALSNLKPVSLelggKSPVLIFDDADVDKAVDLALFGILHN----KGEICVAYSRVFVQEGIYDEFE 318
Cdd:PRK11903 238 AAVlrshpaVVQRSVRVNVEADSL----NSALLGPDAAPGSEAFDLFVKEVVREmtvkSGQKCTAIRRIFVPEALYDAVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 319 KKVLEKAKNWVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKnEGATLLTGGKQVG------NKGYYIEPTIF-TNVKDD 391
Cdd:PRK11903 314 EALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALR-AQAEVLFDGGGFAlvdadpAVAACVGPTLLgASDPDA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 357500467 392 MLIAQD-EIFGPVMALSKFKTIEEGIKKANNTKYGLAAGI 430
Cdd:PRK11903 393 ATAVHDvEVFGPVATLLPYRDAAHALALARRGQGSLVASV 432
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
156-477 |
6.59e-28 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 116.36 E-value: 6.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 156 EPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAhlakeAGIP----DGVLNVLPGfgstaGAAI 231
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLA-----ANIPkyldSKAVKVIEG-----GPAV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 232 TSHM---DIDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVlIFDDADVDKAVDLALFGILHNK-----GEICVA 303
Cdd:PLN02203 177 GEQLlqhKWDKIFFTGSPRVGRIIMTAAA-KHLTPVALELGGKCPC-IVDSLSSSRDTKVAVNRIVGGKwgscaGQACIA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 304 YSRVFVQEG---IYDEFEKKVLEKaknWVVGDPFDPKvQQGPQTSKAQFDKILSYIKHgKNEGATLLTGGkQVGNKGYYI 380
Cdd:PLN02203 255 IDYVLVEERfapILIELLKSTIKK---FFGENPRESK-SMARILNKKHFQRLSNLLKD-PRVAASIVHGG-SIDEKKLFI 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 381 EPTIFTNVKDDMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLD-----IANTVSRSIRAGIIWINcy 455
Cdd:PLN02203 329 EPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKlkrriLSETSSGSVTFNDAIIQ-- 406
|
330 340
....*....|....*....|..
gi 357500467 456 FAFDiDCPFGGYKMSGYGRDYG 477
Cdd:PLN02203 407 YACD-SLPFGGVGESGFGRYHG 427
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
23-441 |
1.30e-27 |
|
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: 115.83 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 23 FINGGFVDSvSGKTFETVDPRTEEVItkiAEATKDDVDI--AVKAAREafDNGPWPR-MPGAERAKIMVKWATLIEQNQE 99
Cdd:cd07128 4 YVAGQWHAG-TGDGRTLHDAVTGEVV---ARVSSEGLDFaaAVAYARE--KGGPALRaLTFHERAAMLKALAKYLMERKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 100 EIAALDTIDGG-KLYSWcktVDVPEAANILRYYAGAA------DKVH--GEVFKTSRNL-----HMYTlmePI-GVVGHI 164
Cdd:cd07128 78 DLYALSAATGAtRRDSW---IDIDGGIGTLFAYASLGrrelpnAHFLveGDVEPLSKDGtfvgqHILT---PRrGVAVHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 165 IPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTplsslffAHLAK-------EAGI-PDGVLNVLpgFGSTAGaaITSHMD 236
Cdd:cd07128 152 NAFNFPVWGMLEKFAPALLAGVPVIVKPATAT-------AYLTEavvkdivESGLlPEGALQLI--CGSVGD--LLDHLG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 237 I-DAVSFTGSTETGRR------VMQAAALSNLKPVSLELGgkspvlIFDDADVDKAVDLALF------GILHNKGEICVA 303
Cdd:cd07128 221 EqDVVAFTGSAATAAKlrahpnIVARSIRFNAEADSLNAA------ILGPDATPGTPEFDLFvkevarEMTVKAGQKCTA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 304 YSRVFVQEGIYD---EFEKKVLEKAknwVVGDPFDPKVQQGPQTSKAQFDKILSYIKHGKnEGATLLTGGKQV------- 373
Cdd:cd07128 295 IRRAFVPEARVDaviEALKARLAKV---VVGDPRLEGVRMGPLVSREQREDVRAAVATLL-AEAEVVFGGPDRfevvgad 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357500467 374 GNKGYYIEPTIFTnVKDDM---LIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTV 441
Cdd:cd07128 371 AEKGAFFPPTLLL-CDDPDaatAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFAREL 440
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
62-485 |
1.32e-24 |
|
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: 106.17 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 62 AVKAAREafDNGPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGGKlySWCKTVDVPEAANILRYYAGAADKV--- 138
Cdd:cd07084 4 ALLAADI--STKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGK--GWMFAENICGDQVQLRARAFVIYSYrip 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 139 HGEVFKTSRNLHMYTLME--PIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAKEAGIPDGV 216
Cdd:cd07084 80 HEPGNHLGQGLKQQSHGYrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGLLPPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 217 LNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVmqaAALSNLKPVSLELGGKSPVLIFDDADVDKAVDLAL-FGILH 295
Cdd:cd07084 160 DVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKL---ALDAKQARIYLELAGFNWKVLGPDAQAVDYVAWQCvQDMTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 296 NKGEICVAYSRVFVQEgiyDEFEKKVLEKAKNWVvgdpfdpkVQQGPQTS---KAQFDKILSYIKHGKNE-GATLLTGGK 371
Cdd:cd07084 237 CSGQKCTAQSMLFVPE---NWSKTPLVEKLKALL--------ARRKLEDLllgPVQTFTTLAMIAHMENLlGSVLLFSGK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 372 QVGNK------GYYIEPTIFTNVKDDM---LIAQDEIFGPVMALSKFKTIEEG--IKKANNTKYGLAAGIV-TKNLDIAN 439
Cdd:cd07084 306 ELKNHsipsiyGACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYsNDPIFLQE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 357500467 440 TVSRSIRAGIIWINCYF---AFDIDCPFGGYKMSGYGRD-YGLEALHKYL 485
Cdd:cd07084 386 LIGNLWVAGRTYAILRGrtgVAPNQNHGGGPAADPRGAGiGGPEAIKLVW 435
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
156-490 |
3.23e-24 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 105.51 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 156 EPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHLAkEAGIPDGVLNVLPGFGSTAGAAITSHM 235
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLL-EQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 236 diDAVSFTGSTETGRRVMQAAAlSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILH-NKGEICVAYSRVFVQEgiy 314
Cdd:PLN02174 190 --DKIFYTGSSKIGRVIMAAAA-KHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWGcNNGQACISPDYILTTK--- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 315 dEFEKKVLEKAK----NWVVGDPFDPKvQQGPQTSKAQFDKiLSYIKHGKNEGATLLTGGKQvGNKGYYIEPTIFTNVKD 390
Cdd:PLN02174 264 -EYAPKVIDAMKkeleTFYGKNPMESK-DMSRIVNSTHFDR-LSKLLDEKEVSDKIVYGGEK-DRENLKIAPTILLDVPL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 391 DMLIAQDEIFGPVMALSKFKTIEEGIKKANNTKYGLAAGIVTKNLDIANTVSRSIRAGIIWIN---CYFAFDIdCPFGGY 467
Cdd:PLN02174 340 DSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNdiaVHLALHT-LPFGGV 418
|
330 340
....*....|....*....|...
gi 357500467 468 KMSGYGRDYGLEALHKYLQVKSV 490
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAV 441
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
59-403 |
7.61e-20 |
|
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: 91.83 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 59 VDIAVKAAREAFDngPWPRMPGAERAKIMVKWATLIEQNQEEIAALDTIDGG----KLyswckTVDVPEAANILRYYAGA 134
Cdd:cd07129 1 VDAAAAAAAAAFE--SYRALSPARRAAFLEAIADEIEALGDELVARAHAETGlpeaRL-----QGELGRTTGQLRLFADL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 135 ADKvhGEVF-----------KTSRNLHMYTLMEPIGVVGHIIPWNFPtIMF------FAKAapcLAAGCTMVLKPAEQTP 197
Cdd:cd07129 74 VRE--GSWLdaridpadpdrQPLPRPDLRRMLVPLGPVAVFGASNFP-LAFsvaggdTASA---LAAGCPVVVKAHPAHP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 198 LSSLFFAHLA----KEAGIPDGVLNVLPGFGSTAGAAITSHMDIDAVSFTGSTETGRRVMQAAALSNL-KPVSLELGGKS 272
Cdd:cd07129 148 GTSELVARAIraalRATGLPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 273 PVLIFDDADVDKAVDLA--LFG-ILHNKGEICVAYSRVFVQEGI-YDEFEKKVLEKAKNWVVGDPFDPKVQQGPQTSKAQ 348
Cdd:cd07129 228 PVFILPGALAERGEAIAqgFVGsLTLGAGQFCTNPGLVLVPAGPaGDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 357500467 349 FdkilsyikhGKNEGATLLTGGkQVGNKGYYIEPTIFTnVKDDMLIA----QDEIFGPV 403
Cdd:cd07129 308 L---------AAAPGVRVLAGG-AAAEGGNQAAPTLFK-VDAAAFLAdpalQEEVFGPA 355
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
128-316 |
9.24e-07 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 51.07 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 128 LRYYAGAADKVHGEVfkTSRNLHMYTLMEPIGVVGHIIPWNFPTIMFFaKAAPCLAAGCTMVLKPAEQTPLSSlFFAHLA 207
Cdd:cd07077 73 ERGITASVGHIQDVL--LPDNGETYVRAFPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTN-RALALL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 208 KEAGIPDGVLNVLPGFGSTAGA----AITSHMDIDAVSFTGstetGRRVMQAA-ALSNLKPVSLELGGKSPVLIFDDADV 282
Cdd:cd07077 149 FQAADAAHGPKILVLYVPHPSDelaeELLSHPKIDLIVATG----GRDAVDAAvKHSPHIPVIGFGAGNSPVVVDETADE 224
|
170 180 190
....*....|....*....|....*....|....
gi 357500467 283 DKAVDLALFGILHNkGEICVAYSRVFVQEGIYDE 316
Cdd:cd07077 225 ERASGSVHDSKFFD-QNACASEQNLYVVDDVLDP 257
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
153-316 |
2.24e-03 |
|
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: 40.33 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 153 TLMEPIGVVGHIIPWNFPTIMFFAKAAPCLAAGCTMVLKPAEQTPLSSLFFAHL----AKEAGIPDGVLNVLPGFGSTAG 228
Cdd:cd07081 91 IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLllqaAVAAGAPENLIGWIDNPSIELA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 229 AAITSHMDIDAVSFTGSTEtgrrvMQAAALSNLKPVSLELGGKSPVLIFDDADVDKAVDLALFGILHNKGEICVAYSRVF 308
Cdd:cd07081 171 QRLMKFPGIGLLLATGGPA-----VVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVI 245
|
....*...
gi 357500467 309 VQEGIYDE 316
Cdd:cd07081 246 VVDSVYDE 253
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
156-454 |
3.94e-03 |
|
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: 39.78 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 156 EPIGVVGHIIPWNFP--TIMFfaKAAPCLAAGCTMVLKPAEQTPLSSLFFAHL----AKEAGIPDGVLNVLPGFGSTAGA 229
Cdd:cd07122 94 EPVGVIAALIPSTNPtsTAIF--KALIALKTRNAIIFSPHPRAKKCSIEAAKImreaAVAAGAPEGLIQWIEEPSIELTQ 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 230 AITSHMDIDAVSFTGSTEtgrrvMQAAALSNLKPVsleLG---GKSPVLIfddaDVDKAVDLALFGILHNK----GEICV 302
Cdd:cd07122 172 ELMKHPDVDLILATGGPG-----MVKAAYSSGKPA---IGvgpGNVPAYI----DETADIKRAVKDIILSKtfdnGTICA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 303 AYSRVFVQEGIYDEF---------------EKKVLEKAKnWVVGDPFDPK-VQQGPQT--SKAQFdKIlsyikhgkNEGA 364
Cdd:cd07122 240 SEQSVIVDDEIYDEVraelkrrgayflneeEKEKLEKAL-FDDGGTLNPDiVGKSAQKiaELAGI-EV--------PEDT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357500467 365 TLLTGG-KQVGNKgyyiEPtiFTNvkddmliaqdEIFGPVMALSKFKTIEEGIKKAN-NTKYGLA---AGIVTKNLDIAN 439
Cdd:cd07122 310 KVLVAEeTGVGPE----EP--LSR----------EKLSPVLAFYRAEDFEEALEKAReLLEYGGAghtAVIHSNDEEVIE 373
|
330
....*....|....*
gi 357500467 440 TVSRSIRAGIIWINC 454
Cdd:cd07122 374 EFALRMPVSRILVNT 388
|
|
| |
