|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
439-923 |
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: 1018.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 439 VKMPYQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLE 518
Cdd:cd07140 2 LKMPHQLFINGEFVDAEGGKTYNTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENGEWGKMNARDRGRLMYRLADLME 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 519 ENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNRNLTFTKKEPLGVCAIIIPWNYPL 598
Cdd:cd07140 82 EHQEELATIESLDSGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGKTIPINQARPNRNLTLTKREPIGVCGIVIPWNYPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 599 MMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQ 678
Cdd:cd07140 162 MMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAGFPKGVINILPGSGSLVGQRLSDHPDVRKLGFTGSTPIGKH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 679 IMKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIG 758
Cdd:cd07140 242 IMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 759 DPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQN 838
Cdd:cd07140 322 DPLDRSTDHGPQNHKAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 839 GDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKT 918
Cdd:cd07140 402 GDVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKT 481
|
....*
gi 238814322 919 VTLEY 923
Cdd:cd07140 482 VTIEY 486
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
441-920 |
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: 750.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 441 MPYQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEEN 520
Cdd:cd07091 2 QPTGLFINNEFVDSVSGKTFPTINPATEEVICQVAEADEEDVDAAVKAARAAFETGWWRKMDPRERGRLLNKLADLIERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 521 QEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqarpNRNLTFTKKEPLGVCAIIIPWNYPLMM 600
Cdd:cd07091 82 RDELAALESLDNGKPLEESAKGDVALSIKCLRYYAGWADKIQGKTIPID----GNFLAYTRREPIGVCGQIIPWNFPLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 601 LAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIM 680
Cdd:cd07091 158 LAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAGFPPGVVNIVPGFGPTAGAAISSHMDVDKIAFTGSTAVGRTIM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 681 KSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDP 760
Cdd:cd07091 238 EAAAKSNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 761 LDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngD 840
Cdd:cd07091 318 FDPDTFQGPQVSKAQFDKILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFK--T 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 841 IDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVT 920
Cdd:cd07091 396 EDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAVT 475
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
438-923 |
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: 609.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 438 MVKMPYQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFenGEWGRMNARERGRLMYRLADLL 517
Cdd:COG1012 1 MTTPEYPLFIGGEWVAAASGETFDVINPATGEVLARVPAATAEDVDAAVAAARAAF--PAWAATPPAERAAILLRAADLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 518 EENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPInqARPNRnLTFTKKEPLGVCAIIIPWNYP 597
Cdd:COG1012 79 EERREELAALLTLETGKPLAEA-RGEVDRAADFLRYYAGEARRLYGETIPS--DAPGT-RAYVRREPLGVVGAITPWNFP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 598 LMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGK 677
Cdd:COG1012 155 LALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGLPAGVLNVVTGDGSEVGAALVAHPDVDKISFTGSTAVGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 678 QIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKI 757
Cdd:COG1012 235 RIAAAAA-ENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 758 GDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQR-PGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKF 836
Cdd:COG1012 314 GDPLDPGTDMGPLISEAQLERVLAYIEDAVAEGAELLTGGRRPDGeGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 837 QngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVA-APFGGVKQSGFGKDLGEEALNEYLK 915
Cdd:COG1012 394 D--DEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDGTTGAVPqAPFGGVKQSGIGREGGREGLEEYTE 471
|
....*...
gi 238814322 916 TKTVTLEY 923
Cdd:COG1012 472 TKTVTIRL 479
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
444-921 |
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: 605.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 444 QCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENG-EWGRMNARERGRLMYRLADLLEENQE 522
Cdd:cd07141 8 KIFINNEWHDSVSGKTFPTINPATGEKICEVQEGDKADVDKAVKAARAAFKLGsPWRTMDASERGRLLNKLADLIERDRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 523 ELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqarpNRNLTFTKKEPLGVCAIIIPWNYPLMMLA 602
Cdd:cd07141 88 YLASLETLDNGKPFSKSYLVDLPGAIKVLRYYAGWADKIHGKTIPMD----GDFFTYTRHEPVGVCGQIIPWNFPLLMAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKS 682
Cdd:cd07141 164 WKLAPALACGNTVVLKPAEQTPLTALYLASLIKEAGFPPGVVNVVPGYGPTAGAAISSHPDIDKVAFTGSTEVGKLIQQA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 683 CAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLD 762
Cdd:cd07141 244 AGKSNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 763 RSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDID 842
Cdd:cd07141 324 PKTEQGPQIDEEQFKKILELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFK--TID 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238814322 843 GVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07141 402 EVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTI 480
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
454-919 |
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: 605.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 454 ADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSG 533
Cdd:pfam00171 3 DSESETIEVINPATGEVIATVPAATAEDVDAAIAAARAAFP--AWRKTPAAERAAILRKAADLLEERKDELAELETLENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 534 AVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPInqaRPNRnLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGN 613
Cdd:pfam00171 81 KPLAEA-RGEVDRAIDVLRYYAGLARRLDGETLPS---DPGR-LAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 614 TLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSL 693
Cdd:pfam00171 156 TVVLKPSELTPLTALLLAELFEEAGLPAGVLNVVTGSGAEVGEALVEHPDVRKVSFTGSTAVGRHIAEAAA-QNLKRVTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 694 ELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHK 773
Cdd:pfam00171 235 ELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 774 AHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEY 853
Cdd:pfam00171 315 AQLERVLKYVEDAKEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFK--DEEEAIEIANDTEY 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238814322 854 GLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDV-AAPFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:pfam00171 393 GLAAGVFTSDLERALRVARRLEAGMVWINDYTTGDAdGLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
497-921 |
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: 562.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTlALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqarPNRN 576
Cdd:cd07078 13 AWAALPPAERAAILRKLADLLEERREELAALETLETGKPIE-EALGEVARAADTFRYYAGLARRLHGEVIPSP---DPGE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 577 LTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQ 656
Cdd:cd07078 89 LAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVTGDGDEVGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 657 RLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFV 736
Cdd:cd07078 169 ALASHPRVDKISFTGSTAVGKAIMRAAA-ENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCTAASRLLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 737 EESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGG-RQVQRPGFFMEPTVFTDV 815
Cdd:cd07078 248 HESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGkRLEGGKGYFVPPTVLTDV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 816 EDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNK-TDVAAPFG 894
Cdd:cd07078 328 DPDMPIAQEEIFGPVLPVIPFK--DEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVgAEPSAPFG 405
|
410 420
....*....|....*....|....*..
gi 238814322 895 GVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07078 406 GVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
439-919 |
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: 557.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 439 VKMPYQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENgEWGRMNARERGRLMYRLADLLE 518
Cdd:cd07144 4 YDQPTGLFINNEFVKSSDGETIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFES-WWSKVTGEERGELLDKLADLVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 519 ENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqarpNRNLTFTKKEPLGVCAIIIPWNYPL 598
Cdd:cd07144 83 KNRDLLAAIEALDSGKPYHSNALGDLDEIIAVIRYYAGWADKIQGKTIPTS----PNKLAYTLHEPYGVCGQIIPWNYPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 599 MMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQ 678
Cdd:cd07144 159 AMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAGFPPGVVNIIPGYGAVAGSALAEHPDVDKIAFTGSTATGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 679 IMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKK-MKI 757
Cdd:cd07144 239 VMKA-AAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQnYKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 758 GDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGG---RQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVIS 834
Cdd:cd07144 318 GSPFDDDTVVGPQVSKTQYDRVLSYIEKGKKEGAKLVYGGekaPEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVIS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 835 KFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYL 914
Cdd:cd07144 398 KFK--TYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYT 475
|
....*
gi 238814322 915 KTKTV 919
Cdd:cd07144 476 QTKAV 480
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
462-921 |
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: 551.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTlALK 541
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEGGAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIR-ETR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSVQTFRYFAGWCDKIQGSTIPINqaRPNRnLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07114 80 AQVRYLAEWYRYYAGLADKIEGAVIPVD--KGDY-LNFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 622 VTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPL 701
Cdd:cd07114 157 HTPASTLELAKLAEEAGFPPGVVNVVTGFGPETGEALVEHPLVAKIAFTGGTETGRHIARAAA-ENLAPVTLELGGKSPN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 702 IIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQ 781
Cdd:cd07114 236 IVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQLEKVER 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 782 YCETGVKEGATLVYGGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLAS 857
Cdd:cd07114 316 YVARAREEGARVLTGGERPSGAdlgaGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFD--DEEEAIALANDSEYGLAA 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 858 GVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07114 394 GIWTRDLARAHRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSVWI 457
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
442-919 |
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: 543.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 442 PYQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEENQ 521
Cdd:cd07142 3 HTKLFINGQFVDAASGKTFPTIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDEGPWPRMTGYERSRILLRFADLLEKHA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 522 EELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQArpnrNLTFTKKEPLGVCAIIIPWNYPLMML 601
Cdd:cd07142 83 DELAALETWDNGKPYEQARYAEVPLAARLFRYYAGWADKIHGMTLPADGP----HHVYTLHEPIGVVGQIIPWNFPLLMF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMK 681
Cdd:cd07142 159 AWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAGLPDGVLNIVTGFGPTAGAAIASHMDVDKVAFTGSTEVGKIIMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 682 SCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPL 761
Cdd:cd07142 239 LAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 762 DRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDI 841
Cdd:cd07142 319 RKGVEQGPQVDKEQFEKILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFK--TV 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814322 842 DGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:cd07142 397 DEVIKRANNSKYGLAAGVFSKNIDTANTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
457-919 |
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: 541.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 457 GKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVY 536
Cdd:cd07112 1 GETFATINPATGRVLAEVAACDAADVDRAVAAARRAFESGVWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 537 TLALKTHIGMSVQTFRYFAGWCDKIQGSTIPInqarPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLV 616
Cdd:cd07112 81 SDALAVDVPSAANTFRWYAEAIDKVYGEVAPT----GPDALALITREPLGVVGAVVPWNFPLLMAAWKIAPALAAGNSVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 617 LKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVSNLKKVSLELG 696
Cdd:cd07112 157 LKPAEQSPLTALRLAELALEAGLPAGVLNVVPGFGHTAGEALGLHMDVDALAFTGSTEVGRRFLEYSGQSNLKRVWLECG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 697 GKSPLIIFNDCE-LDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAH 775
Cdd:cd07112 237 GKSPNIVFADAPdLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVSEAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 776 LEKLLQYCETGVKEGATLVYGGRQVQR--PGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFqnGDIDGVLQRANSTEY 853
Cdd:cd07112 317 FDKVLGYIESGKAEGARLVAGGKRVLTetGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITF--DSEEEAVALANDSVY 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238814322 854 GLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:cd07112 395 GLAASVWTSDLSRAHRVARRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
462-919 |
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: 535.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALK 541
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEA--WSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSVQTFRYFAGWCDKIQGSTIPInqaRPnRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07115 79 LDVPRAADTFRYYAGWADKIEGEVIPV---RG-PFLNYTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 622 VTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVsNLKKVSLELGGKSPL 701
Cdd:cd07115 155 LTPLSALRIAELMAEAGFPAGVLNVVTGFGEVAGAALVEHPDVDKITFTGSTAVGRKIMQGAAG-NLKRVSLELGGKSAN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 702 IIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQ 781
Cdd:cd07115 234 IVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRVLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 782 YCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFqnGDIDGVLQRANSTEYGLASGVFT 861
Cdd:cd07115 314 YVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRF--RDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 238814322 862 RDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:cd07115 392 RDLGRAHRVAAALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSV 449
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
446-919 |
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: 533.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:cd07119 1 YIDGEWVEAASGKTRDIINPANGEVIATVPEGTAEDAKRAIAAARRAFDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPinqaRPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKS 605
Cdd:cd07119 81 RLETLNTGKTLRES-EIDIDDVANCFRYYAGLATKETGEVYD----VPPHVISRTVREPVGVCGLITPWNYPLLQAAWKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 606 AACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAv 685
Cdd:cd07119 156 APALAAGNTVVIKPSEVTPLTTIALFELIEEAGLPAGVVNLVTGSGATVGAELAESPDVDLVSFTGGTATGRSIMRAAA- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 SNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07119 235 GNVKKVALELGGKNPNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 766 DHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDI 841
Cdd:cd07119 315 EMGPLVSAEHREKVLSYIQLGKEEGARLVCGGKRPTGDelakGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFD--TE 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814322 842 DGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:cd07119 393 EEAIRLANDTPYGLAGAVWTKDIARANRVARRLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
439-919 |
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: 532.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 439 VKMPYQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENgEWGR-MNARERGRLMYRLADLL 517
Cdd:cd07143 3 YEQPTGLFINGEFVDSVHGGTVKVYNPSTGKLITKIAEATEADVDIAVEVAHAAFET-DWGLkVSGSKRGRCLSKLADLM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 518 EENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARpnrnLTFTKKEPLGVCAIIIPWNYP 597
Cdd:cd07143 82 ERNLDYLASIEALDNGKTFGTAKRVDVQASADTFRYYGGWADKIHGQVIETDIKK----LTYTRHEPIGVCGQIIPWNFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 598 LMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGK 677
Cdd:cd07143 158 LLMCAWKIAPALAAGNTIVLKPSELTPLSALYMTKLIPEAGFPPGVINVVSGYGRTCGNAISSHMDIDKVAFTGSTLVGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 678 QIMKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKI 757
Cdd:cd07143 238 KVMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 758 GDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQ 837
Cdd:cd07143 318 GDPFAEDTFQGPQVSQIQYERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 838 ngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTK 917
Cdd:cd07143 398 --TEEEAIKRANDSTYGLAAAVFTNNINNAIRVANALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIK 475
|
..
gi 238814322 918 TV 919
Cdd:cd07143 476 AV 477
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
431-919 |
1.46e-180 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 531.32 E-value: 1.46e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 431 SKEVNEIMVKMP----YQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARER 506
Cdd:PLN02766 5 GNCGGASGVKVPeikfTKLFINGEFVDAASGKTFETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDHGPWPRMSGFER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 507 GRLMYRLADLLEENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPInqARPNRNltFTKKEPLG 586
Cdd:PLN02766 85 GRIMMKFADLIEEHIEELAALDTIDAGKLFALGKAVDIPAAAGLLRYYAGAADKIHGETLKM--SRQLQG--YTLKEPIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 587 VCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRK 666
Cdd:PLN02766 161 VVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTPLSALFYAHLAKLAGVPDGVINVVTGFGPTAGAAIASHMDVDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 667 LGFTGSTPIGKQIMKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVT 746
Cdd:PLN02766 241 VSFTGSTEVGRKIMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 747 RVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEES 826
Cdd:PLN02766 321 KLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 827 FGPIMVISKFQNgdIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLG 906
Cdd:PLN02766 401 FGPVMSLMKFKT--VEEAIKKANNTKYGLAAGIVTKDLDVANTVSRSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQG 478
|
490
....*....|...
gi 238814322 907 EEALNEYLKTKTV 919
Cdd:PLN02766 479 MDALDKYLQVKSV 491
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
463-921 |
1.56e-174 |
|
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: 513.52 E-value: 1.56e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 463 INPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFK--TWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEA-RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 543 HIGMSVQTFRYFAGWCDKIQGSTIPinQARPNRNLtFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07103 79 EVDYAASFLEWFAEEARRIYGRTIP--SPAPGKRI-LVIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 623 TPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLI 702
Cdd:cd07103 156 TPLSALALAELAEEAGLPAGVLNVVTGSPAEIGEALCASPRVRKISFTGSTAVGKLLMAQAA-DTVKRVSLELGGNAPFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 703 IFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQY 782
Cdd:cd07103 235 VFDDADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 783 CETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTR 862
Cdd:cd07103 315 VEDAVAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFD--TEDEVIARANDTPYGLAAYVFTR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 238814322 863 DINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07103 393 DLARAWRVAEALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
462-922 |
8.01e-171 |
|
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: 504.53 E-value: 8.01e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlK 541
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQK--EWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEA-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSVQTFRYFAGWCDKIQGSTIPInqarPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07090 78 VDIDSSADCLEYYAGLAPTLSGEHVPL----PGGSFAYTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 622 VTPLTALKFAELSVKAGFPKGVINIIPGsGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPL 701
Cdd:cd07090 154 FTPLTALLLAEILTEAGLPDGVFNVVQG-GGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAA-KGIKHVTLELGGKSPL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 702 IIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQ 781
Cdd:cd07090 232 IIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 782 YCETGVKEGATLVYGGRQVQ-----RPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQNgdIDGVLQRANSTEYGLA 856
Cdd:cd07090 312 YIESAKQEGAKVLCGGERVVpedglENGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDT--EEEVIRRANDTTYGLA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238814322 857 SGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTLE 922
Cdd:cd07090 390 AGVFTRDLQRAHRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYVE 455
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
462-921 |
1.63e-169 |
|
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: 500.94 E-value: 1.63e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALK 541
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFP--GWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITLART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSVQTFRYFAGWCDKIQGSTIPinqaRPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07093 79 RDIPRAAANFRFFADYILQLDGESYP----QDGGALNYVLRQPVGVAGLITPWNLPLMLLTWKIAPALAFGNTVVLKPSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 622 VTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKSPL 701
Cdd:cd07093 155 WTPLTAWLLAELANEAGLPPGVVNVVHGFGPEAGAALVAHPDVDLISFTGETATGRTIMRA-AAPNLKPVSLELGGKNPN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 702 IIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQ 781
Cdd:cd07093 234 IVFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 782 YCETGVKEGATLVYGGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLAS 857
Cdd:cd07093 314 YVELARAEGATILTGGGRPELPdlegGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFD--DEEEAIELANDTPYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 858 GVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07093 392 YVWTRDLGRAHRVARRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
438-922 |
8.68e-169 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 500.56 E-value: 8.68e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 438 MVKMP-YQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADL 516
Cdd:PRK13252 1 MSRQPlQSLYIDGAYVEATSGETFEVINPATGEVLATVQAATPADVEAAVASAKQGQK--IWAAMTAMERSRILRRAVDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 517 LEENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQArpnrNLTFTKKEPLGVCAIIIPWNY 596
Cdd:PRK13252 79 LRERNDELAALETLDTGKPIQETSVVDIVTGADVLEYYAGLAPALEGEQIPLRGG----SFVYTRREPLGVCAGIGAWNY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 597 PLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIaGQRLSEHPDIRKLGFTGSTPIG 676
Cdd:PRK13252 155 PIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGLPDGVFNVVQGDGRV-GAWLTEHPDIAKVSFTGGVPTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 677 KQIMKSCAVSnLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMK 756
Cdd:PRK13252 234 KKVMAAAAAS-LKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 757 IGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQR----PGFFMEPTVFTDVEDYMYLAKEESFGPIMV 832
Cdd:PRK13252 313 IGDPMDPATNFGPLVSFAHRDKVLGYIEKGKAEGARLLCGGERLTEggfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 833 ISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNE 912
Cdd:PRK13252 393 VLTFD--DEDEVIARANDTEYGLAAGVFTADLSRAHRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEH 470
|
490
....*....|
gi 238814322 913 YLKTKTVTLE 922
Cdd:PRK13252 471 YTQIKSVQVE 480
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
439-919 |
5.09e-166 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 495.10 E-value: 5.09e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 439 VKMPY-QCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLL 517
Cdd:PLN02466 53 VQVSYtQLLINGQFVDAASGKTFPTLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDEGPWPKMTAYERSRILLRFADLL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 518 EENQEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPinqARPNRNLTfTKKEPLGVCAIIIPWNYP 597
Cdd:PLN02466 133 EKHNDELAALETWDNGKPYEQSAKAELPMFARLFRYYAGWADKIHGLTVP---ADGPHHVQ-TLHEPIGVAGQIIPWNFP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 598 LMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGK 677
Cdd:PLN02466 209 LLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGLPPGVLNVVSGFGPTAGAALASHMDVDKLAFTGSTDTGK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 678 QIMKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKI 757
Cdd:PLN02466 289 IVLELAAKSNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVV 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 758 GDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQ 837
Cdd:PLN02466 369 GDPFKKGVEQGPQIDSEQFEKILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 838 ngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTK 917
Cdd:PLN02466 449 --DLDEVIRRANNTRYGLAAGVFTQNLDTANTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVK 526
|
..
gi 238814322 918 TV 919
Cdd:PLN02466 527 AV 528
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
446-917 |
1.42e-160 |
|
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: 478.54 E-value: 1.42e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFenGEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:TIGR01804 1 FIDGEYVEDSAGTTREIINPANGEVIATVHAATPEDVERAIAAARRAQ--GEWAAMSPMERGRILRRAADLIRERNEELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPInqarPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKS 605
Cdd:TIGR01804 79 KLETLDTGKTLQETIVADMDSGADVFEFFAGLAPALNGEIIPL----GGPSFAYTIREPLGVCVGIGAWNYPLQIASWKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 606 AACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKScAV 685
Cdd:TIGR01804 155 APALAAGNAMVFKPSENTPLTALKVAEIMEEAGLPKGVFNVVQGDGAEVGPLLVNHPDVAKVSFTGGVPTGKKIMAA-AA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 SNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:TIGR01804 234 GHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGNFFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPFDEAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 766 DHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDI 841
Cdd:TIGR01804 314 EMGPLISAAHRDKVLSYIEKGKAEGATLATGGGRPENVglqnGFFVEPTVFADCTDDMTIVREEIFGPVMTVLTFS--DE 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238814322 842 DGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTK 917
Cdd:TIGR01804 392 DEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGTVWINTYNLYPAEAPFGGYKQSGIGRENGKAALAHYTEVK 467
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
463-921 |
3.43e-153 |
|
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: 459.01 E-value: 3.43e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 463 INPTDGSTICKVSYASLADVDKAVAAAKDAFENGeWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESG-WLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQA-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 543 HIGMSVQTFRYFAGWCDKIQGSTIPINQArpnrNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07109 80 DVEAAARYFEYYGGAADKLHGETIPLGPG----YFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 623 TPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLI 702
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALNVVTGLGAEAGAALVAHPGVDHISFTGSVETGIAVMRAAA-ENVVPVTLELGGKSPQI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 703 IFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRsTDHGPQNHKAHLEKLLQY 782
Cdd:cd07109 235 VFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLED-PDLGPLISAKQLDRVEGF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 783 CETGVKEGATLVYGGRQVQRP---GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFqnGDIDGVLQRANSTEYGLASGV 859
Cdd:cd07109 314 VARARARGARIVAGGRIAEGApagGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPF--DDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238814322 860 FTRDINKAMYVSEKLEAGTVFINTYNKT-DVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07109 392 WTRDGDRALRVARRLRAGQVFVNNYGAGgGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
493-921 |
5.63e-149 |
|
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: 447.94 E-value: 5.63e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 493 FENGEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIpiNQAR 572
Cdd:cd07118 32 FDKGPWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQA-RGEIEGAADLWRYAASLARTLHGDSY--NNLG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 573 PNRnLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGG 652
Cdd:cd07118 109 DDM-LGLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEFTSGTTLMLAELLIEAGLPAGVVNIVTGYGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 653 IAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAG 732
Cdd:cd07118 188 TVGQAMTEHPDVDMVSFTGSTRVGKAIAAAAA-RNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 733 RLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQV-QRPGFFMEPTV 811
Cdd:cd07118 267 RLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEGATLLLGGERLaSAAGLFYQPTI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 812 FTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAA 891
Cdd:cd07118 347 FTDVTPDMAIAREEIFGPVLSVLTFD--TVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVNTFLDGSPEL 424
|
410 420 430
....*....|....*....|....*....|
gi 238814322 892 PFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07118 425 PFGGFKQSGIGRELGRYGVEEYTELKTVHL 454
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
497-921 |
5.85e-149 |
|
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: 444.75 E-value: 5.85e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGWCDKIQGSTIPINqarPNRN 576
Cdd:cd06534 9 AWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEAL-GEVARAIDTFRYAAGLADKLGGPELPSP---DPGG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 577 LTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQ 656
Cdd:cd06534 85 EAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVNVVPGGGDEVGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 657 RLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFV 736
Cdd:cd06534 165 ALLSHPRVDKISFTGSTAVGKAIMKAAA-ENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASRLLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 737 EESIHDEFVTRVVeeikkmkigdpldrstdhgpqnhkahlekllqycetgvkegatlvyggrqvqrpgffmepTVFTDVE 816
Cdd:cd06534 244 HESIYDEFVEKLV------------------------------------------------------------TVLVDVD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 817 DYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNK-TDVAAPFGG 895
Cdd:cd06534 264 PDMPIAQEEIFGPVLPVIRFK--DEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIgVGPEAPFGG 341
|
410 420
....*....|....*....|....*.
gi 238814322 896 VKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd06534 342 VKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
443-923 |
1.56e-148 |
|
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: 447.95 E-value: 1.56e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 443 YQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQE 522
Cdd:cd07559 1 YDNFINGEWVAPSKGEYFDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKT--WGKTSVAERANILNKIADRIEENLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 523 ELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQarpnRNLTFTKKEPLGVCAIIIPWNYPLMMLA 602
Cdd:cd07559 79 LLAVAETLDNGKPIRETLAADIPLAIDHFRYFAGVIRAQEGSLSEIDE----DTLSYHFHEPLGVVGQIIPWNFPLLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKS 682
Cdd:cd07559 155 WKLAPALAAGNTVVLKPASQTPLSILVLMEL-IGDLLPKGVVNVVTGFGSEAGKPLASHPRIAKLAFTGSTTVGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 683 cAVSNLKKVSLELGGKSPLIIFND-----CELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKI 757
Cdd:cd07559 234 -AAENLIPVTLELGGKSPNIFFDDamdadDDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 758 GDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVI 833
Cdd:cd07559 313 GNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGgldkGYFYEPTLIKGGNNDMRIFQEEIFGPVLAV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 834 SKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEY 913
Cdd:cd07559 393 ITFK--DEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRETHKMMLDHY 470
|
490
....*....|
gi 238814322 914 LKTKTVTLEY 923
Cdd:cd07559 471 QQTKNILVSY 480
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
446-921 |
1.64e-147 |
|
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: 444.79 E-value: 1.64e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:cd07088 1 YINGEFVPSSSGETIDVLNPATGEVVATVPAATAEDADRAVDAAEAAQK--AWERLPAIERAAYLRKLADLIRENADELA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNRNLtFTKKEPLGVCAIIIPWNYPLMMLAWKS 605
Cdd:cd07088 79 KLIVEEQGKTLSLA-RVEVEFTADYIDYMAEWARRIEGEIIP--SDRPNENI-FIFKVPIGVVAGILPWNFPFFLIARKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 606 AACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAV 685
Cdd:cd07088 155 APALVTGNTIVIKPSEETPLNALEFAELVDEAGLPAGVLNIVTGRGSVVGDALVAHPKVGMISLTGSTEAGQKIMEAAAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 sNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07088 235 -NITKVSLELGGKAPAIVMKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAAT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 766 DHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQ-RPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGV 844
Cdd:cd07088 314 DMGPLVNEAALDKVEEMVERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFS--SLDEA 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238814322 845 LQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07088 392 IELANDSEYGLTSYIYTENLNTAMRATNELEFGETYINRENFEAMQGFHAGWKKSGLGGADGKHGLEEYLQTKVVYL 468
|
|
| FMT_core_FDH_N |
cd08647 |
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family ... |
23-225 |
2.65e-147 |
|
10-formyltetrahydrofolate dehydrogenase (FDH), N-terminal hydrolase domain; This family represents the N-terminal hydrolase domain of the bifunctional protein 10-formyltetrahydrofolate dehydrogenase (FDH). This domain contains a 10-formyl-tetrahydrofolate (10-formyl-THF) binding site and shares sequence homology and structural topology with other enzymes utilizing this substrate. This domain functions as a hydrolase, catalyzing the conversion of 10-formyl-THF, a precursor for nucleotide biosynthesis, to tetrahydrofolate (THF). The overall FDH reaction mechanism is a coupling of two sequential reactions, a hydrolase and a formyl dehydrogenase, bridged by a substrate transfer step. The N-terminal hydrolase domain removes the formyl group from 10-formyl-THF and the C-terminal NADP-dependent dehydrogenase domain then reduces the formyl group to carbon dioxide. The two catalytic domains are connected by a third intermediate linker domain that transfers the formyl group, covalently attached to the sulfhydryl group of the phosphopantetheine arm, from the N-terminal domain to the C-terminal domain.
Pssm-ID: 187716 [Multi-domain] Cd Length: 203 Bit Score: 433.80 E-value: 2.65e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 23 LKLALIGQSLFGQEVYSHLRKEGHRVVGVFTVPDKDGKADPLALAAEKDGTPVFKLPKWRVKGKTIKEVAEAYRSVGAEL 102
Cdd:cd08647 1 MKIAVIGQSLFGQEVYKELRKEGHEVVGVFTIPDKDGKADPLALEAEKDGVPVFKFPRWRAKGQAIPEVVAKYKALGAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 103 NVLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTV 182
Cdd:cd08647 81 NVLPFCSQFIPMEVIDAPKHGSIIYHPSILPRHRGASAINWTLIHGDKKAGFTIFWADDGLDTGPILLQKECDVLPNDTV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 238814322 183 DALYNRFLFPEGIKAMVEAVQLIADGKAPRIPQPEEGATYEGI 225
Cdd:cd08647 161 DTLYNRFLYPEGIKAMVEAVRLIAEGKAPRIPQPEEGATYEGI 203
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
446-921 |
2.70e-146 |
|
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: 441.56 E-value: 2.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:cd07138 2 YIDGAWVAPAGTETIDVINPATEEVIGTVPLGTAADVDRAVAAARRAFP--AWSATSVEERAALLERIAEAYEARADELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAG------WCDKIQGSTIpinqarpnrnltftKKEPLGVCAIIIPWNYPLM 599
Cdd:cd07138 80 QAITLEMGAPITLARAAQVGLGIGHLRAAADalkdfeFEERRGNSLV--------------VREPIGVCGLITPWNWPLN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 600 MLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQI 679
Cdd:cd07138 146 QIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGLPAGVFNLVNGDGPVVGEALSAHPDVDMVSFTGSTRAGKRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 680 MKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGD 759
Cdd:cd07138 226 AEA-AADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 760 PLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGrqVQRP-----GFFMEPTVFTDVEDYMYLAKEESFGPIMVIS 834
Cdd:cd07138 305 PRDPATTLGPLASAAQFDRVQGYIQKGIEEGARLVAGG--PGRPeglerGYFVKPTVFADVTPDMTIAREEIFGPVLSII 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 835 KFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINtYNKTDVAAPFGGVKQSGFGKDLGEEALNEYL 914
Cdd:cd07138 383 PYD--DEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHIN-GAAFNPGAPFGGYKQSGNGREWGRYGLEEFL 459
|
....*..
gi 238814322 915 KTKTVTL 921
Cdd:cd07138 460 EVKSIQG 466
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
463-920 |
3.62e-146 |
|
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: 440.61 E-value: 3.62e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 463 INPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALKT 542
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPS--WRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 543 HIGMSVQTFRYFAGWCDKIQGSTIpiNQARPNRnLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07092 80 ELPGAVDNFRFFAGAARTLEGPAA--GEYLPGH-TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 623 TPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKSPLI 702
Cdd:cd07092 157 TPLTTLLLAEL-AAEVLPPGVVNVVCGGGASAGDALVAHPRVRMVSLTGSVRTGKKVARA-AADTLKRVHLELGGKAPVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 703 IFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQY 782
Cdd:cd07092 235 VFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 783 CEtGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTR 862
Cdd:cd07092 315 VE-RAPAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFD--DEDEAIELANDVEYGLASSVWTR 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 238814322 863 DINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVT 920
Cdd:cd07092 392 DVGRAMRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVM 449
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
446-921 |
4.66e-146 |
|
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: 441.24 E-value: 4.66e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:cd07139 2 FIGGRWVAPSGSETIDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWcdkiqGSTIPINQARP--NRNLTFTKKEPLGVCAIIIPWNYPLMMLAW 603
Cdd:cd07139 82 RLWTAENGMPISWSRRAQGPGPAALLRYYAAL-----ARDFPFEERRPgsGGGHVLVRREPVGVVAAIVPWNAPLFLAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 604 KSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGsGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSC 683
Cdd:cd07139 157 KIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGLPPGVVNVVPA-DREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 684 AvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:cd07139 236 G-ERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 764 STDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGrqvQRP-----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQn 838
Cdd:cd07139 315 ATQIGPLASARQRERVEGYIAKGRAEGARLVTGG---GRPagldrGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYD- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 839 gDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYnKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKT 918
Cdd:cd07139 391 -DEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKS 468
|
...
gi 238814322 919 VTL 921
Cdd:cd07139 469 IYL 471
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
441-919 |
1.30e-143 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 435.11 E-value: 1.30e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 441 MPYQCFINGQFTDADdGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEEN 520
Cdd:PRK13473 1 MQTKLLINGELVAGE-GEKQPVYNPATGEVLAEIAEASAAQVDAAVAAADAAFP--EWSQTTPKERAEALLKLADAIEEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 521 QEELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQG-----------STIpinqarpnrnltftKKEPLGVCA 589
Cdd:PRK13473 78 ADEFARLESLNCGKPLHLALNDEIPAIVDVFRFFAGAARCLEGkaageyleghtSMI--------------RRDPVGVVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 590 IIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAgFPKGVINIIPGSGGIAGQRLSEHPDIRKLGF 669
Cdd:PRK13473 144 SIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADI-LPPGVLNVVTGRGATVGDALVGHPKVRMVSL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 670 TGSTPIGKQIMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVV 749
Cdd:PRK13473 223 TGSIATGKHVLSA-AADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 750 EEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEG-ATLVYGGRQVQRPGFFMEPTVFTDV--EDYMYlaKEES 826
Cdd:PRK13473 302 AAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGArqDDEIV--QREV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 827 FGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLG 906
Cdd:PRK13473 380 FGPVVSVTPFD--DEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKQSGYGKDMS 457
|
490
....*....|...
gi 238814322 907 EEALNEYLKTKTV 919
Cdd:PRK13473 458 LYGLEDYTVVRHV 470
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
446-919 |
1.25e-142 |
|
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: 432.44 E-value: 1.25e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKtyDTINPTDGS-TICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEEL 524
Cdd:cd07097 4 YIDGEWVAGGDGE--ENRNPSDTSdVVGKYARASAEDADAAIAAAAAAFP--AWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 525 ATIEALDSGAvyTLAL-KTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNRNLtFTKKEPLGVCAIIIPWNYPLMMLAW 603
Cdd:cd07097 80 ARLLTREEGK--TLPEaRGEVTRAGQIFRYYAGEALRLSGETLP--STRPGVEV-ETTREPLGVVGLITPWNFPIAIPAW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 604 KSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSc 683
Cdd:cd07097 155 KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGLPAGVFNLVMGSGSEVGQALVEHPDVDAVSFTGSTAVGRRIAAA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 684 AVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:cd07097 234 AAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 764 STDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRP--GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDI 841
Cdd:cd07097 314 GVDIGPVVSERQLEKDLRYIEIARSEGAKLVYGGERLKRPdeGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVR--DY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 842 DGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN-TYNKTDVAAPFGGVKQSGFG-KDLGEEALNEYLKTKTV 919
Cdd:cd07097 392 DEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAGVVMVNlPTAGVDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
446-923 |
2.18e-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: 429.17 E-value: 2.18e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEnGEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:cd07113 3 FIDGRPVAGQSEKRLDITNPATEQVIASVASATEADVDAAVASAWRAFV-SAWAKTTPAERGRILLRLADLIEQHGEELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPN--RNLTFTKKEPLGVCAIIIPWNYPLMMLAW 603
Cdd:cd07113 82 QLETLCSGKSIHLSRAFEVGQSANFLRYFAGWATKINGETLAPSIPSMQgeRYTAFTRREPVGVVAGIVPWNFSVMIAVW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 604 KSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIaGQRLSEHPDIRKLGFTGSTPIGKQIMKSc 683
Cdd:cd07113 162 KIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAGIPDGVLNVVNGKGAV-GAQLISHPDVAKVSFTGSVATGKKIGRQ- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 684 AVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:cd07113 240 AASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 764 STDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPT--VFTDVEDYMYlaKEESFGPIMVISKFQNGdi 841
Cdd:cd07113 320 SVMFGPLANQPHFDKVCSYLDDARAEGDEIVRGGEALAGEGYFVQPTlvLARSADSRLM--REETFGPVVSFVPYEDE-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 842 DGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07113 396 EELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
..
gi 238814322 922 EY 923
Cdd:cd07113 476 RY 477
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
446-917 |
1.52e-139 |
|
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: 424.50 E-value: 1.52e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:cd07111 25 FINGKWVKPENRKSFPTINPATGEVLASVLQAEEEDVDAAVAAARTAFES--WSALPGHVRARHLYRIARHIQKHQRLFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQgstipinQARPNRnltftkkEPLGVCAIIIPWNYPLMMLAWKS 605
Cdd:cd07111 103 VLESLDNGKPIRESRDCDIPLVARHFYHHAGWAQLLD-------TELAGW-------KPVGVVGQIVPWNFPLLMLAWKI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 606 AACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGiAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAV 685
Cdd:cd07111 169 CPALAMGNTVVLKPAEYTPLTALLFAEICAEAGLPPGVLNIVTGNGS-FGSALANHPGVDKVAFTGSTEVGRALRRATAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 SNlKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07111 248 TG-KKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 766 DHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQNGdiDGVL 845
Cdd:cd07111 327 DMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTA--KEAV 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238814322 846 QRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTK 917
Cdd:cd07111 405 ALANNTPYGLAASVWSENLSLALEVALSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYLRPS 476
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
462-923 |
2.22e-137 |
|
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: 417.93 E-value: 2.22e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTlALK 541
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFP--EWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVS-AML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSVQTFRYFAGWCDKIQGSTIPInqarPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07107 78 GDVMVAAALLDYFAGLVTELKGETIPV----GGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 622 VTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKSPL 701
Cdd:cd07107 154 QAPLSALRLAEL-AREVLPPGVFNILPGDGATAGAALVRHPDVKRIALIGSVPTGRAIMRA-AAEGIKHVTLELGGKNAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 702 IIFNDCELDKAVR-MGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLL 780
Cdd:cd07107 232 IVFPDADPEAAADaAVAGMNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVSRQQYDRVM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 781 QYCETGVKEGATLVYGGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLA 856
Cdd:cd07107 312 HYIDSAKREGARLVTGGGRPEGPalegGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWR--DEAEMVAQANGVEYGLT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238814322 857 SGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTLEY 923
Cdd:cd07107 390 AAIWTNDISQAHRTARRVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNVRL 456
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
443-919 |
1.14e-136 |
|
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: 416.86 E-value: 1.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 443 YQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQE 522
Cdd:cd07117 1 YGLFINGEWVKGSSGETIDSYNPANGETLSEITDATDADVDRAVKAAQEAFKT--WRKTTVAERANILNKIADIIDENKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 523 ELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINQarpnRNLTFTKKEPLGVCAIIIPWNYPLMMLA 602
Cdd:cd07117 79 LLAMVETLDNGKPIRETRAVDIPLAADHFRYFAGVIRAEEGSANMIDE----DTLSIVLREPIGVVGQIIPWNFPFLMAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKS 682
Cdd:cd07117 155 WKLAPALAAGNTVVIKPSSTTSLSLLELAKI-IQDVLPKGVVNIVTGKGSKSGEYLLNHPGLDKLAFTGSTEVGRDVAIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 683 cAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLD 762
Cdd:cd07117 234 -AAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 763 RSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQn 838
Cdd:cd07117 313 PDTQMGAQVNKDQLDKILSYVDIAKEEGAKILTGGHRLTENgldkGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFK- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 839 gDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKT 918
Cdd:cd07117 392 -TEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRETHKSMLDAYTQMKN 470
|
.
gi 238814322 919 V 919
Cdd:cd07117 471 I 471
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
462-920 |
4.58e-136 |
|
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: 414.83 E-value: 4.58e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALk 541
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFP--RWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSVQTFRYFAGWCDKI---QGSTIPINQARPNRNltfTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLK 618
Cdd:cd07110 78 WDVDDVAGCFEYYADLAEQLdakAERAVPLPSEDFKAR---VRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 619 PAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGK 698
Cdd:cd07110 155 PSELTSLTELELAEIAAEAGLPPGVLNVVTGTGDEAGAPLAAHPGIDKISFTGSTATGSQVMQAAA-QDIKPVSLELGGK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 699 SPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEK 778
Cdd:cd07110 234 SPIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 779 LLQYCETGVKEGATLVYGGRQVQ--RPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLA 856
Cdd:cd07110 314 VLSFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFA--TEDEAIALANDSEYGLA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 857 SGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVT 920
Cdd:cd07110 392 AAVISRDAERCDRVAEALEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQIT 455
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
463-919 |
4.90e-136 |
|
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: 414.72 E-value: 4.90e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 463 INPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWgRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALKT 542
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDW-STDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMTARAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 543 HIGMSVQTFRYFAGWCDKIQGS-TIPINQARPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07089 81 QVDGPIGHLRYFADLADSFPWEfDLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 622 VTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPL 701
Cdd:cd07089 161 DTPLSALLLGEIIAETDLPAGVVNVVTGSDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAA-ATLKRVLLELGGKSAN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 702 IIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQ 781
Cdd:cd07089 240 IVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRVEG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 782 YCETGVKEGATLVYGGRqvqRP-----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLA 856
Cdd:cd07089 320 YIARGRDEGARLVTGGG---RPagldkGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYD--DDDEAVRIANDSDYGLS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238814322 857 SGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:cd07089 395 GGVWSADVDRAYRVARRIRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSI 457
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
446-922 |
6.98e-135 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 413.14 E-value: 6.98e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:PRK09847 23 FINGEYTAAAENETFETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERGDWSLSSPAKRKAVLNKLADLMEAHAEELA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqarpNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKS 605
Cdd:PRK09847 103 LLETLDTGKPIRHSLRDDIPGAARAIRWYAEAIDKVYGEVATTS----SHELAMIVREPVGVIAAIVPWNFPLLLTCWKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 606 AACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAV 685
Cdd:PRK09847 179 GPALAAGNSVILKPSEKSPLSAIRLAGLAKEAGLPDGVLNVVTGFGHEAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 SNLKKVSLELGGKSPLIIFNDC-ELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRS 764
Cdd:PRK09847 259 SNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 765 TDHGPQNHKAHLEKLLQYCETGVKEGaTLVYGGRQVQRPGfFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQNGdiDGV 844
Cdd:PRK09847 339 TTMGTLIDCAHADSVHSFIREGESKG-QLLLDGRNAGLAA-AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSE--EQA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 845 LQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEY--LKTKTVTLE 922
Cdd:PRK09847 415 LQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFteLKTIWISLE 494
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
444-921 |
2.87e-134 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 411.39 E-value: 2.87e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 444 QCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEE 523
Cdd:PLN02278 26 QGLIGGKWTDAYDGKTFPVYNPATGEVIANVPCMGRAETNDAIASAHDAFP--SWSKLTASERSKILRRWYDLIIANKED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 524 LATIEALDSGAVYTLAL-KTHIGMSVqtFRYFAGWCDKIQGSTIPINQarPNRNLtFTKKEPLGVCAIIIPWNYPLMMLA 602
Cdd:PLN02278 104 LAQLMTLEQGKPLKEAIgEVAYGASF--LEYFAEEAKRVYGDIIPSPF--PDRRL-LVLKQPVGVVGAITPWNFPLAMIT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKS 682
Cdd:PLN02278 179 RKVGPALAAGCTVVVKPSELTPLTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVRKITFTGSTAVGKKLMAG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 683 CAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLD 762
Cdd:PLN02278 259 AA-ATVKRVSLELGGNAPFIVFDDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 763 RSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDID 842
Cdd:PLN02278 338 EGVTQGPLINEAAVQKVESHVQDAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFK--TEE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238814322 843 GVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:PLN02278 416 EAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCL 494
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
462-921 |
4.40e-134 |
|
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: 409.44 E-value: 4.40e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFenGEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAvytlALK 541
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAF--PEWAATPARERGKLLARIADALEARSEELARLLALETGN----ALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 TH----IGMSVQTFRYFAGWCDKIQGSTIPinqARPNRnLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVL 617
Cdd:cd07108 75 TQarpeAAVLADLFRYFGGLAGELKGETLP---FGPDV-LTYTVREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 618 KPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKScAVSNLKKVSLELGG 697
Cdd:cd07108 151 KAAEDAPLAVLLLAEI-LAQVLPAGVLNVITGYGEECGAALVDHPDVDKVTFTGSTEVGKIIYRA-AADRLIPVSLELGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 698 KSPLIIFNDCELDKAVR---MGMGavFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKA 774
Cdd:cd07108 229 KSPMIVFPDADLDDAVDgaiAGMR--FTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAIISEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 775 HLEKLLQYCETGVKE-GATLVYGGRQ----VQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRAN 849
Cdd:cd07108 307 QFAKVCGYIDLGLSTsGATVLRGGPLpgegPLADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWK--DEDEVIAMAN 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238814322 850 STEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLG-EEALNEYLKTKTVTL 921
Cdd:cd07108 385 DSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASlEGMLEHFTQKKTVNI 457
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
460-921 |
1.01e-132 |
|
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: 405.83 E-value: 1.01e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 460 YDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLA 539
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEEDVEKAIAAAKEGAK--EMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 540 LKtHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNRN-LTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLK 618
Cdd:cd07149 79 RK-EVDRAIETLRLSAEEAKRLAGETIPFDASPGGEGrIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 619 PAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKScavSNLKKVSLELGGK 698
Cdd:cd07149 158 PASQTPLSALKLAELLLEAGLPKGALNVVTGSGETVGDALVTDPRVRMISFTGSPAVGEAIARK---AGLKKVTLELGSN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 699 SPLIIFNDCELDKAV-RMGMGAvFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLE 777
Cdd:cd07149 235 AAVIVDADADLEKAVeRCVSGA-FANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 778 KLLQYCETGVKEGATLVYGGRqvqRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLAS 857
Cdd:cd07149 314 RIEEWVEEAVEGGARLLTGGK---RDGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFD--TLDEAIAMANDSPYGLQA 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238814322 858 GVFTRDINKAMYVSEKLEAGTVFIN---TYnKTDvAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07149 389 GVFTNDLQKALKAARELEVGGVMINdssTF-RVD-HMPYGGVKESGTGREGPRYAIEEMTEIKLVCF 453
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
498-921 |
1.64e-132 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 404.99 E-value: 1.64e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 498 WGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGwcdkiqgSTIP---INQARPN 574
Cdd:cd07106 35 WSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEA-QFEVGGAVAWLRYTAS-------LDLPdevIEDDDTR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 575 RnlTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAgFPKGVINIIPGSGGIa 654
Cdd:cd07106 107 R--VELRRKPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQEV-LPPGVLNVVSGGDEL- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 655 GQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVR-MGMGAvFFNKGENCIAAGR 733
Cdd:cd07106 183 GPALTSHPDIRKISFTGSTATGKKVMASAA-KTLKRVTLELGGNDAAIVLPDVDIDAVAPkLFWGA-FINSGQVCAAIKR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 734 LFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFT 813
Cdd:cd07106 261 LYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKGAKVLAGGEPLDGPGYFIPPTIVD 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 814 DVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPF 893
Cdd:cd07106 341 DPPEGSRIVDEEQFGPVLPVLKYS--DEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVWINTHGALDPDAPF 418
|
410 420
....*....|....*....|....*...
gi 238814322 894 GGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07106 419 GGHKQSGIGVEFGIEGLKEYTQTQVINI 446
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
446-923 |
3.35e-131 |
|
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: 402.88 E-value: 3.35e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEnGEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:cd07131 2 YIGGEWVDSASGETFDSRNPADLEEVVGTFPLSTASDVDAAVEAAREAF-PEWRKVPAPRRAEYLFRAAELLKKRKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNRNLtFTKKEPLGVCAIIIPWNYPLMMLAWKS 605
Cdd:cd07131 81 RLVTREMGKPLAEG-RGDVQEAIDMAQYAAGEGRRLFGETVP--SELPNKDA-MTRRQPIGVVALITPWNFPVAIPSWKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 606 AACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAV 685
Cdd:cd07131 157 FPALVCGNTVVFKPAEDTPACALKLVELFAEAGLPPGVVNVVHGRGEEVGEALVEHPDVDVVSFTGSTEVGERIGETCAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 SNlKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07131 237 PN-KRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 766 DHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQR----PGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFqnGDI 841
Cdd:cd07131 316 DMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEV--SSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 842 DGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINtyNKT---DVAAPFGGVKQSGFG-KDLGEEALNEYLKTK 917
Cdd:cd07131 394 EEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGITYVN--APTigaEVHLPFGGVKKSGNGhREAGTTALDAFTEWK 471
|
....*.
gi 238814322 918 TVTLEY 923
Cdd:cd07131 472 AVYVDY 477
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
444-920 |
2.61e-128 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 396.41 E-value: 2.61e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 444 QCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAF---ENGEWGRMNARERGRLMYRLADLLEEN 520
Cdd:PLN02467 9 QLFIGGEWREPVLGKRIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFkrnKGKDWARTTGAVRAKYLRAIAAKITER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 521 QEELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGWCDKIQGS-----TIPINQARpnrnlTFTKKEPLGVCAIIIPWN 595
Cdd:PLN02467 89 KSELAKLETLDCGKPLDEAA-WDMDDVAGCFEYYADLAEALDAKqkapvSLPMETFK-----GYVLKEPLGVVGLITPWN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 596 YPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPI 675
Cdd:PLN02467 163 YPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTGLGTEAGAPLASHPGVDKIAFTGSTAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 676 GKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKM 755
Cdd:PLN02467 243 GRKIMTAAA-QMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 756 KIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGR--QVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVI 833
Cdd:PLN02467 322 KISDPLEEGCRLGPVVSEGQYEKVLKFISTAKSEGATILCGGKrpEHLKKGFFIEPTIITDVTTSMQIWREEVFGPVLCV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 834 SKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEY 913
Cdd:PLN02467 402 KTFS--TEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVWINCSQPCFCQAPWGGIKRSGFGRELGEWGLENY 479
|
....*..
gi 238814322 914 LKTKTVT 920
Cdd:PLN02467 480 LSVKQVT 486
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
497-921 |
1.09e-127 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 391.89 E-value: 1.09e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYtlaLKTH--IGMSVQTFRYFAGWCDKIQGSTIPinQARPN 574
Cdd:cd07104 15 AWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTR---PKAAfeVGAAIAILREAAGLPRRPEGEILP--SDVPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 575 RnLTFTKKEPLGVCAIIIPWNYPLMmLAWKSAA-CLAAGNTLVLKPAQVTPLT-ALKFAELSVKAGFPKGVINIIPGSGG 652
Cdd:cd07104 90 K-ESMVRRVPLGVVGVISPFNFPLI-LAMRSVApALALGNAVVLKPDSRTPVTgGLLIAEIFEEAGLPKGVLNVVPGGGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 653 IAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVsNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAG 732
Cdd:cd07104 168 EIGDALVEHPRVRMISFTGSTAVGRHIGELAGR-HLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 733 RLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQ-NHKAhLEKLLQYCETGVKEGATLVYGGRqvqRPGFFMEPTV 811
Cdd:cd07104 247 RILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLiNERQ-VDRVHAIVEDAVAAGARLLTGGT---YEGLFYQPTV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 812 FTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN--TYNKtDV 889
Cdd:cd07104 323 LSDVTPDMPIFREEIFGPVAPVIPFD--DDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHINdqTVND-EP 399
|
410 420 430
....*....|....*....|....*....|..
gi 238814322 890 AAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07104 400 HVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
460-921 |
4.23e-125 |
|
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: 385.91 E-value: 4.23e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 460 YDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLA 539
Cdd:cd07150 1 FDDLNPADGSVYARVAVGSRQDAERAIAAAYDAFP--AWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 540 LkTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNRnLTFTKKEPLGVCAIIIPWNYPLMmLAWKSAA-CLAAGNTLVLK 618
Cdd:cd07150 79 W-FETTFTPELLRAAAGECRRVRGETLP--SDSPGT-VSMSVRRPLGVVAGITPFNYPLI-LATKKVAfALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 619 PAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVsNLKKVSLELGGK 698
Cdd:cd07150 154 PSEETPVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDPRVRMVTFTGSTAVGREIAEKAGR-HLKKITLELGGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 699 SPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEK 778
Cdd:cd07150 233 NPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 779 LLQYCETGVKEGATLVYGGRqvqRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASG 858
Cdd:cd07150 313 IKRQVEDAVAKGAKLLTGGK---YDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAK--DAEEALELANDTEYGLSAA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 859 VFTRDINKAMYVSEKLEAGTVFINTYNKTDVA-APFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07150 388 ILTNDLQRAFKLAERLESGMVHINDPTILDEAhVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
461-921 |
6.55e-125 |
|
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: 385.55 E-value: 6.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 461 DTINPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAl 540
Cdd:cd07145 2 EVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDV--MSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 541 KTHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNRN-LTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP 619
Cdd:cd07145 79 RVEVERTIRLFKLAAEEAKVLRGETIPVDAYEYNERrIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 620 AQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKS 699
Cdd:cd07145 159 SSNTPLTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVNMISFTGSTAVGLLIASK-AGGTGKKVALELGGSD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 700 PLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKL 779
Cdd:cd07145 238 PMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAVERM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 780 LQYCETGVKEGATLVYGGRQVQrpGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGV 859
Cdd:cd07145 318 ENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVK--DDEEAVEIANSTEYGLQASV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 860 FTRDINKAMYVSEKLEAGTVFIN--TYNKTDvAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07145 394 FTNDINRALKVARELEAGGVVINdsTRFRWD-NLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
497-919 |
6.38e-120 |
|
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: 371.41 E-value: 6.38e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAgwcDKI----QGSTIPINQAR 572
Cdd:cd07100 14 AWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEA-RAEVEKCAWICRYYA---ENAeaflADEPIETDAGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 573 pnrnlTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGV-INIIPGSG 651
Cdd:cd07100 90 -----AYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVfQNLLIDSD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 652 GIAgqRLSEHPDIRKLGFTGSTPIGKQImKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAA 731
Cdd:cd07100 165 QVE--AIIADPRVRGVTLTGSERAGRAV-AAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 732 GRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTV 811
Cdd:cd07100 242 KRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPTV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 812 FTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAA 891
Cdd:cd07100 322 LTDVTPGMPAYDEELFGPVAAVIKVK--DEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFINGMVKSDPRL 399
|
410 420
....*....|....*....|....*...
gi 238814322 892 PFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:cd07100 400 PFGGVKRSGYGRELGRFGIREFVNIKTV 427
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
445-923 |
2.35e-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: 369.20 E-value: 2.35e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 445 CFINGQFTDADdGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFenGEWGRMNARERGRLMYRLADLLEENQEEL 524
Cdd:cd07086 1 GVIGGEWVGSG-GETFTSRNPANGEPIARVFPASPEDVEAAVAAAREAF--KEWRKVPAPRRGEIVRQIGEALRKKKEAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 525 ATIEALDSGAVYTLALKthigmSVQTF----RYFAGWCDKIQGSTIPinQARPNRNLtFTKKEPLGVCAIIIPWNYPLMM 600
Cdd:cd07086 78 GRLVSLEMGKILPEGLG-----EVQEMidicDYAVGLSRMLYGLTIP--SERPGHRL-MEQWNPLGVVGVITAFNFPVAV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 601 LAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKA----GFPKGVINIIPGSGGIaGQRLSEHPDIRKLGFTGSTPIG 676
Cdd:cd07086 150 PGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDG-GELLVHDPRVPLVSFTGSTEVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 677 KQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMK 756
Cdd:cd07086 229 RRVGETVA-RRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 757 IGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQR--PGFFMEPTVFTDVEDYMYLAKEESFGPIMVIS 834
Cdd:cd07086 308 IGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 835 KFQngDIDGVLQRANSTEYGLASGVFTRDINKAM-YVSEK-LEAGTVFINT-YNKTDVAAPFGGVKQSGFGKDLGEEALN 911
Cdd:cd07086 388 KFD--SLEEAIAINNDVPQGLSSSIFTEDLREAFrWLGPKgSDCGIVNVNIpTSGAEIGGAFGGEKETGGGRESGSDAWK 465
|
490
....*....|..
gi 238814322 912 EYLKTKTVTLEY 923
Cdd:cd07086 466 QYMRRSTCTINY 477
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
443-923 |
1.81e-116 |
|
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: 364.47 E-value: 1.81e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 443 YQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQE 522
Cdd:cd07116 1 YDNFIGGEWVAPVKGEYFDNITPVTGKVFCEVPRSTAEDIELALDAAHAAKE--AWGKTSVAERANILNKIADRMEANLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 523 ELATIEALDSGAVYTLALKTHIGMSVQTFRYFAGWCDKIQGSTIPINqarpNRNLTFTKKEPLGVCAIIIPWNYPLMMLA 602
Cdd:cd07116 79 MLAVAETWDNGKPVRETLAADIPLAIDHFRYFAGCIRAQEGSISEID----ENTVAYHFHEPLGVVGQIIPWNFPLLMAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKS 682
Cdd:cd07116 155 WKLAPALAAGNCVVLKPAEQTPASILVLMEL-IGDLLPPGVVNVVNGFGLEAGKPLASSKRIAKVAFTGETTTGRLIMQY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 683 cAVSNLKKVSLELGGKSPLIIFNDCE------LDKAVRmGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMK 756
Cdd:cd07116 234 -ASENIIPVTLELGGKSPNIFFADVMdaddafFDKALE-GFVMFALNQGEVCTCPSRALIQESIYDRFMERALERVKAIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 757 IGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPG-----FFMEPTVFTDveDYMYLAKEESFGPIM 831
Cdd:cd07116 312 QGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGERNELGGllgggYYVPTTFKGG--NKMRIFQEEIFGPVL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 832 VISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALN 911
Cdd:cd07116 390 AVTTFK--DEEEALEIANDTLYGLGAGVWTRDGNTAYRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLD 467
|
490
....*....|..
gi 238814322 912 EYLKTKTVTLEY 923
Cdd:cd07116 468 HYQQTKNLLVSY 479
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
444-921 |
5.07e-115 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 360.76 E-value: 5.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 444 QCFINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEE 523
Cdd:PRK11241 12 QALINGEWLDANNGEVIDVTNPANGDKLGSVPKMGADETRAAIDAANRALP--AWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 524 LATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPINQarPNRNLTFTKkEPLGVCAIIIPWNYPLMMLAW 603
Cdd:PRK11241 90 LARLMTLEQGKPLAEA-KGEISYAASFIEWFAEEGKRIYGDTIPGHQ--ADKRLIVIK-QPIGVTAAITPWNFPAAMITR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 604 KSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSC 683
Cdd:PRK11241 166 KAGPALAAGCTMVLKPASQTPFSALALAELAIRAGIPAGVFNVVTGSAGAVGGELTSNPLVRKLSFTGSTEIGRQLMEQC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 684 AvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:PRK11241 246 A-KDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 764 STDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFqnGDIDG 843
Cdd:PRK11241 325 GVTIGPLIDEKAVAKVEEHIADALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRF--KDEAD 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814322 844 VLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:PRK11241 403 VIAQANDTEFGLAAYFYARDLSRVFRVGEALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCI 480
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
462-921 |
1.83e-114 |
|
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: 358.19 E-value: 1.83e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFENGEWgRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlK 541
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFDETDW-AHDPRLRARVLLELADAFEANAERLARLLALENGKILGEA-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSVQTFRYFAGWCDKIQGSTIpinQARPNrNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:cd07120 79 FEISGAISELRYYAGLARTEAGRMI---EPEPG-SFSLVLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 622 VTPLTALKFAELSVKA-GFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSP 700
Cdd:cd07120 155 QTAQINAAIIRILAEIpSLPAGVVNLFTESGSEGAAHLVASPDVDVISFTGSTATGRAIMAAAA-PTLKRLGLELGGKTP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 701 LIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLL 780
Cdd:cd07120 234 CIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDRVD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 781 QYCETGVKEGAT-LVYGGRQVQR--PGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLAS 857
Cdd:cd07120 314 RMVERAIAAGAEvVLRGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFD--DEAEAVALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 858 GVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07120 392 SVWTRDLARAMRVARAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
461-921 |
4.33e-112 |
|
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: 352.12 E-value: 4.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 461 DTINPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAL 540
Cdd:cd07094 2 DVHNPYDGEVIGKVPADDRADAEEALATARAGAEN--RRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 541 KtHIGMSVQTFRYFAGWCDKIQGSTIP--INQARPNRnLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLK 618
Cdd:cd07094 80 V-EVDRAIDTLRLAAEEAERIRGEEIPldATQGSDNR-LAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 619 PAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMkscAVSNLKKVSLELGGK 698
Cdd:cd07094 158 PASKTPLSALELAKILVEAGVPEGVLQVVTGEREVLGDAFAADERVAMLSFTGSAAVGEALR---ANAGGKRIALELGGN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 699 SPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEK 778
Cdd:cd07094 235 APVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 779 LLQYCETGVKEGATLVYGGRqvqRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASG 858
Cdd:cd07094 315 VERWVEEAVEAGARLLCGGE---RDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYD--DFEEAIRIANSTDYGLQAG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238814322 859 VFTRDINKAMYVSEKLEAGTVFIN--TYNKTDvAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07094 390 IFTRDLNVAFKAAEKLEVGGVMVNdsSAFRTD-WMPFGGVKESGVGREGVPYAMEEMTEEKTVVI 453
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
449-922 |
1.25e-107 |
|
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: 340.82 E-value: 1.25e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 449 GQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAfeNGEWGRMNARERGRLMYRLADLLEENQEELATIE 528
Cdd:cd07151 1 GEWRDGTSERTIDVLNPYTGETLAEIPAASKEDVDEAYRAAAAA--QKEWAATLPQERAEILEKAAQILEERRDEIVEWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 529 ALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPIN-QARPNRnltfTKKEPLGVCAIIIPWNYPLMmLAWKSAA 607
Cdd:cd07151 79 IRESGSTRIKA-NIEWGAAMAITREAATFPLRMEGRILPSDvPGKENR----VYREPLGVVGVISPWNFPLH-LSMRSVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 608 -CLAAGNTLVLKPAQVTPLTA-LKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAv 685
Cdd:cd07151 153 pALALGNAVVLKPASDTPITGgLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHPVPRLISFTGSTPVGRHIGELAG- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 SNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07151 232 RHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 766 DHGPQNHKAHLEKLLQYCETGVKEGATLVYGGrqvQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVL 845
Cdd:cd07151 312 VVGPLINESQVDGLLDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKAD--DEEEAL 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238814322 846 QRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVA-APFGGVKQSGFGKDLGEEALNEYLKTKTVTLE 922
Cdd:cd07151 387 ELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPhVPFGGEKNSGLGRFNGEWALEEFTTDKWISVQ 464
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
497-921 |
2.51e-105 |
|
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: 333.39 E-value: 2.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLA---LKTHIGMsvqtFRYFAGWCDKIQGSTIPinQARP 573
Cdd:cd07105 15 AWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAgfnVDLAAGM----LREAASLITQIIGGSIP--SDKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 574 NRnLTFTKKEPLGVCAIIIPWNYPLMmLAWKSAAC-LAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGG 652
Cdd:cd07105 89 GT-LAMVVKEPVGVVLGIAPWNAPVI-LGTRAIAYpLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGVLNVVTHSPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 653 IAGQR---LSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVrmgMGAV---FFNKGE 726
Cdd:cd07105 167 DAPEVveaLIAHPAVRKVNFTGSTRVGRIIAETAA-KHLKPVLLELGGKAPAIVLEDADLDAAA---NAALfgaFLNSGQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 727 NCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDpldrsTDHGPQ---NHKAHLEKLLqycETGVKEGATLVYGGRQVQRP 803
Cdd:cd07105 243 ICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLvsaAAADRVKELV---DDALSKGAKLVVGGLADESP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 804 -GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFqnGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN 882
Cdd:cd07105 315 sGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRV--KDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGAVHIN 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 238814322 883 TYNKTDVA-APFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07105 393 GMTVHDEPtLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
443-920 |
3.55e-103 |
|
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: 330.72 E-value: 3.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 443 YQCFINGQftDADDGKTYDTINPTDGS-TICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQ 521
Cdd:cd07124 33 YPLVIGGK--EVRTEEKIESRNPADPSeVLGTVQKATKEEAEAAVQAARAAFP--TWRRTPPEERARLLLRAAALLRRRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 522 EELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGWCDKIQGStiPINQARPNRNLTFTkkEPLGVCAIIIPWNYPLMML 601
Cdd:cd07124 109 FELAAWMVLEVGKNWAEAD-ADVAEAIDFLEYYAREMLRLRGF--PVEMVPGEDNRYVY--RPLGVGAVISPWNFPLAIL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMK 681
Cdd:cd07124 184 AGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEEVGDYLVEHPDVRFIAFTGSREVGLRIYE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 682 SCAV-----SNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMK 756
Cdd:cd07124 264 RAAKvqpgqKWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALK 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 757 IGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGaTLVYGGR--QVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVIS 834
Cdd:cd07124 344 VGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEG-RLLLGGEvlELAAEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 835 KFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINtyNKTDVA----APFGGVKQSGFG-KDLGEEA 909
Cdd:cd07124 423 KAK--DFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYAN--RKITGAlvgrQPFGGFKMSGTGsKAGGPDY 498
|
490
....*....|.
gi 238814322 910 LNEYLKTKTVT 920
Cdd:cd07124 499 LLQFMQPKTVT 509
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
510-923 |
5.74e-103 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 326.31 E-value: 5.74e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 510 MYRLADLLEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPINqaRPNRNLtFTKKEPLGVCA 589
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLA-EVEVAFTADYIDYMAEWARRYEGEIIQSD--RPGENI-LLFKRALGVTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 590 IIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGF 669
Cdd:PRK10090 77 GILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIGLPKGVFNLVLGRGETVGQELAGNPKVAMVSM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 670 TGSTPIGKQIMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVV 749
Cdd:PRK10090 157 TGSVSAGEKIMAA-AAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 750 EEIKKMKIGDPLDRST-DHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFG 828
Cdd:PRK10090 236 EAMQAVQFGNPAERNDiAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 829 PIMVISKFQNgdIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEE 908
Cdd:PRK10090 316 PVLPVVAFDT--LEEAIAMANDSDYGLTSSIYTQNLNVAMKAIKGLKFGETYINRENFEAMQGFHAGWRKSGIGGADGKH 393
|
410
....*....|....*
gi 238814322 909 ALNEYLKTKTVTLEY 923
Cdd:PRK10090 394 GLHEYLQTQVVYLQS 408
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
460-917 |
8.35e-103 |
|
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: 327.67 E-value: 8.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 460 YDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLA 539
Cdd:cd07147 1 LEVTNPYTGEVVARVALAGPDDIEEAIAAAVKAFR--PMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 540 lKTHIGMSVQTFRYFAGWCDKIQGSTIPIN-QARPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLK 618
Cdd:cd07147 79 -RGEVARAIDTFRIAAEEATRIYGEVLPLDiSARGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 619 PAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAgQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVsnlKKVSLELGGK 698
Cdd:cd07147 158 PASRTPLSALILGEVLAETGLPKGAFSVLPCSRDDA-DLLVTDERIKLLSFTGSPAVGWDLKARAGK---KKVVLELGGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 699 SPLIIFNDCELDKAV-RMGMGAvFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLE 777
Cdd:cd07147 234 AAVIVDSDADLDFAAqRIIFGA-FYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 778 KLLQYCETGVKEGATLVYGGRqvqRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLAS 857
Cdd:cd07147 313 RVEGWVNEAVDAGAKLLTGGK---RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYD--DFDEALAAVNDSKFGLQA 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238814322 858 GVFTRDINKAMYVSEKLEAGTVFINtynktDV------AAPFGGVKQSGFGKDLGEEALNEYLKTK 917
Cdd:cd07147 388 GVFTRDLEKALRAWDELEVGGVVIN-----DVptfrvdHMPYGGVKDSGIGREGVRYAIEEMTEPR 448
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
497-920 |
2.62e-101 |
|
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: 323.49 E-value: 2.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSG----AVYTLALKTHIGMsvqtfRYFAGWCDKI-----QGSTIP 567
Cdd:cd07101 33 AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGkarrHAFEEVLDVAIVA-----RYYARRAERLlkprrRRGAIP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 568 -INQARPNRNltftkkePLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINI 646
Cdd:cd07101 108 vLTRTTVNRR-------PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 647 IPGSGGIAGQRLSEHPDIrkLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGE 726
Cdd:cd07101 181 VTGPGSEVGGAIVDNADY--VMFTGSTATGRVVAERAG-RRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 727 NCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRqvQRPG-- 804
Cdd:cd07101 258 LCVSIERIYVHESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGR--ARPDlg 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 805 -FFMEPTVFTDVEDYMYLAKEESFGPIMVISKFqnGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN- 882
Cdd:cd07101 336 pYFYEPTVLTGVTEDMELFAEETFGPVVSIYRV--ADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNe 413
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 238814322 883 ----TYNKTDvaAPFGGVKQSGFGKDLGEEALNEYLKTKTVT 920
Cdd:cd07101 414 gyaaAWASID--APMGGMKDSGLGRRHGAEGLLKYTETQTVA 453
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
497-920 |
6.32e-101 |
|
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: 322.63 E-value: 6.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGWCDKIQGStipinQARPNRN 576
Cdd:cd07099 33 AWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAG-LEVLLALEAIDWAARNAPRVLAP-----RKVPTGL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 577 LTFTKK-----EPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSG 651
Cdd:cd07099 107 LMPNKKatveyRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAGPPQGVLQVVTGDG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 652 GiAGQRLSEHPdIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRmgmGAV---FFNKGENC 728
Cdd:cd07099 187 A-TGAALIDAG-VDKVAFTGSVATGRKVMAAAA-ERLIPVVLELGGKDPMIVLADADLERAAA---AAVwgaMVNAGQTC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 729 IAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFME 808
Cdd:cd07099 261 ISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMTTARQLDIVRRHVDDAVAKGAKALTGGARSNGGGPFYE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 809 PTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN--TYNK 886
Cdd:cd07099 341 PTVLTDVPHDMDVMREETFGPVLPVMPVA--DEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINdvLLTA 418
|
410 420 430
....*....|....*....|....*....|....
gi 238814322 887 TDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVT 920
Cdd:cd07099 419 GIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIA 452
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
446-920 |
2.68e-100 |
|
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: 321.77 E-value: 2.68e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:cd07085 4 FINGEWVESKTTEWLDVYNPATGEVIARVPLATAEEVDAAVAAAKAAFP--AWSATPVLKRQQVMFKFRQLLEENLDELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTIPinQARPNRNlTFTKKEPLGVCAIIIPWNYPLMMLAWKS 605
Cdd:cd07085 82 RLITLEHGKTLADA-RGDVLRGLEVVEFACSIPHLLKGEYLE--NVARGID-TYSYRQPLGVVAGITPFNFPAMIPLWMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 606 AACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGsGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKScAV 685
Cdd:cd07085 158 PMAIACGNTFVLKPSERVPGAAMRLAELLQEAGLPDGVLNVVHG-GKEAVNALLDHPDIKAVSFVGSTPVGEYIYER-AA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 SNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRST 765
Cdd:cd07085 236 ANGKRVQALGGAKNHAVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 766 DHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFqnGDI 841
Cdd:cd07085 316 DMGPVISPAAKERIEGLIESGVEEGAKLVLDGRGVKVPgyenGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRV--DTL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 842 DGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINtynkTDVAAP-----FGGVKQSGFGkDL---GEEALNEY 913
Cdd:cd07085 394 DEAIAIINANPYGNGAAIFTRSGAAARKFQREVDAGMVGIN----VPIPVPlaffsFGGWKGSFFG-DLhfyGKDGVRFY 468
|
....*..
gi 238814322 914 LKTKTVT 920
Cdd:cd07085 469 TQTKTVT 475
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
499-921 |
1.20e-97 |
|
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: 313.91 E-value: 1.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 499 GRMNARERGRLMYRLADLLEENQEELATIEALDSGavytLALKT---HIGMSVQTFRYFAGWCDKIQGSTIPINQARP-N 574
Cdd:cd07146 35 STLTRYQRSAILNKAAALLEARREEFARLITLESG----LCLKDtryEVGRAADVLRFAAAEALRDDGESFSCDLTANgK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 575 RNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIA 654
Cdd:cd07146 111 ARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAGLPPDMLSVVTGEPGEI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 655 GQRLSEHPDIRKLGFTGSTPIGKQImksCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRL 734
Cdd:cd07146 191 GDELITHPDVDLVTFTGGVAVGKAI---AATAGYKRQLLELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 735 FVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGrqvQRPGFFMEPTVFTD 814
Cdd:cd07146 268 LVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIENRVEEAIAQGARVLLGN---QRQGALYAPTVLDH 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 815 VEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVA-APF 893
Cdd:cd07146 345 VPPDAELVTEETFGPVAPVIRVK--DLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNEVPGFRSElSPF 422
|
410 420
....*....|....*....|....*....
gi 238814322 894 GGVKQSGFGKDLG-EEALNEYLKTKTVTL 921
Cdd:cd07146 423 GGVKDSGLGGKEGvREAMKEMTNVKTYSL 451
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
497-920 |
3.06e-97 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 315.28 E-value: 3.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALK--THIGMsvqTFRYFAGWCDKI-----QGSTIPI- 568
Cdd:PRK09407 69 AWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEevLDVAL---TARYYARRAPKLlaprrRAGALPVl 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 569 NQARPNRNltftkkePLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIP 648
Cdd:PRK09407 146 TKTTELRQ-------PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQVVT 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 649 GSGGIAGQRLSEHPDIrkLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENC 728
Cdd:PRK09407 219 GPGPVVGTALVDNADY--LMFTGSTATGRVLAEQAG-RRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLC 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 729 IAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRqvQRP--G-F 805
Cdd:PRK09407 296 ISIERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGK--ARPdlGpL 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 806 FMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN--- 882
Cdd:PRK09407 374 FYEPTVLTGVTPDMELAREETFGPVVSVYPVA--DVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNegy 451
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 238814322 883 --TYNKTDvaAPFGGVKQSGFGKDLGEEALNEYLKTKTVT 920
Cdd:PRK09407 452 aaAWGSVD--APMGGMKDSGLGRRHGAEGLLKYTESQTIA 489
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
497-921 |
6.13e-97 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 311.54 E-value: 6.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVytlALKTH--IGMSVQTFRYFAGWCDKIQGSTIPINQARpn 574
Cdd:cd07152 28 AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSI---RPKAGfeVGAAIGELHEAAGLPTQPQGEILPSAPGR-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 575 rnLTFTKKEPLGVCAIIIPWNYPLMmLAWKS-AACLAAGNTLVLKPAQVTPLTA-LKFAELSVKAGFPKGVINIIPGsGG 652
Cdd:cd07152 103 --LSLARRVPLGVVGVISPFNFPLI-LAMRSvAPALALGNAVVLKPDPRTPVSGgVVIARLFEEAGLPAGVLHVLPG-GA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 653 IAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAG 732
Cdd:cd07152 179 DAGEALVEDPNVAMISFTGSTAVGRKVGEAAG-RHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 733 RLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRqvqRPGFFMEPTVF 812
Cdd:cd07152 258 RHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGGT---YDGLFYRPTVL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 813 TDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN--TYNKtDVA 890
Cdd:cd07152 335 SGVKPGMPAFDEEIFGPVAPVTVFD--SDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINdqTVND-EPH 411
|
410 420 430
....*....|....*....|....*....|..
gi 238814322 891 APFGGVKQSGFGKDLGEEA-LNEYLKTKTVTL 921
Cdd:cd07152 412 NPFGGMGASGNGSRFGGPAnWEEFTQWQWVTV 443
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
497-920 |
1.04e-95 |
|
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: 309.23 E-value: 1.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGavytlalKTHI----GMSVQTfryfagwCDKIQ-----GSTIP 567
Cdd:cd07098 33 EWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTG-------KTMVdaslGEILVT-------CEKIRwtlkhGEKAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 568 INQARPNRNLTFTKK-----EPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKA----G 638
Cdd:cd07098 99 RPESRPGGLLMFYKRarveyEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIREClaacG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 639 FPKGVINIIPGSGGiAGQRLSEHPDIRKLGFTGSTPIGKQIMKsCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMG 718
Cdd:cd07098 179 HDPDLVQLVTCLPE-TAEALTSHPVIDHITFIGSPPVGKKVMA-AAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 719 AVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGP---QNHKAHLEKLLQyceTGVKEGATLVY 795
Cdd:cd07098 257 GTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAmisPARFDRLEELVA---DAVEKGARLLA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 796 GGRQVQRP----GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVS 871
Cdd:cd07098 334 GGKRYPHPeypqGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKAS--DDEEAVEIANSTEYGLGASVFGKDIKRARRIA 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 238814322 872 EKLEAGTVFINTYNKT--DVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVT 920
Cdd:cd07098 412 SQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVT 462
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
443-919 |
1.70e-94 |
|
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: 306.03 E-value: 1.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 443 YQCFINGQFTDADdGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFeNGEWGRMNARERGRLMYRLADLLEENQE 522
Cdd:cd07082 2 FKYLINGEWKESS-GKTIEVYSPIDGEVIGSVPALSALEILEAAETAYDAG-RGWWPTMPLEERIDCLHKFADLLKENKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 523 ELATIEALDSGAVYTLALKtHIGMSVQTFRYFAGWCDKIQGSTIPINQARPNRN-LTFTKKEPLGVCAIIIPWNYPLMML 601
Cdd:cd07082 80 EVANLLMWEIGKTLKDALK-EVDRTIDYIRDTIEELKRLDGDSLPGDWFPGTKGkIAQVRREPLGVVLAIGPFNYPLNLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMK 681
Cdd:cd07082 159 VSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGFPKGVVNVVTGRGREIGDPLVTHGRIDVISFTGSTEVGNRLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 682 ScavSNLKKVSLELGGKSPLIIFNDCELDKAV-RMGMGAVFFNkGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDP 760
Cdd:cd07082 239 Q---HPMKRLVLELGGKDPAIVLPDADLELAAkEIVKGALSYS-GQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 761 LDRSTDHGP--QNHKA-HLEKLLqycETGVKEGATLVYGGRqvQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQ 837
Cdd:cd07082 315 WDNGVDITPliDPKSAdFVEGLI---DDAVAKGATVLNGGG--REGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 838 ngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNK--TDVaAPFGGVKQSGFGKDLGEEALNEYLK 915
Cdd:cd07082 390 --DIEEAIELANKSNYGLQASIFTKDINKARKLADALEVGTVNINSKCQrgPDH-FPFLGRKDSGIGTQGIGDALRSMTR 466
|
....
gi 238814322 916 TKTV 919
Cdd:cd07082 467 RKGI 470
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
463-921 |
1.43e-89 |
|
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: 292.23 E-value: 1.43e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 463 INPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlKT 542
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQK--GWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQA-GG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 543 HIGMSVQTFRYFagwCDKIQGSTIPINQARPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQV 622
Cdd:cd07102 78 EIRGMLERARYM---ISIAEEALADIRVPEKDGFERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 623 TPLTALKFAELSVKAGFPKGVINIIPGSGGIaGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVsNLKKVSLELGGKSPLI 702
Cdd:cd07102 155 TPLCGERFAAAFAEAGLPEGVFQVLHLSHET-SAALIADPRIDHVSFTGSVAGGRAIQRAAAG-RFIKVGLELGGKDPAY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 703 IFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQY 782
Cdd:cd07102 233 VRPDADLDAAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 783 CETGVKEGATLVYGG---RQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQNgDiDGVLQRANSTEYGLASGV 859
Cdd:cd07102 313 IADAIAKGARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKS-D-AEAIALMNDSEYGLTASV 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238814322 860 FTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVTL 921
Cdd:cd07102 391 WTKDIARAEALGEQLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
434-920 |
1.34e-85 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 283.68 E-value: 1.34e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 434 VNEIMVKmPYQCFINGQFTDADDgkTYDTINPTDGS-TICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYR 512
Cdd:TIGR01237 25 VKEQLGK-TYPLVINGERVETEN--KIVSINPCDKSeVVGTVSKASQEHAEHALQAAAKAFE--AWKKTDPEERAAILFK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 513 LADLLEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGSTiPINQARPNRNLTFTkkEPLGVCAIII 592
Cdd:TIGR01237 100 AAAIVRRRRHEFSALLVKEVGKPWNEA-DAEVAEAIDFMEYYARQMIELAKGK-PVNSREGETNQYVY--TPTGVTVVIS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 593 PWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGS 672
Cdd:TIGR01237 176 PWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAGLPKGVVQFVPGSGSEVGDYLVDHPKTSLITFTGS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 673 TPIGKQIMKSCAV-----SNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTR 747
Cdd:TIGR01237 256 REVGTRIFERAAKvqpgqKHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHEKVYDEVVER 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 748 VVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGaTLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESF 827
Cdd:TIGR01237 336 FVEITESLKVGPPDSADVYVGPVIDQKSFNKIMEYIEIGKAEG-RLVSGGCGDDSKGYFIGPTIFADVDRKARLAQEEIF 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 828 GPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRD---INKAmyvSEKLEAGTVFIntyNKTDVAA-----PFGGVKQS 899
Cdd:TIGR01237 415 GPVVAFIRAS--DFDEALEIANNTEYGLTGGVISNNrdhINRA---KAEFEVGNLYF---NRNITGAivgyqPFGGFKMS 486
|
490 500
....*....|....*....|..
gi 238814322 900 GFG-KDLGEEALNEYLKTKTVT 920
Cdd:TIGR01237 487 GTDsKAGGPDYLALFMQAKTVT 508
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
462-919 |
6.04e-85 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 280.09 E-value: 6.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlK 541
Cdd:PRK09406 5 TINPATGETVKTFTALTDDEVDAAIARAHARFRD--YRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA-K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSVQTFRYFAGWCDKIQGSTiPINQARPNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQ 621
Cdd:PRK09406 82 AEALKCAKGFRYYAEHAEALLADE-PADAAAVGASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 622 VTPLTALKFAELSVKAGFPKGVI-NIIPGSGGIagQRLSEHPDIRKLGFTGSTPIGKQImKSCAVSNLKKVSLELGGKSP 700
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFqTLLVGSGAV--EAILRDPRVAAATLTGSEPAGRAV-AAIAGDEIKKTVLELGGSDP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 701 LIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLL 780
Cdd:PRK09406 238 FIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 781 QYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPimVISKFQNGDIDGVLQRANSTEYGLASGVF 860
Cdd:PRK09406 318 KQVDDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGP--VASLYRVADIDEAIEIANATTFGLGSNAW 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 238814322 861 TRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:PRK09406 396 TRDEAEQERFIDDLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
443-920 |
9.08e-85 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 281.44 E-value: 9.08e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 443 YQCFINGQFTDADDgkTYDTINPTDGS-TICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQ 521
Cdd:PRK03137 37 YPLIIGGERITTED--KIVSINPANKSeVVGRVSKATKELAEKAMQAALEAFE--TWKKWSPEDRARILLRAAAIIRRRK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 522 EELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKI-QGStiPINQaRPN-RNLTFTkkEPLGVCAIIIPWNYPLM 599
Cdd:PRK03137 113 HEFSAWLVKEAGKPWAEA-DADTAEAIDFLEYYARQMLKLaDGK--PVES-RPGeHNRYFY--IPLGVGVVISPWNFPFA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 600 MLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQI 679
Cdd:PRK03137 187 IMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGLPAGVVNFVPGSGSEVGDYLVDHPKTRFITFTGSREVGLRI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 680 MKSCAVSN-----LKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKK 754
Cdd:PRK03137 267 YERAAKVQpgqiwLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKE 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 755 MKIGDPLDRsTDHGPQNHKAHLEKLLQYCETGVKEGaTLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVIS 834
Cdd:PRK03137 347 LTVGNPEDN-AYMGPVINQASFDKIMSYIEIGKEEG-RLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 835 KFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGtvfiNTY-NKTDVAA-----PFGGVKQSGF-GKDLGE 907
Cdd:PRK03137 425 KAK--DFDHALEIANNTEYGLTGAVISNNREHLEKARREFHVG----NLYfNRGCTGAivgyhPFGGFNMSGTdSKAGGP 498
|
490
....*....|...
gi 238814322 908 EALNEYLKTKTVT 920
Cdd:PRK03137 499 DYLLLFLQAKTVS 511
|
|
| Fmt |
COG0223 |
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis]; |
23-327 |
1.41e-76 |
|
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439993 [Multi-domain] Cd Length: 308 Bit Score: 252.33 E-value: 1.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 23 LKLALIGQSLFGQEVYSHLRKEGHRVVGVFTVPDKD---GK---ADPLALAAEKDGTPVFKlPKwRVKGKtikEVAEAYR 96
Cdd:COG0223 1 MRIVFMGTPDFAVPSLEALLAAGHEVVAVVTQPDRPagrGRkltPSPVKELALEHGIPVLQ-PE-SLKDP---EFLEELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 97 SVGAELNVLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDV 176
Cdd:COG0223 76 ALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLLPRYRGAAPIQWAILNGDTETGVTIMQMDEGLDTGDILLQEEVPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 177 EPNDTVDALYNRfLFPEGIKAMVEAVQLIADGKAPRIPQPEEGATYEGIQKKENAEISWDQSAEVLHNWIRGHDKVPGAW 256
Cdd:COG0223 156 GPDDTAGSLHDK-LAELGAELLLETLDALEAGTLTPTPQDESGATYAPKISKEDGRIDWSRPAEEIHRLIRALNPWPGAF 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 257 TEINGQMVTFYGStllnssvppgEPLEIKGAKKPGLV---TKNGLVLFGNDGkALTVRNLQFEDGKMIPASQYF 327
Cdd:COG0223 235 TTLDGKRLKIWKA----------RVLEEAGGGAPGTIlavDKDGLLVACGDG-ALRLLELQPAGKKRMSAADFL 297
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
445-902 |
2.26e-75 |
|
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: 256.35 E-value: 2.26e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 445 CFINGQFTDADDGKTYdtINPTDG-STICKVSYASLADVDKAVAAAKDAFenGEWGRMNARERGRLMYRLADLLEENQEE 523
Cdd:cd07125 35 PIINGEETETGEGAPV--IDPADHeRTIGEVSLADAEDVDAALAIAAAAF--AGWSATPVEERAEILEKAADLLEANRGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 524 LATIEALDSGAvyTLAlKTHIGMS--VQTFRYFAGWCDKIQGSTIPINQARPNRNLTFtkkEPLGVCAIIIPWNYPLMML 601
Cdd:cd07125 111 LIALAAAEAGK--TLA-DADAEVReaIDFCRYYAAQARELFSDPELPGPTGELNGLEL---HGRGVFVCISPWNFPLAIF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMK 681
Cdd:cd07125 185 TGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEALVAHPRIDGVIFTGSTETAKLINR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 682 SCAVSNLKKVSL--ELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGD 759
Cdd:cd07125 265 ALAERDGPILPLiaETGGKNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 760 PLDRSTDHGPQNHKAHLEKLLQYCETGVKEgATLVYggrQVQRP---GFFMEPTVFTDVEDYMYlaKEESFGPIMVISKF 836
Cdd:cd07125 345 PWDLSTDVGPLIDKPAGKLLRAHTELMRGE-AWLIA---PAPLDdgnGYFVAPGIIEIVGIFDL--TTEVFGPILHVIRF 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238814322 837 QNGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIntyNKTDVAA-----PFGGVKQSGFG 902
Cdd:cd07125 419 KAEDLDEAIEDINATGYGLTLGIHSRDEREIEYWRERVEAGNLYI---NRNITGAivgrqPFGGWGLSGTG 486
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
457-923 |
6.60e-75 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 253.67 E-value: 6.60e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 457 GKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVY 536
Cdd:cd07130 11 GGVVTSISPANGEPIARVRQATPEDYESTIKAAQEAFK--EWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 537 TLALKthigmSVQTF----RYFAGWCDKIQGSTIPinQARPNRNLtFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAG 612
Cdd:cd07130 89 PEGLG-----EVQEMidicDFAVGLSRQLYGLTIP--SERPGHRM-MEQWNPLGVVGVITAFNFPVAVWGWNAAIALVCG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 613 NTLVLKPAQVTPLTALK----FAELSVKAGFPKGVINIIPGsGGIAGQRLSEHPDIRKLGFTGSTPIGKQImkSCAVS-N 687
Cdd:cd07130 161 NVVVWKPSPTTPLTAIAvtkiVARVLEKNGLPGAIASLVCG-GADVGEALVKDPRVPLVSFTGSTAVGRQV--GQAVAaR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 688 LKKVSLELGGKSPLIIFNDCELDKAVRmgmgAVFF----NKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:cd07130 238 FGRSLLELGGNNAIIVMEDADLDLAVR----AVLFaavgTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 764 STDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTdVEDYMYLAKEESFGPIMVISKFQngDIDG 843
Cdd:cd07130 314 GTLVGPLHTKAAVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFD--TLEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 844 VLQRANSTEYGLASGVFTRDINKA-MYVSEK-LEAGTVFINT-YNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTVT 920
Cdd:cd07130 391 AIAWNNEVPQGLSSSIFTTDLRNAfRWLGPKgSDCGIVNVNIgTSGAEIGGAFGGEKETGGGRESGSDAWKQYMRRSTCT 470
|
...
gi 238814322 921 LEY 923
Cdd:cd07130 471 INY 473
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
443-920 |
5.54e-70 |
|
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: 240.94 E-value: 5.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 443 YQCFINGQFTDADDGKTydTINPTD-GSTICKVSYASLADVDKAVAAAKDAFenGEWGRMNARERGRLMYRLADLLEENQ 521
Cdd:cd07083 19 YPLVIGGEWVDTKERMV--SVSPFApSEVVGTTAKADKAEAEAALEAAWAAF--KTWKDWPQEDRARLLLKAADLLRRRR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 522 EELATIEALDSGAVYTLALKThIGMSVQTFRYFAGWCDKIQGSTIPINQARPNRNLTFTKkePLGVCAIIIPWNYPLMML 601
Cdd:cd07083 95 RELIATLTYEVGKNWVEAIDD-VAEAIDFIRYYARAALRLRYPAVEVVPYPGEDNESFYV--GLGAGVVISPWNFPVAIF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 602 AWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMK 681
Cdd:cd07083 172 TGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGFPPGVVQFLPGVGEEVGAYLTEHERIRGINFTGSLETGKKIYE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 682 SCA-----VSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMK 756
Cdd:cd07083 252 AAArlapgQTWFKRLYVETGGKNAIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 757 IGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGaTLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKF 836
Cdd:cd07083 332 VGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEG-QLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 837 QNGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAA--PFGGVKQSGFG-KDLGEEALNEY 913
Cdd:cd07083 411 KDDDFAEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINRKITGALVGvqPFGGFKLSGTNaKTGGPHYLRRF 490
|
....*..
gi 238814322 914 LKTKTVT 920
Cdd:cd07083 491 LEMKAVA 497
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
462-919 |
5.06e-69 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 237.07 E-value: 5.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 462 TINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlK 541
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFR--DWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQA-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 542 THIGMSvqtfryfAGWCDKIQGSTIPINQARPN---RNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLK 618
Cdd:PRK13968 88 AEVAKS-------ANLCDWYAEHGPAMLKAEPTlveNQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 619 PAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEhPDIRKLGFTGSTPIGKQImKSCAVSNLKKVSLELGGK 698
Cdd:PRK13968 161 HAPNVMGCAQLIAQVFKDAGIPQGVYGWLNADNDGVSQMIND-SRIAAVTVTGSVRAGAAI-GAQAGAALKKCVLELGGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 699 SPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEK 778
Cdd:PRK13968 239 DPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 779 LLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASG 858
Cdd:PRK13968 319 LHHQVEATLAEGARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAK--DAEHALELANDSEFGLSAT 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238814322 859 VFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:PRK13968 397 IFTTDETQARQMAARLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
512-903 |
3.92e-66 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 227.79 E-value: 3.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 512 RLADLLEENQEELatIEAL--DSGAVYTLALKTHIGMSVQTFRY----FAGWCDKIQGSTIPINQarPNRnlTFTKKEPL 585
Cdd:cd07087 28 ALKRMLTENEEEI--AAALyaDLGKPPAEAYLTEIAVVLGEIDHalkhLKKWMKPRRVSVPLLLQ--PAK--AYVIPEPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 586 GVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHPDir 665
Cdd:cd07087 102 GVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKL-IPKYFDPEAVAVVEGGVEVATALLAEPFD-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 666 KLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFV 745
Cdd:cd07087 179 HIFFTGSPAVGKIVMEA-AAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTCIAPDYVLVHESIKDELI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 746 TRVVEEIKKMkIGDPLDRSTDHGPQNHKAHLEKLLQYcetgvKEGATLVYGGrQVQRPGFFMEPTVFTDVEDYMYLAKEE 825
Cdd:cd07087 258 EELKKAIKEF-YGEDPKESPDYGRIINERHFDRLASL-----LDDGKVVIGG-QVDKEERYIAPTILDDVSPDSPLMQEE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 826 SFGPIMVISKFQNgdIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINtynktDV-------AAPFGGVKQ 898
Cdd:cd07087 331 IFGPILPILTYDD--LDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVN-----DVllhaaipNLPFGGVGN 403
|
....*
gi 238814322 899 SGFGK 903
Cdd:cd07087 404 SGMGA 408
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
497-900 |
3.83e-61 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 214.44 E-value: 3.83e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGA--------VYTLALKthIGMSVQTFRYFAGwcDKiqgsTIPI 568
Cdd:cd07095 15 GWAALSLEERAAILRRFAELLKANKEELARLISRETGKplweaqteVAAMAGK--IDISIKAYHERTG--ER----ATPM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 569 NQARpnrnlTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIP 648
Cdd:cd07095 87 AQGR-----AVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGVLNLVQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 649 GsGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENC 728
Cdd:cd07095 162 G-GRETGEALAAHEGIDGLLFTGSAATGLLLHRQFAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAGQRC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 729 IAAGRLFVEES-IHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFM 807
Cdd:cd07095 241 TCARRLIVPDGaVGDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAGTAFL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 808 EPTVFtDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN-TYNK 886
Cdd:cd07095 321 SPGII-DVTDAADVPDEEIFGPLLQVYRYD--DFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVNWNrPTTG 397
|
410
....*....|....
gi 238814322 887 TDVAAPFGGVKQSG 900
Cdd:cd07095 398 ASSTAPFGGVGLSG 411
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
583-907 |
2.53e-59 |
|
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: 209.39 E-value: 2.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 583 EPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAgQRLSEHP 662
Cdd:cd07134 99 EPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKI-IREAFDEDEVAVFEGDAEVA-QALLELP 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 663 dIRKLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHD 742
Cdd:cd07134 177 -FDHIFFTGSPAVGKIVMAA-AAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDYVFVHESVKD 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 743 EFVTRVVEEIKKMKIGDPLDR-STDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGrQVQRPGFFMEPTVFTDVEDYMYL 821
Cdd:cd07134 255 AFVEHLKAEIEKFYGKDAARKaSPDLARIVNDRHFDRLKGLLDDAVAKGAKVEFGG-QFDAAQRYIAPTVLTNVTPDMKI 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 822 AKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINtynktDVAA-------PFG 894
Cdd:cd07134 334 MQEEIFGPVLPIITYE--DLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVN-----DVVLhflnpnlPFG 406
|
330
....*....|...
gi 238814322 895 GVKQSGFGKDLGE 907
Cdd:cd07134 407 GVNNSGIGSYHGV 419
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
461-902 |
7.69e-56 |
|
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: 199.95 E-value: 7.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 461 DTINPTDGSTICKVSYASLADVDKAVAAAKDAFEN-GEWgrMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLA 539
Cdd:cd07148 2 EVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLDrNNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 540 LkthigmsVQTFRYFAG--WCDK----IQGSTIPIN--QARPNRnLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAA 611
Cdd:cd07148 80 K-------VEVTRAIDGveLAADelgqLGGREIPMGltPASAGR-IAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 612 GNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAgQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVSNlkKV 691
Cdd:cd07148 152 GCPVIVKPALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVA-EKLVTDPRVAFFSFIGSARVGWMLRSKLAPGT--RC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 692 SLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQN 771
Cdd:cd07148 229 ALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 772 HKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFfmEPTVFTDVEDYMYLAKEESFGPIMVIskFQNGDIDGVLQRANST 851
Cdd:cd07148 309 RPREVDRVEEWVNEAVAAGARLLCGGKRLSDTTY--APTVLLDPPRDAKVSTQEIFGPVVCV--YSYDDLDEAIAQANSL 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 238814322 852 EYGLASGVFTRDINKAMYVSEKLEAGTVFIN--TYNKTDvAAPFGGVKQSGFG 902
Cdd:cd07148 385 PVAFQAAVFTKDLDVALKAVRRLDATAVMVNdhTAFRVD-WMPFAGRRQSGYG 436
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
579-902 |
2.91e-55 |
|
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: 198.11 E-value: 2.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 579 FTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRL 658
Cdd:cd07136 95 YIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKI-IEETFDEEYVAVVEGGVEENQELL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 659 SEHPDirKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEE 738
Cdd:cd07136 174 DQKFD--YIFFTGSVRVGKIVMEAAA-KHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTCVAPDYVLVHE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 739 SIHDEFVTRVVEEIKKMKIGDPLDrSTDHGPQNHKAHLEKLLQYCETGvkegaTLVYGGrQVQRPGFFMEPTVFTDVEDY 818
Cdd:cd07136 251 SVKEKFIKELKEEIKKFYGEDPLE-SPDYGRIINEKHFDRLAGLLDNG-----KIVFGG-NTDRETLYIEPTILDNVTWD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 819 MYLAKEESFGPIMVISKFQNgdIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAG------TV--FINTYnktdva 890
Cdd:cd07136 324 DPVMQEEIFGPILPVLTYDT--LDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGggcindTImhLANPY------ 395
|
330
....*....|..
gi 238814322 891 APFGGVKQSGFG 902
Cdd:cd07136 396 LPFGGVGNSGMG 407
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
578-902 |
5.41e-55 |
|
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: 197.06 E-value: 5.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 578 TFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIpgSGGIA-GQ 656
Cdd:cd07135 102 PRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQVV--QGGVPeTT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 657 RLSEHP-DirKLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLF 735
Cdd:cd07135 179 ALLEQKfD--KIFYTGSGRVGRIIAEA-AAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAPDYVL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 736 VEESIHDEFVTRVVEEIKKMKIGDPlDRSTDHGPQNHKAHLEKLLQYCETgvkEGATLVYGGRQvQRPGFFMEPTVFTDV 815
Cdd:cd07135 256 VDPSVYDEFVEELKKVLDEFYPGGA-NASPDYTRIVNPRHFNRLKSLLDT---TKGKVVIGGEM-DEATRFIPPTIVSDV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 816 EDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN-TYNKTDV-AAPF 893
Cdd:cd07135 331 SWDDSLMSEELFGPVLPIIKVD--DLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINdTLIHVGVdNAPF 408
|
....*....
gi 238814322 894 GGVKQSGFG 902
Cdd:cd07135 409 GGVGDSGYG 417
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
578-903 |
1.01e-54 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 197.94 E-value: 1.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 578 TFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAgFPKGVINIIPGSGGIAGQR 657
Cdd:PTZ00381 103 SYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVIEGGVEVTTEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 658 LSEHPDIrkLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVE 737
Cdd:PTZ00381 182 LKEPFDH--IFFTGSPRVGKLVMQA-AAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVAPDYVLVH 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 738 ESIHDEFVTRVVEEIKKMkIGDPLDRSTDHGPQNHKAHLEKLLQYCETgvkEGATLVYGGrQVQRPGFFMEPTVFTDVED 817
Cdd:PTZ00381 259 RSIKDKFIEALKEAIKEF-FGEDPKKSEDYSRIVNEFHTKRLAELIKD---HGGKVVYGG-EVDIENKYVAPTIIVNPDL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 818 YMYLAKEESFGPIMVISKFQNgdIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIN--TYNKTDVAAPFGG 895
Cdd:PTZ00381 334 DSPLMQEEIFGPILPILTYEN--IDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINdcVFHLLNPNLPFGG 411
|
....*...
gi 238814322 896 VKQSGFGK 903
Cdd:PTZ00381 412 VGNSGMGA 419
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
415-906 |
1.42e-54 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 197.83 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 415 KLRGEDQEVELVVDYISKEVNEIMVKMPYQCF-----INGQFTDadDGKTYDTINPTDGSTIC-KVSYASLADVDKAVAA 488
Cdd:TIGR01238 5 EGRKNSLGIDLDNESELKPLEAQIHAWADKTWqaapiIGHSYKA--DGEAQPVTNPADRRDIVgQVFHANLAHVQAAIDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 489 AKDAFEngEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALkTHIGMSVQTFRYFAgwcdkiqgstipi 568
Cdd:TIGR01238 83 AQQAFP--TWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAI-AEVREAVDFCRYYA------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 569 NQARpnRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIP 648
Cdd:TIGR01238 147 KQVR--DVLGEFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGFPAGTIQLLP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 649 GSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVSNLKKVSL--ELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGE 726
Cdd:TIGR01238 225 GRGADVGAALTSDPRIAGVAFTGSTEVAQLINQTLAQREDAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 727 NCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGP-------QNHKAHLEKLLQyceTGvKEGATLVYGGRQ 799
Cdd:TIGR01238 305 RCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPvidaeakQNLLAHIEHMSQ---TQ-KKIAQLTLDDSR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 800 VQRPGFFMEPTVFtDVEDYMYLaKEESFGPIMVISKFQNGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTV 879
Cdd:TIGR01238 381 ACQHGTFVAPTLF-ELDDIAEL-SEEVFGPVLHVVRYKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNC 458
|
490 500 510
....*....|....*....|....*....|..
gi 238814322 880 FIntyNKTDVAA-----PFGGVKQSGFGKDLG 906
Cdd:TIGR01238 459 YV---NRNQVGAvvgvqPFGGQGLSGTGPKAG 487
|
|
| Formyl_trans_N |
pfam00551 |
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ... |
23-202 |
1.09e-53 |
|
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.
Pssm-ID: 395436 [Multi-domain] Cd Length: 181 Bit Score: 184.80 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 23 LKLALI--GQSLFGQEVYSHLRKEGHRVVGVFTVPDKDGKADPLALAAEKDGTPVFKLPKWRVKGKTIKEVAEAYRSVGA 100
Cdd:pfam00551 1 MKIAVLisGTGSNLQALIDALRKGGQDADVVLVISNKDKAAGLGRAEQAGIPTFVFEHKGLTPRSLFDQELADALRALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 101 ELNVLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPND 180
Cdd:pfam00551 81 DVIVLAGYMRILPPEFLQAPPGGILNIHPSLLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDD 160
|
170 180
....*....|....*....|..
gi 238814322 181 TVDALYNRFLFPEGiKAMVEAV 202
Cdd:pfam00551 161 TAETLYNRVADLEH-KALPRVL 181
|
|
| FDH_Hydrolase_C |
cd08703 |
The C-terminal subdomain of the hydrolase domain on the bi-functional protein ... |
228-327 |
1.83e-52 |
|
The C-terminal subdomain of the hydrolase domain on the bi-functional protein 10-formyltetrahydrofolate dehydrogenase; The family represents the C-terminal subdomain of the hydrolase domain on the bi-functional protein, 10-formyltetrahydrofolate dehydrogenase (FDH). FDH catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. The protein comprises two functional domains: the N-terminal hydrolase domain that removes a formyl group from 10-formyltetrahydrofolate and the C-terminal NADP-dependent dehydrogenase domain that reduces the formyl group to carbon dioxide. The hydrolase domain contains an N-terminal formyl transferase catalytic core subdomain and this C-terminal subdomain, which may be involved in substrate binding.
Pssm-ID: 187731 [Multi-domain] Cd Length: 100 Bit Score: 177.92 E-value: 1.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 228 KENAEISWDQSAEVLHNWIRGHDKVPGAWTEINGQMVTFYGSTLLNSSVPPGEPLEIKGAKKPGLVTKNGLVLFGNDGKA 307
Cdd:cd08703 1 KELAKINWDQTAEALHNFIRGNDKVPGAWATIDGEQVTLFGSSLWKGGKPPGGEVEVEGLERPGIVHKNGLLITGSDGKM 80
|
90 100
....*....|....*....|
gi 238814322 308 LTVRNLQFEDGKMIPASQYF 327
Cdd:cd08703 81 VNVKRLQFEDGKMIPASKYG 100
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
503-919 |
2.68e-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: 189.23 E-value: 2.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 503 ARERGRLMYRLADLLEENQEELAtiEAL--DSG---AVYTLALKthIGMSVQTFRY----FAGWCdkiqgstipinqaRP 573
Cdd:cd07133 19 LEERRDRLDRLKALLLDNQDALA--EAIsaDFGhrsRHETLLAE--ILPSIAGIKHarkhLKKWM-------------KP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 574 NR---NLTFT------KKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAgFPKGVI 644
Cdd:cd07133 82 SRrhvGLLFLpakaevEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 645 NIIPGSGGIAgQRLSEHP-DirKLGFTGSTPIGKQIMKSCAvSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFN 723
Cdd:cd07133 161 AVVTGGADVA-AAFSSLPfD--HLLFTGSTAVGRHVMRAAA-ENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 724 KGENCIAAGRLFVEESIHDEFVTRVVEEIKKMkIGDPLDrSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRP 803
Cdd:cd07133 237 AGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLAD-NPDYTSIINERHYARLQGLLEDARAKGARVIELNPAGEDF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 804 --GFFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFI 881
Cdd:cd07133 315 aaTRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYD--SLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTI 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 238814322 882 NtynktDVA-------APFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:cd07133 393 N-----DTLlhvaqddLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
445-923 |
1.04e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 186.96 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 445 CFINGQFtdADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQEEL 524
Cdd:PLN02315 23 CYVGGEW--RANGPLVSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKI--WMQVPAPKRGEIVRQIGDALRAKLDYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 525 ATIEALDSGAVytlaLKTHIGmSVQTF----RYFAGWCDKIQGSTIPinQARPNrNLTFTKKEPLGVCAIIIPWNYPLMM 600
Cdd:PLN02315 99 GRLVSLEMGKI----LAEGIG-EVQEIidmcDFAVGLSRQLNGSIIP--SERPN-HMMMEVWNPLGIVGVITAFNFPCAV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 601 LAWKSAACLAAGNTLVLKPAQVTPLTALK----FAELSVKAGFPKGVINIIPGSGGIaGQRLSEHPDIRKLGFTGSTPIG 676
Cdd:PLN02315 171 LGWNACIALVCGNCVVWKGAPTTPLITIAmtklVAEVLEKNNLPGAIFTSFCGGAEI-GEAIAKDTRIPLVSFTGSSKVG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 677 kqIMKSCAV-SNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKM 755
Cdd:PLN02315 250 --LMVQQTVnARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 756 KIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVfTDVEDYMYLAKEESFGPIMVISK 835
Cdd:PLN02315 328 KIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGGKILTGGSAIESEGNFVQPTI-VEISPDADVVKEELFGPVLYVMK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 836 FQNgdIDGVLQRANSTEYGLASGVFTR--DINKAMYVSEKLEAGTVFINT-YNKTDVAAPFGGVKQSGFGKDLGEEALNE 912
Cdd:PLN02315 407 FKT--LEEAIEINNSVPQGLSSSIFTRnpETIFKWIGPLGSDCGIVNVNIpTNGAEIGGAFGGEKATGGGREAGSDSWKQ 484
|
490
....*....|.
gi 238814322 913 YLKTKTVTLEY 923
Cdd:PLN02315 485 YMRRSTCTINY 495
|
|
| fmt |
TIGR00460 |
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than ... |
23-330 |
1.12e-49 |
|
methionyl-tRNA formyltransferase; The top-scoring characterized proteins other than methionyl-tRNA formyltransferase (fmt) itself are formyltetrahydrofolate dehydrogenases. The mitochondrial methionyl-tRNA formyltransferases are so divergent that, in a multiple alignment of bacterial fmt, mitochondrial fmt, and formyltetrahydrofolate dehydrogenases, the mitochondrial fmt appears the most different. However, because both bacterial and mitochondrial fmt are included in the seed alignment, all credible fmt sequences score higher than any non-fmt sequence. This enzyme modifies Met on initiator tRNA to f-Met. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273088 [Multi-domain] Cd Length: 313 Bit Score: 178.36 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 23 LKLALIGQSLFGQEVYSHLRKEGHRVVGVFTVPDKDG------KADPLALAAEKDGTPVFKLPKWRvkgktIKEVAEAYR 96
Cdd:TIGR00460 1 LRIVFFGTPTFSLPVLEELREDNFEVVGVVTQPDKPAgrgkklTPPPVKVLAEEKGIPVFQPEKQR-----QLEELPLVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 97 SVGAELNVLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDV 176
Cdd:TIGR00460 76 ELKPDVIVVVSFGKILPKEFLDLFPYGCINVHPSLLPRWRGGAPIQRAILNGDKKTGVTIMQMVPKMDAGDILKQETFPI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 177 EPNDTVDALYNRfLFPEGIKAMVEAVQLIADGKAPRIPQPEEGATYEGIQKKENAEISWDQSAEVLHNWIRGHDKVPGAW 256
Cdd:TIGR00460 156 EEEDNSGTLSDK-LSELGAQLLIETLKELPEGKNKPEPQDAEEATYAPKISKEQERIDWNQSAEELLNKIRALNPWPTAW 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 257 TEINGQMVTFYGSTLLNSSVPPGEPLEIKGAKKPGLvtkngLVLFGNDGkALTVRNLQFEDGKMIPASQYFSTG 330
Cdd:TIGR00460 235 LTFEGKNIKIHKAKVIDLSTYKAKPGEIVYHNKKGI-----LVACGKDG-ILLLLSLQPPGKKVMRAEDFYNGS 302
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
446-923 |
6.91e-49 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 183.79 E-value: 6.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTDADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:PLN02419 117 LIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFP--LWRNTPITTRQRVMLKFQELIRKNMDKLA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGAVytlaLKTHIGMSVQTFRYFAGWCDKiqgSTIPINQARPNRNL---TFTKKEPLGVCAIIIPWNYPLMMLA 602
Cdd:PLN02419 195 MNITTEQGKT----LKDSHGDIFRGLEVVEHACGM---ATLQMGEYLPNVSNgvdTYSIREPLGVCAGICPFNFPAMIPL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 603 WKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQrLSEHPDIRKLGFTGSTPIGKQIMKS 682
Cdd:PLN02419 268 WMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNA-ICDDEDIRAVSFVGSNTAGMHIYAR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 683 CAVSNlKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGR-LFVEESihDEFVTRVVEEIKKMKIGDPL 761
Cdd:PLN02419 347 AAAKG-KRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTvVFVGDA--KSWEDKLVERAKALKVTCGS 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 762 DRSTDHGPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGF----FMEPTVFTDVEDYMYLAKEESFGPIMVIskFQ 837
Cdd:PLN02419 424 EPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYekgnFIGPTILSGVTPDMECYKEEIFGPVLVC--MQ 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 838 NGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTynKTDVAAPFGGV--KQSGFGKDL---GEEALNE 912
Cdd:PLN02419 502 ANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINV--PIPVPLPFFSFtgNKASFAGDLnfyGKAGVDF 579
|
490
....*....|.
gi 238814322 913 YLKTKTVTLEY 923
Cdd:PLN02419 580 FTQIKLVTQKQ 590
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
443-918 |
1.35e-48 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 180.34 E-value: 1.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 443 YQCFINGQFTDADDGKTYDTINPTDGSTICKVSYASladvdkaVAAAKDAFENGE-----WGRMNARERGRLMYRLADLL 517
Cdd:PLN00412 16 YKYYADGEWRTSSSGKSVAITNPSTRKTQYKVQACT-------QEEVNKAMESAKaaqkaWAKTPLWKRAELLHKAAAIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 518 EENQEELAtiEALdsgaVYTLA-----LKTHIGMSVQTFRYFA-------GWCDKIQGSTIPINQarpnRN-LTFTKKEP 584
Cdd:PLN00412 89 KEHKAPIA--ECL----VKEIAkpakdAVTEVVRSGDLISYTAeegvrilGEGKFLVSDSFPGNE----RNkYCLTSKIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 585 LGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDI 664
Cdd:PLN00412 159 LGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGFPKGLISCVTGKGSEIGDFLTMHPGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 665 RKLGFTGSTpIGKQIMKSCAVSNLKkvsLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEF 744
Cdd:PLN00412 239 NCISFTGGD-TGIAISKKAGMVPLQ---MELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 745 VTRVVEEIKKMKIGDPLDRStDHGPQNHKAHLEKLLQYCETGVKEGATLVyggRQVQRPGFFMEPTVFTDVEDYMYLAKE 824
Cdd:PLN00412 315 VEKVNAKVAKLTVGPPEDDC-DITPVVSESSANFIEGLVMDAKEKGATFC---QEWKREGNLIWPLLLDNVRPDMRIAWE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 825 ESFGPIMVISKFqnGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFINTY-NKTDVAAPFGGVKQSGFGK 903
Cdd:PLN00412 391 EPFGPVLPVIRI--NSVEEGIHHCNASNFGLQGCVFTRDINKAILISDAMETGTVQINSApARGPDHFPFQGLKDSGIGS 468
|
490
....*....|....*
gi 238814322 904 DLGEEALNEYLKTKT 918
Cdd:PLN00412 469 QGITNSINMMTKVKS 483
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
446-920 |
2.13e-48 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 186.56 E-value: 2.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGqftdadDGKTYDTINPTDGS-TICKVSYASLADVDKAVAAAKDAFenGEWGRMNARERGRLMYRLADLLEENQEE- 523
Cdd:PRK11904 556 IING------EGEARPVVSPADRRrVVGEVAFADAEQVEQALAAARAAF--PAWSRTPVEERAAILERAADLLEANRAEl 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 524 --LATIEAldsGavytlalKT-HIGMS-----VQTFRYFAgwcdkiqgstipiNQARpnrnLTFTKKEPL---------- 585
Cdd:PRK11904 628 iaLCVREA---G-------KTlQDAIAevreaVDFCRYYA-------------AQAR----RLFGAPEKLpgptgesnel 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 586 -----GVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSE 660
Cdd:PRK11904 681 rlhgrGVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGIPKDVLQLLPGDGATVGAALTA 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 661 HPDIRKLGFTGSTPIGKQIMKSCAVSNLKKVSL--ELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEE 738
Cdd:PRK11904 761 DPRIAGVAFTGSTETARIINRTLAARDGPIVPLiaETGGQNAMIVDSTALPEQVVDDVVTSAFRSAGQRCSALRVLFVQE 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 739 SIHDefvtRVVEEIK----KMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETgVKEGATLVYggrQVQRP-----GFFMEP 809
Cdd:PRK11904 841 DIAD----RVIEMLKgamaELKVGDPRLLSTDVGPVIDAEAKANLDAHIER-MKREARLLA---QLPLPagtenGHFVAP 912
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 810 TVFtDVEDYMYLaKEESFGPIMVISKFQNGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIntyNKTDV 889
Cdd:PRK11904 913 TAF-EIDSISQL-EREVFGPILHVIRYKASDLDKVIDAINATGYGLTLGIHSRIEETADRIADRVRVGNVYV---NRNQI 987
|
490 500 510
....*....|....*....|....*....|....*..
gi 238814322 890 AA-----PFGGVKQSGFG-KDLGEEALNEYLKTKTVT 920
Cdd:PRK11904 988 GAvvgvqPFGGQGLSGTGpKAGGPHYLLRFATEKTVT 1024
|
|
| FMT_core |
cd08369 |
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ... |
25-204 |
4.38e-48 |
|
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.
Pssm-ID: 187712 [Multi-domain] Cd Length: 173 Bit Score: 168.62 E-value: 4.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 25 LALIGQSLFGQEVYSHLR-KEGHRVVGVFTVPDKDGKADPLALAAEKdgtpvfkLPKWRVKGKTIKEVAEAYRSVGAELN 103
Cdd:cd08369 1 IVILGSGNIGQRVLKALLsKEGHEIVGVVTHPDSPRGTAQLSLELVG-------GKVYLDSNINTPELLELLKEFAPDLI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 104 VLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVD 183
Cdd:cd08369 74 VSINFRQIIPPEILKLPPGGAINIHPSLLPRYRGVNPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAG 153
|
170 180
....*....|....*....|.
gi 238814322 184 ALYNRfLFPEGIKAMVEAVQL 204
Cdd:cd08369 154 TLYQR-LIELGPKLLKEALQK 173
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
446-900 |
2.71e-45 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 170.52 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 446 FINGQFTdADDGKTYDTINPTDGSTICKVSYASLADVDKAVAAAKDAFEngEWGRMNARERGRLMYRLADLLEENQEELA 525
Cdd:PRK09457 4 WINGDWI-AGQGEAFESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFP--AWARLSFEERQAIVERFAALLEENKEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 526 TIEALDSGA--------VYTLALKthIGMSVQTFRYFAGwcdkIQGSTIPINQArpnrnltFTKKEPLGVCAIIIPWNYP 597
Cdd:PRK09457 81 EVIARETGKplweaateVTAMINK--IAISIQAYHERTG----EKRSEMADGAA-------VLRHRPHGVVAVFGPYNFP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 598 LMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGsGGIAGQRLSEHPDIRKLGFTGSTPIGK 677
Cdd:PRK09457 148 GHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGLPAGVLNLVQG-GRETGKALAAHPDIDGLLFTGSANTGY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 678 QIMKSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIH-DEFVTRVVEEIKKMK 756
Cdd:PRK09457 227 LLHRQFAGQPEKILALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 757 IGDPLDRSTDH-GPQNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVFtDVEDYMYLAKEESFGPIMVISK 835
Cdd:PRK09457 307 VGRWDAEPQPFmGAVISEQAAQGLVAAQAQLLALGGKSLLEMTQLQAGTGLLTPGII-DVTGVAELPDEEYFGPLLQVVR 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238814322 836 FQngDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVfinTYNK----TDVAAPFGGVKQSG 900
Cdd:PRK09457 386 YD--DFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRAGIV---NWNKpltgASSAAPFGGVGASG 449
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
453-902 |
3.94e-45 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 176.98 E-value: 3.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 453 DADDGKTYDTINPTD-GSTICKVSYASLADVDKAVAAAKDAFENgeWGRMNARERGRLMYRLADLLEENQEEL---ATIE 528
Cdd:PRK11905 562 GDVDGGTRPVLNPADhDDVVGTVTEASAEDVERALAAAQAAFPE--WSATPAAERAAILERAADLMEAHMPELfalAVRE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 529 AldsGAVYTLAlkthIGM---SVQTFRYFAgwcdkiqgstipiNQARpnRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKS 605
Cdd:PRK11905 640 A---GKTLANA----IAEvreAVDFLRYYA-------------AQAR--RLLNGPGHKPLGPVVCISPWNFPLAIFTGQI 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 606 AACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAV 685
Cdd:PRK11905 698 AAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPKDALQLLPGDGRTVGAALVADPRIAGVMFTGSTEVARLIQRTLAK 777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 686 SNLKKVSL--ELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDR 763
Cdd:PRK11905 778 RSGPPVPLiaETGGQNAMIVDSSALPEQVVADVIASAFDSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRL 857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 764 STDHGPQNHKAHLEKLLQYCETGVKEGaTLVYggrQVQRP-----GFFMEPTVFtDVEDYMYLaKEESFGPIMVISKFQN 838
Cdd:PRK11905 858 STDVGPVIDAEAQANIEAHIEAMRAAG-RLVH---QLPLPaetekGTFVAPTLI-EIDSISDL-EREVFGPVLHVVRFKA 931
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 839 GDIDGVLQRANSTEYGLASGVFTRdINKAM-YVSEKLEAGTVFIntyNKTDVAA-----PFGGVKQSGFG 902
Cdd:PRK11905 932 DELDRVIDDINATGYGLTFGLHSR-IDETIaHVTSRIRAGNIYV---NRNIIGAvvgvqPFGGEGLSGTG 997
|
|
| FMT_core_Met-tRNA-FMT_N |
cd08646 |
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ... |
23-222 |
5.55e-45 |
|
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187715 [Multi-domain] Cd Length: 204 Bit Score: 161.07 E-value: 5.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 23 LKLALIGQSLFGQEVYSHLRKEGHRVVGVFTVPDKD---GK---ADPLALAAEKDGTPVFKLPKWRvkgktIKEVAEAYR 96
Cdd:cd08646 1 MRIVFMGTPDFAVPSLEALLKSGHEVVAVVTQPDKPrgrGKkltPSPVKELALELGLPVLQPEKLK-----DEEFLEELK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 97 SVGAELNVLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDV 176
Cdd:cd08646 76 ALKPDLIVVVAYGQILPKEILDLPPYGCINVHPSLLPKYRGAAPIQRAILNGDKETGVTIMKMDEGLDTGDILAQEEVPI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 238814322 177 EPNDTVDALYNRfLFPEGIKAMVEAVQLIADGKAPRIPQPEEGATY 222
Cdd:cd08646 156 DPDDTAGELLDK-LAELGADLLLEVLDDIEAGKLNPVPQDESEATY 200
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
498-902 |
9.55e-45 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 175.51 E-value: 9.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 498 WGRMNARERGRLMYRLADLLEENQEELATI-----------------EALDsgavytlalkthigmsvqtF-RYFAgwcd 559
Cdd:COG4230 609 WSATPVEERAAILERAADLLEAHRAELMALlvreagktlpdaiaevrEAVD-------------------FcRYYA---- 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 560 kiqgstipiNQARpNRNLTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGF 639
Cdd:COG4230 666 ---------AQAR-RLFAAPTVLRGRGVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGV 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 640 PKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVSNLKKVSL--ELGGKSPLIIfnD----CEldKAV 713
Cdd:COG4230 736 PADVLQLLPGDGETVGAALVADPRIAGVAFTGSTETARLINRTLAARDGPIVPLiaETGGQNAMIV--DssalPE--QVV 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 714 RMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETGVKEGaTL 793
Cdd:COG4230 812 DDVLASAFDSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG-RL 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 794 VYggrQVQRP-----GFFMEPTVF--TDVEDymyLaKEESFGPIMVISKFQNGDIDGVLQRANSTEYGLASGVFTRdINK 866
Cdd:COG4230 891 VH---QLPLPeecanGTFVAPTLIeiDSISD---L-EREVFGPVLHVVRYKADELDKVIDAINATGYGLTLGVHSR-IDE 962
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 238814322 867 -AMYVSEKLEAGTVFIntyNKTDVAA-----PFGGVKQSGFG 902
Cdd:COG4230 963 tIDRVAARARVGNVYV---NRNIIGAvvgvqPFGGEGLSGTG 1001
|
|
| FMT_core_like_2 |
cd08822 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
23-223 |
2.73e-44 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187724 [Multi-domain] Cd Length: 192 Bit Score: 158.39 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 23 LKLALIGQSLFGQEVYSHLRKEGHRVVGVfTVPDKDGKADPLALAAEKDGTPVFKLPKwrVKGKTIKEvaeayrsvGAEL 102
Cdd:cd08822 1 MKIAIAGQKWFGTAVLEALRARGIALLGV-AAPEEGDRLAAAARTAGSRGLPRAGVAV--LPADAIPP--------GTDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 103 NVLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTV 182
Cdd:cd08822 70 IVAAHCHAFISAKTRARARLGAIGYHPSLLPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGDTA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 238814322 183 DALYNRFLFPEGIKAMVEAVQ-LIADGKAPRIPQPEEGATYE 223
Cdd:cd08822 150 AELWRRALAPMGVKLLTQVIDaLLRGGNLPAQPQDERLATWE 191
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
497-900 |
1.81e-40 |
|
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: 156.98 E-value: 1.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEelatiealdsgavYTLALKTHIGMS--------------VQTFRYFAGWCDKIQ 562
Cdd:cd07123 84 EWARMPFEDRAAIFLKAADLLSGKYR-------------YELNAATMLGQGknvwqaeidaacelIDFLRFNVKYAEELY 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 563 GSTiPINQARPNRNltFTKKEPL-GVCAIIIPWNY----------PLMMlawksaaclaaGNTLVLKPAQVTPLTALKFA 631
Cdd:cd07123 151 AQQ-PLSSPAGVWN--RLEYRPLeGFVYAVSPFNFtaiggnlagaPALM-----------GNVVLWKPSDTAVLSNYLVY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 632 ELSVKAGFPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVS-----NLKKVSLELGGKSPLIIFND 706
Cdd:cd07123 217 KILEEAGLPPGVINFVPGDGPVVGDTVLASPHLAGLHFTGSTPTFKSLWKQIGENldryrTYPRIVGETGGKNFHLVHPS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 707 CELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETG 786
Cdd:cd07123 297 ADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVIDEKAFDRIKGYIDHA 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 787 VKE-GATLVYGGRQVQRPGFFMEPTVFTdVEDYMY-LAKEESFGPIMVISKFQNGDIDGVLQRANST-EYGLASGVFTRD 863
Cdd:cd07123 377 KSDpEAEIIAGGKCDDSVGYFVEPTVIE-TTDPKHkLMTEEIFGPVLTVYVYPDSDFEETLELVDTTsPYALTGAIFAQD 455
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 238814322 864 ---INKAmyvSEKLE--AGTVFINTYNKTDVAA--PFGGVKQSG 900
Cdd:cd07123 456 rkaIREA---TDALRnaAGNFYINDKPTGAVVGqqPFGGARASG 496
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
572-912 |
3.84e-40 |
|
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: 154.30 E-value: 3.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 572 RPNRNLT------FTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVK----AGFPk 641
Cdd:cd07132 82 PVKKNLAtllddvYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKyldkECYP- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 642 gVINiipgsGGI--AGQRLSEHPDirKLGFTGSTPIGKQIMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGA 719
Cdd:cd07132 161 -VVL-----GGVeeTTELLKQRFD--YIFYTGSTSVGKIVMQA-AAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 720 VFFNKGENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDrSTDHGP---QNHKAHLEKLLqycetgvkEGATLVYG 796
Cdd:cd07132 232 KFINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKE-SPDYGRiinDRHFQRLKKLL--------SGGKVAIG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 797 GRQVQRPGfFMEPTVFTDVEDYMYLAKEESFGPIMVISKFQNgdIDGVLQRANSTEYGLASGVFTRD---INKAMyvsEK 873
Cdd:cd07132 303 GQTDEKER-YIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNN--LDEAIEFINSREKPLALYVFSNNkkvINKIL---SN 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238814322 874 LEAGTVFINtynktDV-------AAPFGGVKQSGFG-------------------KDLGEEALNE 912
Cdd:cd07132 377 TSSGGVCVN-----DTimhytldSLPFGGVGNSGMGayhgkysfdtfshkrsclvKSLNMEKLNS 436
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
583-902 |
5.31e-37 |
|
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: 144.86 E-value: 5.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 583 EPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHP 662
Cdd:cd07137 100 EPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKL-IPEYLDTKAIKVIEGGVPETTALLEQKW 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 663 DirKLGFTGSTPIGKQIMkSCAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVF-FNKGENCIAAGRLFVEESIH 741
Cdd:cd07137 179 D--KIFFTGSPRVGRIIM-AAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQACIAPDYVLVEESFA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 742 DEFVTRVVEEIKKMKIGDPldRSTDHGPQ----NHKAHLEKLLQycETGVKegATLVYGGrQVQRPGFFMEPTVFTDVED 817
Cdd:cd07137 256 PTLIDALKNTLEKFFGENP--KESKDLSRivnsHHFQRLSRLLD--DPSVA--DKIVHGG-ERDEKNLYIEPTILLDPPL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 818 YMYLAKEESFGPIMVISKFQNgdIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVfinTYNKTDV-----AAP 892
Cdd:cd07137 329 DSSIMTEEIFGPLLPIITVKK--IEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGV---TFNDTVVqyaidTLP 403
|
330
....*....|
gi 238814322 893 FGGVKQSGFG 902
Cdd:cd07137 404 FGGVGESGFG 413
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
505-902 |
5.88e-34 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 141.26 E-value: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 505 ERGRLMYRLADLLEENQEELATIEALDSGAVYTLALkTHIGMSVQTFRYFAGwcdkiqgstipinQARPnrnlTFTKK-- 582
Cdd:PRK11809 705 ERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAI-AEVREAVDFLRYYAG-------------QVRD----DFDNDth 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 583 EPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEHP 662
Cdd:PRK11809 767 RPLGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGVPAGVVQLLPGRGETVGAALVADA 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 663 DIRKLGFTGSTPIGKQIMKSCAvSNL----KKVSL--ELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFV 736
Cdd:PRK11809 847 RVRGVMFTGSTEVARLLQRNLA-GRLdpqgRPIPLiaETGGQNAMIVDSSALTEQVVADVLASAFDSAGQRCSALRVLCL 925
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 737 EESIHDEFVTRVVEEIKKMKIGDPlDR-STDHGP---QNHKAHLEKLLQYCETGVKEGATLVYGGRQVQRPGFFMEPTVF 812
Cdd:PRK11809 926 QDDVADRTLKMLRGAMAECRMGNP-DRlSTDIGPvidAEAKANIERHIQAMRAKGRPVFQAARENSEDWQSGTFVPPTLI 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 813 tDVEDYMYLaKEESFGPIMVISKFQNGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVFIntyNKTDVAA- 891
Cdd:PRK11809 1005 -ELDSFDEL-KREVFGPVLHVVRYNRNQLDELIEQINASGYGLTLGVHTRIDETIAQVTGSAHVGNLYV---NRNMVGAv 1079
|
410
....*....|....*
gi 238814322 892 ----PFGGVKQSGFG 902
Cdd:PRK11809 1080 vgvqPFGGEGLSGTG 1094
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
583-903 |
2.86e-29 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 122.91 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 583 EPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTAlKFAELSVKAGFPKGVINIIPGsGGIAGQRLSEHP 662
Cdd:PLN02203 107 EPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATS-AFLAANIPKYLDSKAVKVIEG-GPAVGEQLLQHK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 663 -DirKLGFTGSTPIGKQIMkSCAVSNLKKVSLELGGKSPLIIfnDC-----ELDKAVRMGMGAVFFN-KGENCIAAGRLF 735
Cdd:PLN02203 185 wD--KIFFTGSPRVGRIIM-TAAAKHLTPVALELGGKCPCIV--DSlsssrDTKVAVNRIVGGKWGScAGQACIAIDYVL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 736 VEEsihdEFVTRVVEEIKKMK---IGDPLDRSTDHGPQNHKAHLEKLLQYCETGvKEGATLVYGGrQVQRPGFFMEPTVF 812
Cdd:PLN02203 260 VEE----RFAPILIELLKSTIkkfFGENPRESKSMARILNKKHFQRLSNLLKDP-RVAASIVHGG-SIDEKKLFIEPTIL 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 813 TDVEDYMYLAKEESFGPIMVISKFQNgdIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVfinTYNKTDV--- 889
Cdd:PLN02203 334 LNPPLDSDIMTEEIFGPLLPIITVKK--IEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSV---TFNDAIIqya 408
|
330
....*....|....*.
gi 238814322 890 --AAPFGGVKQSGFGK 903
Cdd:PLN02203 409 cdSLPFGGVGESGFGR 424
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
496-915 |
4.29e-28 |
|
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: 118.49 E-value: 4.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 496 GEWGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALKthIGMSVQTFRYFAgwcDKIQGSTIPINQA-RPN 574
Cdd:cd07084 13 KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAEN--ICGDQVQLRARA---FVIYSYRIPHEPGnHLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 575 RNLTFTKKE---PLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAG-FPKGVINIIPGS 650
Cdd:cd07084 88 QGLKQQSHGyrwPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPPEDVTLINGD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 651 GGiAGQRLSEHPDIRKLGFTGSTPIGKQImkscaVSNLK--KVSLELGGKSPLIIFNDCE-----LDKAVR-MGMGAvff 722
Cdd:cd07084 168 GK-TMQALLLHPNPKMVLFTGSSRVAEKL-----ALDAKqaRIYLELAGFNWKVLGPDAQavdyvAWQCVQdMTACS--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 723 nkGENCIAAGRLFVEESIHDE-FVTRVVEEIKKMKIGDP-LDRSTDHGPQNHKAHLEKLLqycetgvkeGATLVYGGRQV 800
Cdd:cd07084 239 --GQKCTAQSMLFVPENWSKTpLVEKLKALLARRKLEDLlLGPVQTFTTLAMIAHMENLL---------GSVLLFSGKEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 801 QR------PGFFMEPTVF--TDVEDYMYLA-KEESFGPIMVISKFQNGDIDGVLQRANSTEYGLASGVFTRDINKAMYVS 871
Cdd:cd07084 308 KNhsipsiYGACVASALFvpIDEILKTYELvTEEIFGPFAIVVEYKKDQLALVLELLERMHGSLTAAIYSNDPIFLQELI 387
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 238814322 872 EKLE-AGTVFINTYNKTDVAAP---FGGVKQSGFGKDLG-EEALNEYLK 915
Cdd:cd07084 388 GNLWvAGRTYAILRGRTGVAPNqnhGGGPAADPRGAGIGgPEAIKLVWR 436
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
583-919 |
2.92e-27 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 116.68 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 583 EPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELsVKAGFPKGVINIIPGSGGIAGQRLSEHP 662
Cdd:PLN02174 111 EPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKL-LEQYLDSSAVRVVEGAVTETTALLEQKW 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 663 DirKLGFTGSTPIGKQIMkSCAVSNLKKVSLELGGKSPLIIFNDCELDKAV-RMGMGAVFFNKGENCIAAGRLFVEESIH 741
Cdd:PLN02174 190 D--KIFYTGSSKIGRVIM-AAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVrRIIAGKWGCNNGQACISPDYILTTKEYA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 742 DEFVTRVVEEIKKMKIGDPLDrSTDHG---PQNHKAHLEKLLQYCETGVKegatLVYGGRQvQRPGFFMEPTVFTDVEDY 818
Cdd:PLN02174 267 PKVIDAMKKELETFYGKNPME-SKDMSrivNSTHFDRLSKLLDEKEVSDK----IVYGGEK-DRENLKIAPTILLDVPLD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 819 MYLAKEESFGPIMVISKFQNGD--IDGVLQRANSteygLASGVFTRDINKAMYVSEKLEAGTVFINtynktDVAA----- 891
Cdd:PLN02174 341 SLIMSEEIFGPLLPILTLNNLEesFDVIRSRPKP----LAAYLFTHNKKLKERFAATVSAGGIVVN-----DIAVhlalh 411
|
330 340 350
....*....|....*....|....*....|
gi 238814322 892 --PFGGVKQSGFGKDLGEEALNEYLKTKTV 919
Cdd:PLN02174 412 tlPFGGVGESGMGAYHGKFSFDAFSHKKAV 441
|
|
| PRK06988 |
PRK06988 |
formyltransferase; |
112-326 |
6.38e-26 |
|
formyltransferase;
Pssm-ID: 235902 [Multi-domain] Cd Length: 312 Bit Score: 109.40 E-value: 6.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 112 IPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNrflf 191
Cdd:PRK06988 90 IPVDLLALAPRGAYNMHGSLLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVDQTAVPILPDDTAAQVFD---- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 192 pegiKAMVEAVQLIA-------DGKAPRIPQPEEGATYEGIQKKENAEISWDQSAEVLHNWIRG-HDKVPGAWTEINGQM 263
Cdd:PRK06988 166 ----KVTVAAEQTLWrvlpallAGEAPHLPNDLAQGSYFGGRKPEDGRIDWSKPAAQVYNLIRAvAPPYPGAFTDLGGTR 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238814322 264 VtfygstLLNSSVPPGEPLEIKGAKKPGL-VTKNGLVLFGNDGKA---LTVRNLQFEDGKMIPASQY 326
Cdd:PRK06988 242 F------VVARARLAAPGAAAARDLPPGLhVSDNALFGVCGDGRAvsiLELRRQQDGGETVVTPAQF 302
|
|
| FMT_core_like_4 |
cd08651 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
24-205 |
9.29e-26 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187720 [Multi-domain] Cd Length: 180 Bit Score: 105.04 E-value: 9.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 24 KLALIGQSLFGQEVYSHLRKEGHRVVGVFTVPDKDGKADP----LALAAEKDGTPVFKLpkwrvkgKTI--KEVAEAYRS 97
Cdd:cd08651 1 RIVFIGCVEFSLIALEAILEAGGEVVGVITLDDSSSNNDSdyldLDSFARKNGIPYYKF-------TDIndEEIIEWIKE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 98 VGAELNvlpFC---TQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSC 174
Cdd:cd08651 74 ANPDII---FVfgwSQLLKPEILAIPRLGVIGFHPTKLPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPF 150
|
170 180 190
....*....|....*....|....*....|.
gi 238814322 175 DVEPNDTVDALYNRFlfpegIKAMVEAVQLI 205
Cdd:cd08651 151 PIDKDDTANSLYDKI-----MEAAKQQIDKF 176
|
|
| PLN02285 |
PLN02285 |
methionyl-tRNA formyltransferase |
48-326 |
8.12e-23 |
|
methionyl-tRNA formyltransferase
Pssm-ID: 215159 [Multi-domain] Cd Length: 334 Bit Score: 100.54 E-value: 8.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 48 VVGVFTVPDKDGK------ADPLALAAEKDGTP---VFKLPKWRVKGktikeVAEAYRSVGAELNVLPFCTQFIPMDIID 118
Cdd:PLN02285 38 VAAVVTQPPARRGrgrklmPSPVAQLALDRGFPpdlIFTPEKAGEED-----FLSALRELQPDLCITAAYGNILPQKFLD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 119 SPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRfLFPEGIKAM 198
Cdd:PLN02285 113 IPKLGTVNIHPSLLPLYRGAAPVQRALQDGVNETGVSVAFTVRALDAGPVIAQERVEVDEDIKAPELLPL-LFELGTKLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 199 VEAVQLIADGKAPRI--PQPEEGATYEGIQKKENAEISWDQSAEVLHNWIRGHDKVPGawteingqmvTFYGSTLLNSSV 276
Cdd:PLN02285 192 LRELPSVLDGSAKDKatPQDDSKATHAPKISPEESWLSFDEEARVLHNKVRAFAGWPG----------TRAKFQLVDDGD 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 277 PPGEPLEIK--------------GAKKPGLVTKNGLVLFGNDGKALTVRNLQFEDGKMIPASQY 326
Cdd:PLN02285 262 GEREVLELKiittrvceaggeqtGSADAVTFKKDSLLVPCGGGTWLEVLEVQPPGKKVMKAKDF 325
|
|
| Formyl_trans_C |
pfam02911 |
Formyl transferase, C-terminal domain; |
227-327 |
1.95e-21 |
|
Formyl transferase, C-terminal domain;
Pssm-ID: 460744 [Multi-domain] Cd Length: 99 Bit Score: 89.64 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 227 KKENAEISWDQSAEVLHNWIRGHDKVPGAWTEINGQMVTFYGStllnssvppgEPLEIKGAKKPGLV--TKNGLVLFGND 304
Cdd:pfam02911 3 KKEDGRIDWNQPAEEIHRLIRALDPWPGAYTFLNGKRVKLLKA----------SVLDQESGAAPGTIvtVDKGGLLVACG 72
|
90 100
....*....|....*....|...
gi 238814322 305 GKALTVRNLQFEDGKMIPASQYF 327
Cdd:pfam02911 73 DGALLILELQLEGKKPMSAEDFL 95
|
|
| PRK08125 |
PRK08125 |
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ... |
115-325 |
1.53e-20 |
|
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;
Pssm-ID: 236156 [Multi-domain] Cd Length: 660 Bit Score: 96.98 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 115 DIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRFLFPEG 194
Cdd:PRK08125 91 EILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAAR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 195 iKAMVEAVQLIADGKAPRIPQPEEGATYEGIQKKENAEISWDQSAEVLHNWIRG-HDKVPGAWTEINGQMVTFYGSTlln 273
Cdd:PRK08125 171 -QLLEQTLPAIKHGNIPEIPQDESQATYFGRRTPADGLIDWHKPASTLHNLVRAvTDPWPGAFSYVGEQKFTVWSSR--- 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 238814322 274 ssVPPGEPleikgAKKPGLV-TKNGLVLFGNDGkALTVRNLQFEDGKMIPASQ 325
Cdd:PRK08125 247 --VLPDAS-----GAQPGTVlSVAPLRIACGEG-ALEIVTGQAGDGLYMQGSQ 291
|
|
| FMT_core_ArnA_N |
cd08644 |
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ... |
39-224 |
2.02e-20 |
|
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.
Pssm-ID: 187713 [Multi-domain] Cd Length: 203 Bit Score: 90.48 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 39 SHLRKEGHRVVGVFTVPDKDGKA---DPLALAAEKDGTPVF-----KLPKWRvkgktikevaEAYRSVGAELNVLPFCTQ 110
Cdd:cd08644 17 EALLAAGFEVVAVFTHTDNPGENiwfGSVAQLAREHGIPVFtpddiNHPEWV----------ERLRALKPDLIFSFYYRH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 111 FIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRFL 190
Cdd:cd08644 87 MISEDILEIARLGAFNLHGSLLPKYRGRAPLNWALINGETETGVTLHRMTKKPDAGAIVDQEKVPILPDDTAKSLFHKLC 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 238814322 191 FPEGikaMVEAVQL--IADGKAPRIPQPEEGATYEG 224
Cdd:cd08644 167 VAAR---RLLARTLpaLKAGKARERPQDETQASYFG 199
|
|
| PurN |
COG0299 |
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ... |
47-209 |
2.46e-19 |
|
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440068 [Multi-domain] Cd Length: 202 Bit Score: 87.01 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 47 RVVGVFTvpdkDgKADPLALA-AEKDGTPVFKLPKWRVKGKTI--KEVAEAYRSVGAELNVL---------PFCTQFipm 114
Cdd:COG0299 30 EIVLVIS----N-RPDAYGLErARAAGIPTFVLDHKDFPSREAfdAALLEALDAYGPDLVVLagfmriltpEFVRAF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 115 diidspkHGSII-YHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRFLfPE 193
Cdd:COG0299 102 -------PGRIInIHPSLLPAFPGLHAHRQALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAARIL-EQ 173
|
170
....*....|....*.
gi 238814322 194 GIKAMVEAVQLIADGK 209
Cdd:COG0299 174 EHRLYPEAIRLLAEGR 189
|
|
| Met_tRNA_FMT_C |
cd08704 |
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ... |
229-323 |
1.55e-16 |
|
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.
Pssm-ID: 187732 [Multi-domain] Cd Length: 87 Bit Score: 75.26 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 229 ENAEISWDQSAEVLHNWIRGHDKVPGAWTEINGQMVTFYGSTLLNSSVPPGEPLEIKgakkpglVTKNGLVLFGNDGkAL 308
Cdd:cd08704 1 EEGRIDWSKSAEEIHNLIRALNPWPGAYTTLNGKRLKILKAEVLEESGEAAPGTILA-------VDKKGLLVACGDG-AL 72
|
90
....*....|....*
gi 238814322 309 TVRNLQFEDGKMIPA 323
Cdd:cd08704 73 EILELQPEGKKRMSA 87
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
504-830 |
5.11e-15 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 78.98 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 504 RERGRLMYRLADLLEENQEELATIEALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDKIQGStipinQARPNRNLTFTKKE 583
Cdd:PRK11903 63 AQRAALLAAIVKVLQANRDAYYDIATANSGTTRNDS-AVDIDGGIFTLGYYAKLGAALGDA-----RLLRDGEAVQLGKD 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 584 PL-----------GVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAG-FPKGVINIIPGSG 651
Cdd:PRK11903 137 PAfqgqhvlvptrGVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPAGALSVVCGSS 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 652 GIAGQRLSEHpDIrkLGFTGSTPIGKQIMKSCAV------SNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKG 725
Cdd:PRK11903 217 AGLLDHLQPF-DV--VSFTGSAETAAVLRSHPAVvqrsvrVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 726 ENCIAAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETgVKEGATLVYGGRQVQRP-- 803
Cdd:PRK11903 294 QKCTAIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGGGFALVda 372
|
330 340 350
....*....|....*....|....*....|...
gi 238814322 804 ----GFFMEPTVF--TDVEDYMYLAKEESFGPI 830
Cdd:PRK11903 373 dpavAACVGPTLLgaSDPDAATAVHDVEVFGPV 405
|
|
| FMT_core_like_3 |
cd08653 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
90-202 |
1.47e-14 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187721 [Multi-domain] Cd Length: 152 Bit Score: 71.86 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 90 EVAEAYRSVGAELNVLPFCtQFIPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGD-KKAGFSVFWADDGLDTGPI 168
Cdd:cd08653 38 EVVAALRALAPDVVSVYGC-GIIKDALLAIPPLGVLNLHGGILPDYRGVHTGFWALANGDpDNVGVTVHLVDAGIDTGDV 116
|
90 100 110
....*....|....*....|....*....|....
gi 238814322 169 LLQRSCDVEPNDTVDALYNRfLFPEGIKAMVEAV 202
Cdd:cd08653 117 LAQARPPLAAGDTLLSLYLR-LYRAGVELMVEAI 149
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
497-829 |
4.28e-14 |
|
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: 75.66 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 497 EWGRMNARERGRLMYRLADLLEENQEELATIEALDSGavYTLALKT-HIGMSVQTFRYFA------GWCDKIQGSTIPIN 569
Cdd:cd07129 14 SYRALSPARRAAFLEAIADEIEALGDELVARAHAETG--LPEARLQgELGRTTGQLRLFAdlvregSWLDARIDPADPDR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 570 QARPNRNLTFTKKePLGVCAIIIPWNYPLmmlAWK-----SAACLAAGNTLVLK--PAQvtPLTALKFAELSVKA----G 638
Cdd:cd07129 92 QPLPRPDLRRMLV-PLGPVAVFGASNFPL---AFSvaggdTASALAAGCPVVVKahPAH--PGTSELVARAIRAAlratG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 639 FPKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCAVSNL-KKVSLELGGKSPLIIFNDCELDKAV---- 713
Cdd:cd07129 166 LPAGVFSLLQGGGREVGVALVKHPAIKAVGFTGSRRGGRALFDAAAARPEpIPFYAELGSVNPVFILPGALAERGEaiaq 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 714 ----RMGMGAvffnkGENCIAAGRLFVEESIH-DEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLqycetgvk 788
Cdd:cd07129 246 gfvgSLTLGA-----GQFCTNPGLVLVPAGPAgDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEALAAAP-------- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 238814322 789 eGATLVYGGrQVQRPGFFMEPTVF-TDVEDYM--YLAKEESFGP 829
Cdd:cd07129 313 -GVRVLAGG-AAAEGGNQAAPTLFkVDAAAFLadPALQEEVFGP 354
|
|
| FMT_core_GART |
cd08645 |
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); ... |
128-198 |
1.29e-13 |
|
Phosphoribosylglycinamide formyltransferase (GAR transformylase, GART); Phosphoribosylglycinamide formyltransferase, also known as GAR transformylase or GART, is an essential enzyme that catalyzes the third step in de novo purine biosynthesis. This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. In prokaryotes, GART is a single domain protein but in most eukaryotes it is the C-terminal portion of a large multifunctional protein which also contains GAR synthetase and aminoimidazole ribonucleotide synthetase activities.
Pssm-ID: 187714 [Multi-domain] Cd Length: 183 Bit Score: 70.11 E-value: 1.29e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238814322 128 HPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRF------LFPEGIKAM 198
Cdd:cd08645 107 HPSLLPKFYGLHAHEAALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPGDTPETLAERIhalehrLYPEAIKLL 183
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
584-880 |
2.01e-13 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 73.68 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 584 PLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAGFPKGVINIIPGSGGIAGQRLSEhPD 663
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATDVDLIHSDGPTMNKILLE-AN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 664 IRKLGFTGSTPIGKQImkscAVSNLKKVSLELGGKSPLIIFNDC-ELDKAVRMGMGAVFFNKGENCIAAGRLFVEESIHD 742
Cdd:cd07126 221 PRMTLFTGSSKVAERL----ALELHGKVKLEDAGFDWKILGPDVsDVDYVAWQCDQDAYACSGQKCSAQSILFAHENWVQ 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 743 efvTRVVEEIKKMKIGDPLDRSTDhGP------QNHKAHLEKLLQYcetgvkEGATLVYGGRQVQ---RPGFF--MEPT- 810
Cdd:cd07126 297 ---AGILDKLKALAEQRKLEDLTI-GPvltwttERILDHVDKLLAI------PGAKVLFGGKPLTnhsIPSIYgaYEPTa 366
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238814322 811 VFTDVEDYMY-----LAKEESFGPIMVISKFQNGDIDGVLQRANSTEYGLASGVFTRDINKAMYVSEKLEAGTVF 880
Cdd:cd07126 367 VFVPLEEIAIeenfeLVTTEVFGPFQVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNGTTY 441
|
|
| FMT_core_NRPS_like |
cd08649 |
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ... |
40-181 |
1.43e-12 |
|
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.
Pssm-ID: 187718 [Multi-domain] Cd Length: 166 Bit Score: 66.51 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 40 HLRKEGHRVVGVFTvpdkdgkADP-LALAAEKDGTPVFklpkwrvkgktikevaEAYRSVGAELNVLPFCTQF------- 111
Cdd:cd08649 17 QLLAAGHRIAAVVS-------TDPaIRAWAAAEGIAVL----------------EPGEALEELLSDEPFDWLFsivnlri 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 112 IPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDT 181
Cdd:cd08649 74 LPSEVLALPRKGAINFHDGPLPRYAGLNATSWALLAGETRHGVTWHRIEEGVDAGDILVQRPFDIAPDDT 143
|
|
| FMT_core_HypX_N |
cd08650 |
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ... |
35-206 |
3.78e-12 |
|
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain.
Pssm-ID: 187719 [Multi-domain] Cd Length: 151 Bit Score: 64.95 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 35 QEVYSHLRKEGHRVVGVFTVPDKdgkadplalaaekdgtpvfklpkwrvkgkTIKEVAEAYRsvgAELNVLPFCTQFIPM 114
Cdd:cd08650 15 QRAFLELRERGHEVSVEYALSDD-----------------------------EMREAVALFA---PDLIICPFLKKRIPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 115 DIIDspKHGSIIYHPSIlPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRFLFPEG 194
Cdd:cd08650 63 EIWS--NYPCLIVHPGI-VGDRGPSSLDWAILEGEKEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYRGEVTDAA 139
|
170
....*....|..
gi 238814322 195 IKAMVEAVQLIA 206
Cdd:cd08650 140 VKAVLEAVENFE 151
|
|
| FMT_core_like_5 |
cd08823 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
106-206 |
4.29e-12 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187725 [Multi-domain] Cd Length: 177 Bit Score: 65.54 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 106 PFCTQF---IPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTV 182
Cdd:cd08823 75 VVVFTFpyrIPQHILDLPPLGFYNLHPGLLPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDTY 154
|
90 100
....*....|....*....|....
gi 238814322 183 DALYNRfLFPEGIKAMVEAVQLIA 206
Cdd:cd08823 155 GLLCSR-LAMLAVGLLEELYQNLA 177
|
|
| PurN |
TIGR00639 |
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ... |
128-208 |
2.17e-11 |
|
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 161973 [Multi-domain] Cd Length: 190 Bit Score: 63.93 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 128 HPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRFLFPEGiKAMVEAVQLIAD 207
Cdd:TIGR00639 108 HPSLLPAFPGLHAVEQALEAGVKESGCTVHYVDEEVDTGPIIAQAKVPILPEDTEETLEQRIHKQEH-RIYPLAIAWFAQ 186
|
.
gi 238814322 208 G 208
Cdd:TIGR00639 187 G 187
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
444-863 |
2.32e-11 |
|
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: 67.29 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 444 QCFINGQFTdADDGKTYDTINPTDGSTICKVSYASLADVDKAvaaakdafengEWGR---------MNARERGRLMYRLA 514
Cdd:cd07128 2 QSYVAGQWH-AGTGDGRTLHDAVTGEVVARVSSEGLDFAAAV-----------AYARekggpalraLTFHERAAMLKALA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 515 DLLEENQEELATIeALDSGAVYTLAlKTHIGMSVQTFRYFAGWCDK--------IQGSTIPINqarpnRNLTFTKKEPL- 585
Cdd:cd07128 70 KYLMERKEDLYAL-SAATGATRRDS-WIDIDGGIGTLFAYASLGRRelpnahflVEGDVEPLS-----KDGTFVGQHILt 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 586 ---GVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKPAQVTPLTALKFAELSVKAG-FPKGVINIIPGSGGiagqRLSEH 661
Cdd:cd07128 143 prrGVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQLICGSVG----DLLDH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 662 PDIRK-LGFTGSTPIGKQIMKSCAVS------NLKKVSLELGGKSPLIIFNDCELDKAVR-----MGMGAvffnkGENCI 729
Cdd:cd07128 219 LGEQDvVAFTGSAATAAKLRAHPNIVarsirfNAEADSLNAAILGPDATPGTPEFDLFVKevareMTVKA-----GQKCT 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 730 AAGRLFVEESIHDEFVTRVVEEIKKMKIGDPLDRSTDHGPQNHKAHLEKLLQYCETgVKEGATLVYGGRQVQRP------ 803
Cdd:cd07128 294 AIRRAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGPDRFEVvgadae 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238814322 804 -GFFMEPTVF--------TDVEDYmylakeESFGPimVISKFQNGDIDGVLQRANSTEYGLASGVFTRD 863
Cdd:cd07128 373 kGAFFPPTLLlcddpdaaTAVHDV------EAFGP--VATLMPYDSLAEAIELAARGRGSLVASVVTND 433
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
513-895 |
6.95e-10 |
|
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: 62.24 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 513 LADLLEENQEELATIEALDSGAVYTLALKTHIGM----------SVQTFRYFAGWCDKIQGSTipinqaRPNRNLTFTKK 582
Cdd:cd07077 25 IANALYDTRQRLASEAVSERGAYIRSLIANWIAMmgcsesklykNIDTERGITASVGHIQDVL------LPDNGETYVRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 583 EPLGVCAIIIPWNYPLMMLAwKSAACLAAGNTLVLKPAQVTPLTAlKFAELS----VKAGFPKGVINIIPGSGGIAGQRL 658
Cdd:cd07077 99 FPIGVTMHILPSTNPLSGIT-SALRGIATRNQCIFRPHPSAPFTN-RALALLfqaaDAAHGPKILVLYVPHPSDELAEEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 659 SEHPDIRKLGFTGSTPIGKQIMKScavSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNkGENCIAAGRLFVee 738
Cdd:cd07077 177 LSHPKIDLIVATGGRDAVDAAVKH---SPHIPVIGFGAGNSPVVVDETADEERASGSVHDSKFFD-QNACASEQNLYV-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 739 siHDEFVTRVVEEIKkmkigdpldrsTDHGPQNHKAHLEKLLQYCETGVKEgatlvyggrqvqrpgffmeptVFTDVEDY 818
Cdd:cd07077 251 --VDDVLDPLYEEFK-----------LKLVVEGLKVPQETKPLSKETTPSF---------------------DDEALESM 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238814322 819 MYLakEESFGPIMVISKFQNGdIDGVLqranstEYG--LASGVFTRDINKAMYVSEKLEAGTVFINTYNKTDVAAPFGG 895
Cdd:cd07077 297 TPL--ECQFRVLDVISAVENA-WMIIE------SGGgpHTRCVYTHKINKVDDFVQYIDTASFYPNESSKKGRGAFAGK 366
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
577-751 |
1.07e-08 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 58.43 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 577 LTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP----AQVTPLTALKFAELSVKAGFPKGVINIIPGSGG 652
Cdd:cd07081 88 GTLIIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPhpraKKVTQRAATLLLQAAVAAGAPENLIGWIDNPSI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 653 IAGQRLSEHPDIRKLGFTGstpiGKQIMKScAVSNLKKVSLELGGKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAG 732
Cdd:cd07081 168 ELAQRLMKFPGIGLLLATG----GPAVVKA-AYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQ 242
|
170
....*....|....*....
gi 238814322 733 RLFVEESIHDEFVTRVVEE 751
Cdd:cd07081 243 SVIVVDSVYDEVMRLFEGQ 261
|
|
| PRK07579 |
PRK07579 |
dTDP-4-amino-4,6-dideoxyglucose formyltransferase; |
108-256 |
3.56e-08 |
|
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
Pssm-ID: 236058 [Multi-domain] Cd Length: 245 Bit Score: 55.29 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 108 CTQFIPMDIIDSPKhgSIIYHPSILPRHRGASAINWTLImGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYN 187
Cdd:PRK07579 74 CKQRFPAKLVNGVR--CINIHPGFNPYNRGWFPQVFSII-NGLKIGATIHEMDEQLDHGPIIAQREVEIESWDSSGSVYA 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238814322 188 RFLFPEgIKAMVEAVQLIADGKAPRIpQPEEGATYEGIQK-KENAEISWDQSAEVLH--NWIRG--HDKVPGAW 256
Cdd:PRK07579 151 RVMDIE-RELVLEHFDAIRDGSYTAK-KPATEGNLNSKKDfKQLREIDLDERGTFRHfiNRLRAltHDDYKNAY 222
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
577-751 |
4.65e-08 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 56.45 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 577 LTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP----AQVTPLTALKFAELSVKAGFPKGVINIIPGSGG 652
Cdd:PRK15398 122 LTLIEYAPFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPhpgaKKVSLRAIELLNEAIVAAGGPENLVVTVAEPTI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 653 IAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCavsnlKKVSLELGGKSPLIIFNDCELDKAVR-MGMGAVFFNkgeN--CI 729
Cdd:PRK15398 202 ETAQRLMKHPGIALLVVTGGPAVVKAAMKSG-----KKAIGAGAGNPPVVVDETADIEKAARdIVKGASFDN---NlpCI 273
|
170 180
....*....|....*....|..
gi 238814322 730 AAGRLFVEESIHDEFVTRVVEE 751
Cdd:PRK15398 274 AEKEVIVVDSVADELMRLMEKN 295
|
|
| FMT_core_like_6 |
cd08820 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
107-203 |
6.95e-08 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187722 [Multi-domain] Cd Length: 173 Bit Score: 53.21 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 107 FCTQF---IPMDIIDSPKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVD 183
Cdd:cd08820 74 ISVQYhwiLPGSILEKAKEIAFNLHNAPLPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDCTVI 153
|
90 100
....*....|....*....|
gi 238814322 184 ALYNRFLFpEGIKAMVEAVQ 203
Cdd:cd08820 154 SLYILAHY-AAIALFGEHIT 172
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
577-751 |
8.21e-08 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 55.71 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 577 LTFTKKEPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP----AQVTPLTALKFAELSVKAGFPKGVINIIPGSGG 652
Cdd:cd07121 90 LTLVEYAPFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPhpgaKKVSAYAVELINKAIAEAGGPDNLVVTVEEPTI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 653 IAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCavsnlKKVSLELGGKSPLIIFNDCELDKAVR-MGMGAVFFNkgeN--CI 729
Cdd:cd07121 170 ETTNELMAHPDINLLVVTGGPAVVKAALSSG-----KKAIGAGAGNPPVVVDETADIEKAARdIVQGASFDN---NlpCI 241
|
170 180
....*....|....*....|..
gi 238814322 730 AAGRLFVEESIHDEFVTRVVEE 751
Cdd:cd07121 242 AEKEVIAVDSVADYLIAAMQRN 263
|
|
| Arna_FMT_C |
cd08702 |
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with ... |
229-320 |
1.14e-06 |
|
C-terminal subdomain of the formyltransferase domain on ArnA, which modifies lipid A with 4-amino-4-deoxy-l-arabinose; Domain found in ArnA with similarity to the C-terminal domain of Formyltransferase. ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal domain of ArnA is a dehydrogenase domain that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the N-terminal domain is a formyltransferase domain that catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the C-terminal subdomain of the formyltransferase domain, downstream of the N-terminal subdomain containing the catalytic center. ArnA forms a hexameric structure (a dimer of trimers), in which the dehydrogenase domains are arranged at the center with the transformylase domains on the outside of the complex.
Pssm-ID: 187730 Cd Length: 92 Bit Score: 47.62 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 229 ENAEISWDQSAEVLHNWIRG-HDKVPGAWTEINGQMVTFYGSTLLNSSVPPGEpleikgakkPGLV---TKNGLVLFGND 304
Cdd:cd08702 1 EDGLIDWRMSAREIYNLVRAvTKPYPGAFTFVGGQKIKIWKARPVDDAFYNGE---------PGKVlsvDGDPLIVACGD 71
|
90
....*....|....*.
gi 238814322 305 GkALTVRNLQFEDGKM 320
Cdd:cd08702 72 G-ALEILEAELDGGLP 86
|
|
| PLN02331 |
PLN02331 |
phosphoribosylglycinamide formyltransferase |
68-200 |
1.45e-06 |
|
phosphoribosylglycinamide formyltransferase
Pssm-ID: 177965 [Multi-domain] Cd Length: 207 Bit Score: 50.08 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 68 AEKDGTPVFKLPKWR--VKGKTIKEVAEAYRSVGAELNVLPFCTQFIPMDIIDSPKHGSIIYHPSILPRHRG----ASAI 141
Cdd:PLN02331 45 ARENGIPVLVYPKTKgePDGLSPDELVDALRGAGVDFVLLAGYLKLIPVELVRAYPRSILNIHPALLPAFGGkgyyGIKV 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238814322 142 NWTLIM-GDKKAGFSVFWADDGLDTGPILLQRSCDVEPNDTVDALYNRFL------FPEGIKAMVE 200
Cdd:PLN02331 125 HKAVIAsGARYSGPTVHFVDEHYDTGRILAQRVVPVLATDTPEELAARVLheehqlYVEVVAALCE 190
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
498-863 |
2.81e-06 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 50.94 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 498 WGRMNARERGRLMYRLADLLEENQEELATIEALDSGAVYTLALK---THI---GMSVQTFRYFAgwCDKIQGSTIPINQA 571
Cdd:cd07127 100 WRDAGARARAGVCLEILQRLNARSFEMAHAVMHTTGQAFMMAFQaggPHAqdrGLEAVAYAWRE--MSRIPPTAEWEKPQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 572 RPNRNLTFTKK---EPLGV-----CAIIIPWN-YPLMMlawksaACLAAGNTLVLKP--AQVTPL--TALKFAELSVKAG 638
Cdd:cd07127 178 GKHDPLAMEKTftvVPRGValvigCSTFPTWNgYPGLF------ASLATGNPVIVKPhpAAILPLaiTVQVAREVLAEAG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 639 F-PKGVINIIPGSGGIAGQRLSEHPDIRKLGFTGSTPIGKQIMKSCavsNLKKVSLELGGKSPLIIFNDCELDKAVRMGM 717
Cdd:cd07127 252 FdPNLVTLAADTPEEPIAQTLATRPEVRIIDFTGSNAFGDWLEANA---RQAQVYTEKAGVNTVVVDSTDDLKAMLRNLA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 718 GAVFFNKGENCIAAGRLFV---------EESIHDEFVTRVVEEIKKMkIGDPlDRSTD--HGPQNH--KAHLEKLLQyce 784
Cdd:cd07127 329 FSLSLYSGQMCTTPQNIYVprdgiqtddGRKSFDEVAADLAAAIDGL-LADP-ARAAAllGAIQSPdtLARIAEARQ--- 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 785 tgvkeGATLVYGGRQVQRPGfFMEPTVFT------DVEDYMYLAkEESFGPIMVISKFQNGDIDGVLQRANSTEYG-LAS 857
Cdd:cd07127 404 -----LGEVLLASEAVAHPE-FPDARVRTplllklDASDEAAYA-EERFGPIAFVVATDSTDHSIELARESVREHGaMTV 476
|
....*.
gi 238814322 858 GVFTRD 863
Cdd:cd07127 477 GVYSTD 482
|
|
| FMT_core_like_1 |
cd08821 |
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ... |
106-247 |
4.03e-04 |
|
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.
Pssm-ID: 187723 [Multi-domain] Cd Length: 211 Bit Score: 42.69 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 106 PFCTQFIPMDIIDspKHGSIIYHPSILPRHRGASAINWTLIMGDKKAGFSVFWADDGLDTGPILLQRscDVEPNDTVDAL 185
Cdd:cd08821 51 PHWSWIIPKEIFE--NFECVVFHMTDLPYGRGGSPLQNLIVRGHYETKISALKMEKGLDTGPIYLKR--DLSLKGTAEEI 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 238814322 186 YNRflFPEGIKAMVeaVQLIADGKAPrIPQPEEGATYEGiQKKENAEISWDQSAEVLHNWIR 247
Cdd:cd08821 127 YER--ASKISLKMI--PELVTKKPKP-IKQEGEPVTFKR-RTPEQSNISNEANLEKIYDFIR 182
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
346-390 |
4.53e-04 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 39.08 E-value: 4.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 238814322 346 ETIKVIWAGILS-NVPIIEDSTDFFKSGASSMDVARLVEEIRQKCG 390
Cdd:pfam00550 1 ERLRELLAEVLGvPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFG 46
|
|
| ALDH_F20_ACDH |
cd07122 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like; Coenzyme A acylating ... |
583-745 |
1.18e-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: 42.48 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 583 EPLGVCAIIIPWNYPLMMLAWKSAACLAAGNTLVLKP---AQVTPLTALKF-AELSVKAGFPKGVINIIPGSGGIAGQRL 658
Cdd:cd07122 94 EPVGVIAALIPSTNPTSTAIFKALIALKTRNAIIFSPhprAKKCSIEAAKImREAAVAAGAPEGLIQWIEEPSIELTQEL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238814322 659 SEHPDIRKLGFTGSTPigkqiMKSCAVSNlKKVSLELG-GKSPLIIFNDCELDKAVRMGMGAVFFNKGENCIAAGRLFVE 737
Cdd:cd07122 174 MKHPDVDLILATGGPG-----MVKAAYSS-GKPAIGVGpGNVPAYIDETADIKRAVKDIILSKTFDNGTICASEQSVIVD 247
|
....*...
gi 238814322 738 ESIHDEFV 745
Cdd:cd07122 248 DEIYDEVR 255
|
|
| |
