|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
25-454 |
0e+00 |
|
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: 728.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 25 VNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEYLAP 104
Cdd:cd07100 1 IEAALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEARAEVEKCAWICRYYAENAEAFLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 105 KLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEHLFQHLI 184
Cdd:cd07100 81 EPIETDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAGFPEGVFQNLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 185 VDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIA 264
Cdd:cd07100 161 IDSDQVEAIIADPRVRGVTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGRLQNAGQSCIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 265 AKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGIIPEGKGFYYPPT 344
Cdd:cd07100 241 AKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLRDELHEQVEEAVAAGATLLLGGKRPDGPGAFYPPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 345 LITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIATHeIEAGACFVNALVASDPRL 424
Cdd:cd07100 321 VLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARR-LEAGMVFINGMVKSDPRL 399
|
410 420 430
....*....|....*....|....*....|
gi 498339450 425 PFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07100 400 PFGGVKRSGYGRELGRFGIREFVNIKTVWV 429
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
1-452 |
1.83e-175 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 499.26 E-value: 1.83e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 1 MKIQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAG 80
Cdd:PRK09406 1 MPIATINPATGETVKTFTALTDDEVDAAIARAHARFRDYRTTTFAQRARWANAAADLLEAEADQVAALMTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 KAEINKCVWLCEHYAEHAEEYLAPKLIQTE---MKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAP 157
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLADEPADAAavgASRAYVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 158 VSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLV 237
Cdd:PRK09406 161 NVPQTALYLADLFRRAGFPDGCFQTLLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 238 LEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQV 317
Cdd:PRK09406 241 MPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVGDPTDPDTDVGPLATEQGRDEVEKQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 318 EKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLE 397
Cdd:PRK09406 321 DDAVAAGATILCGGKRPDGPGWFYPPTVITDITPDMRLYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 498339450 398 KGEHIAThEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:PRK09406 401 EQERFID-DLEAGQVFINGMTVSYPELPFGGVKRSGYGRELSAHGIREFCNIKTV 454
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
5-452 |
6.68e-164 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 470.11 E-value: 6.68e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:PRK13968 11 SVNPATGEQLSVLPWAGADDIENALQLAAAGFRDWRETNIDYRAQKLRDIGKALRARSEEMAQMITREMGKPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGN 164
Cdd:PRK13968 91 AKSANLCDWYAEHGPAMLKAEPTLVENQQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 165 KIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLD 244
Cdd:PRK13968 171 LIAQVFKDAGIPQGVYGWLNADNDGVSQMINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 245 LAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQG 324
Cdd:PRK13968 251 LAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPRDEENALGPMARFDLRDELHHQVEATLAEG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 325 AKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAT 404
Cdd:PRK13968 331 ARLLLGGEKIAGAGNYYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAA 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 498339450 405 hEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:PRK13968 411 -RLECGGVFINGYCASDARVAFGGVKKSGFGRELSHFGLHEFCNIQTV 457
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
3-455 |
6.80e-157 |
|
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: 453.04 E-value: 6.80e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:COG1012 23 FDVINPATGEVLARVPAATAEDVDAAVAAARAAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKPLAEARG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAEHAEEYLAPKL-IQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSG 161
Cdd:COG1012 103 EVDRAADFLRYYAGEARRLYGETIpSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 162 TGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVL 238
Cdd:COG1012 183 SALLLAELLEEAGLPAGVLN--VVTGDGSevgAALVAHPDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 239 EDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVE 318
Cdd:COG1012 261 DDADLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYDEFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 319 KSLKQGAKLLLGG-IIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLE 397
Cdd:COG1012 341 DAVAEGAELLTGGrRPDGEGGYFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLA 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 498339450 398 KGEHIAtHEIEAGACFVN-ALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAVS 455
Cdd:COG1012 421 RARRVA-RRLEAGMVWINdGTTGAVPQAPFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
2-452 |
8.98e-156 |
|
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: 449.29 E-value: 8.98e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 2 KIQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGK 81
Cdd:pfam00171 8 TIEVINPATGEVIATVPAATAEDVDAAIAAARAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKPLAEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 82 AEINKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSG 161
Cdd:pfam00171 88 GEVDRAIDVLRYYAGLARRLDGETLPSDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 162 TGNKIEELFLEAGFPEHLFQHLIVDNDGAAK-IIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLED 240
Cdd:pfam00171 168 TALLLAELFEEAGLPAGVLNVVTGSGAEVGEaLVEHPDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLED 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 241 ADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKS 320
Cdd:pfam00171 248 ADLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDTDMGPLISKAQLERVLKYVEDA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 321 LKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGE 400
Cdd:pfam00171 328 KEEGAKLLTGGEAGLDNGYFVEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERAL 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 498339450 401 HIAtHEIEAGACFVNALVASDPR-LPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:pfam00171 408 RVA-RRLEAGMVWINDYTTGDADgLPFGGFKQSGFGREGGPYGLEEYTEVKTV 459
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
26-454 |
1.36e-143 |
|
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: 417.38 E-value: 1.36e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 26 NERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEYLAPK 105
Cdd:cd07078 1 DAAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALGEVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 106 LIQTEM-KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEHLFQHLI 184
Cdd:cd07078 81 IPSPDPgELAIVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAGLPPGVLNVVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 185 VDNDGA-AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCI 263
Cdd:cd07078 161 GDGDEVgAALASHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQVCT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 264 AAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGIIPEG-KGFYYP 342
Cdd:cd07078 241 AASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAEGAKLLCGGKRLEGgKGYFVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 343 PTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAThEIEAGACFVNA-LVASD 421
Cdd:cd07078 321 PTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAE-RLEAGTVWINDySVGAE 399
|
410 420 430
....*....|....*....|....*....|...
gi 498339450 422 PRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07078 400 PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
6-454 |
5.60e-137 |
|
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: 401.04 E-value: 5.60e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEIN 85
Cdd:cd07103 2 INPATGEVIGEVPDAGAADADAAIDAAAAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKPLAEARGEVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 86 KCVWLCEHYAEHAE----EYLAPKLIQTEMKkakVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSG 161
Cdd:cd07103 82 YAASFLEWFAEEARriygRTIPSPAPGKRIL---VIKQPVGVVAAITPWNFPAAMITRKIAPALAAGCTVVLKPAEETPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 162 TGNKIEELFLEAGFPEHLFQHLIVDNDGAAK-IIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLED 240
Cdd:cd07103 159 SALALAELAEEAGLPAGVLNVVTGSPAEIGEaLCASPRVRKISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 241 ADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKS 320
Cdd:cd07103 239 ADLDKAVDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLKVGNGLDEGTDMGPLINERAVEKVEALVEDA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 321 LKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGE 400
Cdd:cd07103 319 VAKGAKVLTGGKRLGLGGYFYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAW 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 498339450 401 HIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07103 399 RVA-EALEAGMVGINTGLISDAEAPFGGVKESGLGREGGKEGLEEYLETKYVSL 451
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
6-452 |
1.05e-123 |
|
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: 367.34 E-value: 1.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEIN 85
Cdd:cd07102 1 ISPIDGSVIAERPLASLEAVRAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRPIAQAGGEIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 86 KCVWLCEHYAEHAEEYLAPKLIQTEMK-KAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGN 164
Cdd:cd07102 81 GMLERARYMISIAEEALADIRVPEKDGfERYIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 165 KIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLD 244
Cdd:cd07102 161 RFAAAFAEAGLPEGVFQVLHLSHETSAALIADPRIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 245 LAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQG 324
Cdd:cd07102 241 AAAESLVDGAFFNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 325 AKLLLGG---IIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEH 401
Cdd:cd07102 321 ARALIDGalfPEDKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEA 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 498339450 402 IAThEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07102 401 LGE-QLETGTVFMNRCDYLDPALAWTGVKDSGRGVTLSRLGYDQLTRPKSY 450
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
6-452 |
2.58e-121 |
|
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: 361.08 E-value: 2.58e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEIN 85
Cdd:cd07106 2 INPATGEVFASAPVASEAQLDQAVAAAKAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQFEVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 86 KCVWLCEHYAEHAeeyLAPKLIQ-TEMKKAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVLKHAPVSS 160
Cdd:cd07106 82 GAVAWLRYTASLD---LPDEVIEdDDTRRVELRRKPLGVVAAIVPWNFPLllaaWKI----APALLAGNTVVLKPSPFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 161 GTGNKIEELFLEAgFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLED 240
Cdd:cd07106 155 LCTLKLGELAQEV-LPPGVLNVVSGGDELGPALTSHPDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 241 ADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKS 320
Cdd:cd07106 234 VDIDAVAPKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVVGDGLDPGTTLGPVQNKMQYDKVKELVEDA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 321 LKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGE 400
Cdd:cd07106 314 KAKGAKVLAGGEPLDGPGYFIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 498339450 401 HIAThEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07106 394 AVAR-RLEAGTVWINTHGALDPDAPFGGHKQSGIGVEFGIEGLKEYTQTQVI 444
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
25-454 |
7.03e-118 |
|
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: 351.83 E-value: 7.03e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 25 VNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEYLAp 104
Cdd:cd07104 2 VDRAYAAAAAAQKAWAATPPQERAAILRKAAEILEERRDEIADWLIRESGSTRPKAAFEVGAAIAILREAAGLPRRPEG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 105 KLIQTEM--KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLK---HAPVSSGTgnKIEELFLEAGFPEHL 179
Cdd:cd07104 81 EILPSDVpgKESMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKpdsRTPVTGGL--LIAEIFEEAGLPKGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 180 FQHLIVDND--GAAkIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNN 257
Cdd:cd07104 159 LNVVPGGGSeiGDA-LVEHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 258 SGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGiipEGK 337
Cdd:cd07104 238 QGQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINERQVDRVHAIVEDAVAAGARLLTGG---TYE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 338 GFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAThEIEAGACFVNAL 417
Cdd:cd07104 315 GLFYQPTVLSDVTPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAE-RLETGMVHINDQ 393
|
410 420 430
....*....|....*....|....*....|....*...
gi 498339450 418 -VASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07104 394 tVNDEPHVPFGGVKASGGGRFGGPASLEEFTEWQWITV 431
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
3-454 |
1.86e-115 |
|
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: 346.64 E-value: 1.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSREEVREAIEVAEKAKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIEVGKPIKQSRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAEHAEEyLAPKLIQ------TEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLK-- 154
Cdd:cd07145 81 EVERTIRLFKLAAEEAKV-LRGETIPvdayeyNERRIAFTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKps 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 155 -HAPVssgTGNKIEELFLEAGFPEHLFQhlIVDNDG---AAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELG 230
Cdd:cd07145 160 sNTPL---TAIELAKILEEAGLPPGVIN--VVTGYGsevGDEIVTNPKVNMISFTGSTAVGLLIASKAGGTGKKVALELG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 231 GSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLR 310
Cdd:cd07145 235 GSDPMIVLKDADLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDESTDLGPLISPEAV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKSLKQGAKLLLGGIIPEgkGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:cd07145 315 ERMENLVNDAVEKGGKILYGGKRDE--GSFFPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQAS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498339450 391 VFTRDLEKGEHIAtHEIEAGACFVNalvaSDPR-----LPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07145 393 VFTNDINRALKVA-RELEAGGVVIN----DSTRfrwdnLPFGGFKKSGIGREGVRYTMLEMTEEKTIVI 456
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-454 |
3.10e-113 |
|
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: 340.74 E-value: 3.10e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEIN 85
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAEVAAAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGLEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 86 KCVWLCEHYAEHAEEYLAPKLIQTEM----KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSG 161
Cdd:cd07099 81 LALEAIDWAARNAPRVLAPRKVPTGLlmpnKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 162 TGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPhVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDA 241
Cdd:cd07099 161 VGELLAEAWAAAGPPQGVLQVVTGDGATGAALIDAG-VDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 242 DLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLArsdLRENLHI---QVE 318
Cdd:cd07099 240 DLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGADDIGDADIGPMT---TARQLDIvrrHVD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 319 KSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEK 398
Cdd:cd07099 317 DAVAKGAKALTGGARSNGGGPFYEPTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLAR 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 399 GEHIAThEIEAGACFVN--ALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07099 397 AEAIAR-RLEAGAVSINdvLLTAGIPALPFGGVKDSGGGRRHGAEGLREFCRPKAIAR 453
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
7-454 |
8.62e-111 |
|
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: 334.30 E-value: 8.62e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 7 NPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINK 86
Cdd:cd07150 5 NPADGSVYARVAVGSRQDAERAIAAAYDAFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDEGGSTYGKAWFETTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 87 CVWL-------CEHYAEHAEEYLAPKLIQTEMKKAkvchvsLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVS 159
Cdd:cd07150 85 TPELlraaageCRRVRGETLPSDSPGTVSMSVRRP------LGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEET 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 160 SGTGNKIEELFLEAGFPEHLFQhlIVDNDGAA---KIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYL 236
Cdd:cd07150 159 PVIGLKIAEIMEEAGLPKGVFN--VVTGGGAEvgdELVDDPRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 237 VLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQ 316
Cdd:cd07150 237 VLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPRDPDTVIGPLISPRQVERIKRQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 317 VEKSLKQGAKLLLGGiipEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDL 396
Cdd:cd07150 317 VEDAVAKGAKLLTGG---KYDGNFYQPTVLTDVTPDMRIFREETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 498339450 397 EKGEHIAThEIEAGACFVNALVASD-PRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07150 394 QRAFKLAE-RLESGMVHINDPTILDeAHVPFGGVKASGFGREGGEWSMEEFTELKWITV 451
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
3-452 |
2.47e-110 |
|
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: 333.85 E-value: 2.47e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07088 15 IDVLNPATGEVVATVPAATAEDADRAVDAAEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKTLSLARV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAEHAEEYLApKLIQTEMKKAK--VCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSS 160
Cdd:cd07088 95 EVEFTADYIDYMAEWARRIEG-EIIPSDRPNENifIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 161 GTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLV 237
Cdd:cd07088 174 LNALEFAELVDEAGLPAGVLN--IVTGRGSvvgDALVAHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 238 LEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQV 317
Cdd:cd07088 252 MKDADLDLAVKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLVNEAALDKVEEMV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 318 EKSLKQGAKLLLGGIIPE-GKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDL 396
Cdd:cd07088 332 ERAVEAGATLLTGGKRPEgEKGYFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENL 411
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498339450 397 EKGeHIATHEIEAGACFVNalvasdpRLPF-------GGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07088 412 NTA-MRATNELEFGETYIN-------RENFeamqgfhAGWKKSGLGGADGKHGLEEYLQTKVV 466
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
8-452 |
1.69e-109 |
|
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: 331.22 E-value: 1.69e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 8 PATEQIIQNYDCLNEQHVNERLNKAHETYLA--WKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEIN 85
Cdd:cd07118 4 PAHGVVVARYAEGTVEDVDAAVAAARKAFDKgpWPRMSGAERAAVLLKVADLIRARRERLALIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 86 KCVWLCEHYAE-----HAEEY--LAPKLIqtemkkAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPV 158
Cdd:cd07118 84 GAADLWRYAASlartlHGDSYnnLGDDML------GLVLREPIGVVGIITPWNFPFLILSQKLPFALAAGCTVVVKPSEF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 159 SSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPY 235
Cdd:cd07118 158 TSGTTLMLAELLIEAGLPAGVVN--IVTGYGAtvgQAMTEHPDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 236 LVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHI 315
Cdd:cd07118 236 IVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHESIADAFVAAVVARSRKVRVGDPLDPETKVGAIINEAQLAKITD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 316 QVEKSLKQGAKLLLGG-IIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTR 394
Cdd:cd07118 316 YVDAGRAEGATLLLGGeRLASAAGLFYQPTIFTDVTPDMAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSK 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 395 DLEKGEHIATHeIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07118 396 DIDTALTVARR-IRAGTVWVNTFLDGSPELPFGGFKQSGIGRELGRYGVEEYTELKTV 452
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
5-452 |
3.50e-109 |
|
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: 330.28 E-value: 3.50e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYL--AWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07114 1 SINPATGEPWARVPEASAADVDRAVAAARAAFEggAWRKLTPTERGKLLRRLADLIEANAEELAELETRDNGKLIRETRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCV-WLceHY----AEHAEEYLAPkliqteMKKAKV----CHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVL 153
Cdd:cd07114 81 QVRYLAeWY--RYyaglADKIEGAVIP------VDKGDYlnftRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 154 KHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELG 230
Cdd:cd07114 153 KPSEHTPASTLELAKLAEEAGFPPGVVN--VVTGFGPetgEALVEHPLVAKIAFTGGTETGRHIARAAAENLAPVTLELG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 231 GSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLR 310
Cdd:cd07114 231 GKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQMGPLATERQL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKSLKQGAKLLLGGIIPEG----KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYG 386
Cdd:cd07114 311 EKVERYVARAREEGARVLTGGERPSGadlgAGYFFEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498339450 387 LGAAVFTRDLEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07114 391 LAAGIWTRDLARA-HRVARAIEAGTVWVNTYRALSPSSPFGGFKDSGIGRENGIEAIREYTQTKSV 455
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
3-453 |
1.32e-108 |
|
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: 329.08 E-value: 1.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPIT-AGK 81
Cdd:cd07138 16 IDVINPATEEVIGTVPLGTAADVDRAVAAARRAFPAWSATSVEERAALLERIAEAYEARADELAQAITLEMGAPITlARA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 82 AEINKCVWLCEHYAEHAEEYLapklIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLK---HAPV 158
Cdd:cd07138 96 AQVGLGIGHLRAAADALKDFE----FEERRGNSLVVREPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKpseVAPL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 159 SSgtgNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPY 235
Cdd:cd07138 172 SA---IILAEILDEAGLPAGVFN--LVNGDGPvvgEALSAHPDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSAN 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 236 LVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLREnlHI 315
Cdd:cd07138 247 IILDDADLEKAVPRGVAACFANSGQSCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFD--RV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 316 Q--VEKSLKQGAKLLLGGI-IPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:cd07138 325 QgyIQKGIEEGARLVAGGPgRPEGleRGYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGY 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498339450 391 VFTRDLEKGEHIAtHEIEAGACFVNAlVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVA 453
Cdd:cd07138 405 VWSADPERARAVA-RRLRAGQVHING-AAFNPGAPFGGYKQSGNGREWGRYGLEEFLEVKSIQ 465
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
2-452 |
7.59e-107 |
|
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: 324.56 E-value: 7.59e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 2 KIQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLA--WKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPIT- 78
Cdd:cd07112 3 TFATINPATGRVLAEVAACDAADVDRAVAAARRAFESgvWSRLSPAERKAVLLRLADLIEAHRDELALLETLDMGKPISd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 79 AGKAEINKCVWLCEHYAEHAEE-Y--LAPKliqTEMKKAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAA 151
Cdd:cd07112 83 ALAVDVPSAANTFRWYAEAIDKvYgeVAPT---GPDALALITREPLGVVGAVVPWNFPLlmaaWKI----APALAAGNSV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 152 VLKHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDG--AAKII-ENPHVIAVTLTGSGRAGSAVASHAGKF-LKKSVL 227
Cdd:cd07112 156 VLKPAEQSPLTALRLAELALEAGLPAGVLN--VVPGFGhtAGEALgLHMDVDALAFTGSTEVGRRFLEYSGQSnLKRVWL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 228 ELGGSDPYLVLEDA-DLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLAR 306
Cdd:cd07112 234 ECGGKSPNIVFADApDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDPATRMGALVS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 307 SDLRENLHIQVEKSLKQGAKLLLGG--IIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSR 384
Cdd:cd07112 314 EAHFDKVLGYIESGKAEGARLVAGGkrVLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 385 YGLGAAVFTRDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07112 394 YGLAASVWTSDLSRAHRVA-RRLRAGTVWVNCFDEGDITTPFGGFKQSGNGRDKSLHALDKYTELKTT 460
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
24-454 |
1.66e-106 |
|
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: 322.60 E-value: 1.66e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 24 HVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHA----E 99
Cdd:cd07105 1 DADQAVEAAAAAFPAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEETGATAAWAGFNVDLAAGMLREAASLItqiiG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 100 EYLaPKLIQTEMkkAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEHL 179
Cdd:cd07105 81 GSI-PSDKPGTL--AMVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFHEAGLPKGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 180 FQHLIVDNDGAAKI----IENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRL 255
Cdd:cd07105 158 LNVVTHSPEDAPEVvealIAHPAVRKVNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 256 NNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDpldpkTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGIIP- 334
Cdd:cd07105 238 LNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAAAADRVKELVDDALSKGAKLVVGGLADe 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 335 EGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAtHEIEAGACFV 414
Cdd:cd07105 313 SPSGTSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVA-KRIESGAVHI 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 498339450 415 NAL-VASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07105 392 NGMtVHDEPTLPHGGVKSSGYGRFNGKWGIDEFTETKWITI 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
32-454 |
1.05e-105 |
|
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: 318.40 E-value: 1.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 32 AHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEYLAPKLIQTEM 111
Cdd:cd06534 3 ARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 112 -KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDG- 189
Cdd:cd06534 83 gGEAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAGLPPGVVN--VVPGGGd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 190 --AAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKR 267
Cdd:cd06534 161 evGAALLSHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAGQICTAASR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 268 IIVLKSIEEELVNKIIehidafkmgdpldpktklgplarsdlrenlhiqvekslkqgaklllggiipegkgfyyppTLIT 347
Cdd:cd06534 241 LLVHESIYDEFVEKLV------------------------------------------------------------TVLV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 348 QVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAThEIEAGACFVNA-LVASDPRLPF 426
Cdd:cd06534 261 DVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAE-RLRAGTVYINDsSIGVGPEAPF 339
|
410 420
....*....|....*....|....*...
gi 498339450 427 GGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd06534 340 GGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
2-452 |
8.14e-104 |
|
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: 317.23 E-value: 8.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 2 KIQTVNPATEQIIQNYDCLNEQHVNERL---NKAHETYLaWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPIT 78
Cdd:cd07091 20 TFPTINPATEEVICQVAEADEEDVDAAVkaaRAAFETGW-WRKMDPRERGRLLNKLADLIERDRDELAALESLDNGKPLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 79 AG-KAEINKCVWLCEHYAEHAEEYLApKLIQTEMKK-AKVCHVSLGIVFAIMPWNFPF-WQVFRFAvPTIMAGNAAVLKH 155
Cdd:cd07091 99 ESaKGDVALSIKCLRYYAGWADKIQG-KTIPIDGNFlAYTRREPIGVCGQIIPWNFPLlMLAWKLA-PALAAGNTVVLKP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 156 APVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKF-LKKSVLELGG 231
Cdd:cd07091 177 AEQTPLSALYLAELIKEAGFPPGVVN--IVPGFGPtagAAISSHMDVDKIAFTGSTAVGRTIMEAAAKSnLKKVTLELGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 232 SDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRE 311
Cdd:cd07091 255 KSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYDEFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 312 NLHIQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAV 391
Cdd:cd07091 335 KILSYIESGKKEGATLLTGGERHGSKGYFIQPTVFTDVKDDMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGV 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498339450 392 FTRDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07091 415 FTKDINKALRVS-RALKAGTVWVNTYNVFDAAVPFGGFKQSGFGRELGEEGLEEYTQVKAV 474
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
3-454 |
8.26e-104 |
|
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: 317.21 E-value: 8.26e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLA--WKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPIT-A 79
Cdd:cd07139 16 IDVVSPATEEVVGRVPEATPADVDAAVAAARRAFDNgpWPRLSPAERAAVLRRLADALEARADELARLWTAENGMPISwS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 80 GKAEINKCVWLCEHYAEHAEEYLAPKLIQT-EMKKAKVCHVSLGIVFAIMPWNFPFWQ-VFRFAvPTIMAGNAAVLKHAP 157
Cdd:cd07139 96 RRAQGPGPAALLRYYAALARDFPFEERRPGsGGGHVLVRREPVGVVAAIVPWNAPLFLaALKIA-PALAAGCTVVLKPSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 158 VSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLV 237
Cdd:cd07139 175 ETPLDAYLLAEAAEEAGLPPGVVNVVPADREVGEYLVRHPGVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 238 LEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQV 317
Cdd:cd07139 255 LDDADLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDEVVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 318 EKSLKQGAKLLLGGIIPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRD 395
Cdd:cd07139 335 AKGRAEGARLVTGGGRPAGldRGWFVEPTLFADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTAD 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 498339450 396 LEKGEHIATHeIEAGACFVNALvASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07139 415 VERGLAVARR-IRTGTVGVNGF-RLDFGAPFGGFKQSGIGREGGPEGLDAYLETKSIYL 471
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
2-454 |
1.27e-103 |
|
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: 317.04 E-value: 1.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 2 KIQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKI-TSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPI-TA 79
Cdd:cd07144 24 TIKTVNPSTGEVIASVYAAGEEDVDKAVKAARKAFESWWSkVTGEERGELLDKLADLVEKNRDLLAAIEALDSGKPYhSN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 80 GKAEINKCVWLCEHYAEHAEEyLAPKLIQTEMKK-AKVCHVSLGIVFAIMPWNFPF----WQVFrfavPTIMAGNAAVLK 154
Cdd:cd07144 104 ALGDLDEIIAVIRYYAGWADK-IQGKTIPTSPNKlAYTLHEPYGVCGQIIPWNYPLamaaWKLA----PALAAGNTVVIK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 155 HAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGG 231
Cdd:cd07144 179 PAENTPLSLLYFANLVKEAGFPPGVVN--IIPGYGAvagSALAEHPDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 232 SDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHI-DAFKMGDPLDPKTKLGPLARSDLR 310
Cdd:cd07144 257 KSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQESIYDKFVEKFVEHVkQNYKVGSPFDDDTVVGPQVSKTQY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKSLKQGAKLLLGGI---IPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGL 387
Cdd:cd07144 337 DRVLSYIEKGKKEGAKLVYGGEkapEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGL 416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498339450 388 GAAVFTRDLEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07144 417 AAAVFTKDIRRA-HRVARELEAGMVWINSSNDSDVGVPFGGFKMSGIGRELGEYGLETYTQTKAVHI 482
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
5-454 |
5.12e-103 |
|
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: 314.50 E-value: 5.12e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPIT-AGKAE 83
Cdd:cd07093 1 NFNPATGEVLAKVPEGGAAEVDAAVAAAKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKPITlARTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 84 INKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVLKHAPVS 159
Cdd:cd07093 81 IPRAAANFRFFADYILQLDGESYPQDGGALNYVLRQPVGVAGLITPWNLPLmlltWKI----APALAFGNTVVLKPSEWT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 160 SGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYL 236
Cdd:cd07093 157 PLTAWLLAELANEAGLPPGVVN--VVHGFGPeagAALVAHPDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 237 VLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQ 316
Cdd:cd07093 235 VFADADLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPLDPDTEVGPLISKEHLEKVLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 317 VEKSLKQGAKLLLGGIIPE----GKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVF 392
Cdd:cd07093 315 VELARAEGATILTGGGRPElpdlEGGYFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVW 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498339450 393 TRDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07093 395 TRDLGRAHRVA-RRLEAGTVWVNCWLVRDLRTPFGGVKASGIGREGGDYSLEFYTELKNVCI 455
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
3-456 |
1.87e-101 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 312.01 E-value: 1.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:PLN02278 42 FPVYNPATGEVIANVPCMGRAETNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAEHAEEyLAPKLIQTEMKKAK--VCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSS 160
Cdd:PLN02278 122 EVAYGASFLEYFAEEAKR-VYGDIIPSPFPDRRllVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 161 GTGNKIEELFLEAGFPEHLFQHLIVDND--GAAkIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVL 238
Cdd:PLN02278 201 LTALAAAELALQAGIPPGVLNVVMGDAPeiGDA-LLASPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 239 EDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVE 318
Cdd:PLN02278 280 DDADLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLVVGDGFEEGVTQGPLINEAAVQKVESHVQ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 319 KSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEK 398
Cdd:PLN02278 360 DAVSKGAKVLLGGKRHSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQR 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 399 GEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAVSD 456
Cdd:PLN02278 440 AWRVS-EALEYGIVGVNEGLISTEVAPFGGVKQSGLGREGSKYGIDEYLEIKYVCLGN 496
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
5-455 |
1.05e-100 |
|
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: 308.60 E-value: 1.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGK-AE 83
Cdd:cd07115 1 TLNPATGELIARVAQASAEDVDAAVAAARAAFEAWSAMDPAERGRILWRLAELILANADELARLESLDTGKPIRAARrLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 84 INKCVWLCEHYAEHAEEYL-------APKLIQTEMKkakvchvSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHA 156
Cdd:cd07115 81 VPRAADTFRYYAGWADKIEgevipvrGPFLNYTVRE-------PVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSD 233
Cdd:cd07115 154 ELTPLSALRIAELMAEAGFPAGVLN--VVTGFGEvagAALVEHPDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 234 PYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENL 313
Cdd:cd07115 232 ANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGDPLDPKTQMGPLVSQAQFDRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 314 HIQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFT 393
Cdd:cd07115 312 LDYVDVGREEGARLLTGGKRPGARGFFVEPTIFAAVPPEMRIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWT 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498339450 394 RDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAVS 455
Cdd:cd07115 392 RDLGRAHRVA-AALKAGTVWINTYNRFDPGSPFGGYKQSGFGREMGREALDEYTEVKSVWVN 452
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
6-454 |
3.65e-100 |
|
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: 307.25 E-value: 3.65e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKI-TSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAgkAEI 84
Cdd:cd07089 2 INPATEEVIGTAPDAGAADVDAAIAAARRAFDTGDWsTDAEERARCLRQLHEALEARKEELRALLVAEVGAPVMT--ARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEH---YAEHAEEY-----LAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHA 156
Cdd:cd07089 80 MQVDGPIGHlryFADLADSFpwefdLPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQhlIV---DNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSD 233
Cdd:cd07089 160 PDTPLSALLLGEIIAETDLPAGVVN--VVtgsDNAVGEALTTDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 234 PYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENL 313
Cdd:cd07089 238 ANIVLDDADLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTVMGPLISAAQRDRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 314 HIQVEKSLKQGAKLLLGGIIPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAV 391
Cdd:cd07089 318 EGYIARGRDEGARLVTGGGRPAGldKGFYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGV 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498339450 392 FTRDLEKGEHIATHeIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07089 398 WSADVDRAYRVARR-IRTGSVGINGGGGYGPDAPFGGYKQSGLGRENGIEGLEEFLETKSIAY 459
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
5-454 |
2.18e-98 |
|
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: 302.69 E-value: 2.18e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:cd07090 1 VIEPATGEVLATVHCAGAEDVDLAVKSAKAAQKEWSATSGMERGRILRKAADLLRERNDEIARLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPF----WQvfrfAVPTIMAGNAAVLKHAPVSS 160
Cdd:cd07090 81 DSSADCLEYYAGLAPTLSGEHVPLPGGSFAYTRREPLGVCAGIGAWNYPIqiasWK----SAPALACGNAMVYKPSPFTP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 161 GTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLED 240
Cdd:cd07090 157 LTALLLAEILTEAGLPDGVFNVVQGGGETGQLLCEHPDVAKVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 241 ADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKS 320
Cdd:cd07090 237 ADLENAVNGAMMANFLSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKIRIGDPLDEDTQMGALISEEHLEKVLGYIESA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 321 LKQGAKLLLGG--IIPEGK---GFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRD 395
Cdd:cd07090 317 KQEGAKVLCGGerVVPEDGlenGFYVSPCVLTDCTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 498339450 396 LEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07090 397 LQRA-HRVIAQLQAGTCWINTYNISPVEVPFGGYKQSGFGRENGTAALEHYTQLKTVYV 454
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-452 |
2.19e-97 |
|
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: 300.71 E-value: 2.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPA-TEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:cd07097 19 RNPSdTSDVVGKYARASAEDADAAIAAAAAAFPAWRRTSPEARADILDKAGDELEARKEELARLLTREEGKTLPEARGEV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAEEyLAPKLIQTEMKKA--KVCHVSLGIVFAIMPWNFPF----WQvfrfAVPTIMAGNAAVLKHAPV 158
Cdd:cd07097 99 TRAGQIFRYYAGEALR-LSGETLPSTRPGVevETTREPLGVVGLITPWNFPIaipaWK----IAPALAYGNTVVFKPAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 159 SSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPY 235
Cdd:cd07097 174 TPASAWALVEILEEAGLPAGVFN--LVMGSGSevgQALVEHPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 236 LVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLA-RSDLRENLH 314
Cdd:cd07097 252 VVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHDRFVEALVERTKALKVGDALDEGVDIGPVVsERQLEKDLR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 315 iQVEKSLKQGAKLLLGG-IIPEG-KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVF 392
Cdd:cd07097 332 -YIEIARSEGAKLVYGGeRLKRPdEGYYLAPALFAGVTNDMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIV 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498339450 393 TRDLEKGEHIATHeIEAGACFVNALVAS-DPRLPFGGIKESGYG-RELSREGILEFVNTKTV 452
Cdd:cd07097 411 TTSLKHATHFKRR-VEAGVVMVNLPTAGvDYHVPFGGRKGSSYGpREQGEAALEFYTTIKTV 471
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
7-452 |
1.03e-96 |
|
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: 298.36 E-value: 1.03e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 7 NPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINK 86
Cdd:cd07149 5 SPYDGEVIGRVPVASEEDVEKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKPIKDARKEVDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 87 CVwlcEHYAEHAEE--YLAPKLIQT------EMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPV 158
Cdd:cd07149 85 AI---ETLRLSAEEakRLAGETIPFdaspggEGRIGFTIREPIGVVAAITPFNFPLNLVAHKVGPAIAAGNAVVLKPASQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 159 SSGTGNKIEELFLEAGFPEHLFQhlIVDNDG---AAKIIENPHVIAVTLTGSGRAGSAVASHAGkfLKKSVLELGGSDPY 235
Cdd:cd07149 162 TPLSALKLAELLLEAGLPKGALN--VVTGSGetvGDALVTDPRVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 236 LVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHI 315
Cdd:cd07149 238 IVDADADLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDTDVGPMISEAEAERIEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 316 QVEKSLKQGAKLLLGGIIpegKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRD 395
Cdd:cd07149 318 WVEEAVEGGARLLTGGKR---DGAILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTND 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 396 LEKGeHIATHEIEAGACFVNAlvASDPR---LPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07149 395 LQKA-LKAARELEVGGVMIND--SSTFRvdhMPYGGVKESGTGREGPRYAIEEMTEIKLV 451
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
4-452 |
4.83e-94 |
|
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: 292.33 E-value: 4.83e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 4 QTVNPA-TEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07131 17 DSRNPAdLEEVVGTFPLSTASDVDAAVEAAREAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAEGRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEhYAEHAEEYLAPKLIQTEM--KKAKVCHVSLGIVFAIMPWNFPF----WQVFrfavPTIMAGNAAVLKHA 156
Cdd:cd07131 97 DVQEAIDMAQ-YAAGEGRRLFGETVPSELpnKDAMTRRQPIGVVALITPWNFPVaipsWKIF----PALVCGNTVVFKPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQ--HLIVDNDGAAkIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDP 234
Cdd:cd07131 172 EDTPACALKLVELFAEAGLPPGVVNvvHGRGEEVGEA-LVEHPDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 235 YLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLH 314
Cdd:cd07131 251 IIVMDDADLDLALEGALWSAFGTTGQRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 315 IQVEKSLKQGAKLLLGGIIPEG----KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:cd07131 331 NYNEIGKEEGATLLLGGERLTGggyeKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSA 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498339450 391 VFTRDLEKGEHiATHEIEAGACFVNA-LVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07131 411 IYTEDVNKAFR-ARRDLEAGITYVNApTIGAEVHLPFGGVKKSGNGHREAGTTALDAFTEWKA 472
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
5-452 |
6.96e-94 |
|
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: 291.91 E-value: 6.96e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLA--WKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07119 17 IINPANGEVIATVPEGTAEDAKRAIAAARRAFDSgeWPHLPAQERAALLFRIADKIREDAEELARLETLNTGKTLRESEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYA-----EHAEEYLAPkliqtEMKKAKVCHVSLGIVFAIMPWNFPFWQ-VFRFAvPTIMAGNAAVLKHA 156
Cdd:cd07119 97 DIDDVANCFRYYAglatkETGEVYDVP-----PHVISRTVREPVGVCGLITPWNYPLLQaAWKLA-PALAAGNTVVIKPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSD 233
Cdd:cd07119 171 EVTPLTTIALFELIEEAGLPAGVVN--LVTGSGAtvgAELAESPDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 234 PYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENL 313
Cdd:cd07119 249 PNIVFADADFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 314 HIQVEKSLKQGAKLLLGGIIPEG----KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGA 389
Cdd:cd07119 329 LSYIQLGKEEGARLVCGGKRPTGdelaKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498339450 390 AVFTRDLEKGEHIAThEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07119 409 AVWTKDIARANRVAR-RLRAGTVWINDYHPYFAEAPWGGYKQSGIGRELGPTGLEEYQETKHI 470
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
38-435 |
1.14e-93 |
|
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: 289.96 E-value: 1.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 38 AWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVC 117
Cdd:cd07152 28 AWAATPPRERAAVLRRAADLLEEHADEIADWIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQGEILPSAPGRLSLAR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 118 HVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLK---HAPVSSGTgnKIEELFLEAGFPEHLFQHLIVDNDGAAKII 194
Cdd:cd07152 108 RVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKpdpRTPVSGGV--VIARLFEEAGLPAGVLHVLPGGADAGEALV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 195 ENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSI 274
Cdd:cd07152 186 EDPNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHESV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 275 EEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGiipEGKGFYYPPTLITQVKPGMP 354
Cdd:cd07152 266 ADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHAIVDDSVAAGARLEAGG---TYDGLFYRPTVLSGVKPGMP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 355 AFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAtHEIEAGACFVN-ALVASDPRLPFGGIKESG 433
Cdd:cd07152 343 AFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALA-DRLRTGMLHINdQTVNDEPHNPFGGMGASG 421
|
..
gi 498339450 434 YG 435
Cdd:cd07152 422 NG 423
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
6-454 |
2.97e-93 |
|
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: 289.52 E-value: 2.97e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLA-WKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:cd07109 2 FDPSTGEVFARIARGGAADVDRAVQAARRAFESgWLRLSPAERGRLLLRIARLIREHADELARLESLDTGKPLTQARADV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAEEY------LAPKLIQTemkkakVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPV 158
Cdd:cd07109 82 EAAARYFEYYGGAADKLhgetipLGPGYFVY------TVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAED 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 159 SSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPY 235
Cdd:cd07109 156 APLTALRLAELAEEAGLPAGALN--VVTGLGAeagAALVAHPGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 236 LVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPL-DPktKLGPLARSDLRENLH 314
Cdd:cd07109 234 IVFADADLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLeDP--DLGPLISAKQLDRVE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 315 IQVEKSLKQGAKLLLGGIIPEG---KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAV 391
Cdd:cd07109 312 GFVARARARGARIVAGGRIAEGapaGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGV 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498339450 392 FTRDLEKGEHIAtHEIEAGACFVNAL-VASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07109 392 WTRDGDRALRVA-RRLRAGQVFVNNYgAGGGIELPFGGVKKSGHGREKGLEALYNYTQTKTVAV 454
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
3-454 |
3.14e-93 |
|
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: 289.59 E-value: 3.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07151 12 IDVLNPYTGETLAEIPAASKEDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQILEERRDEIVEWLIRESGSTRIKANI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCE---HYAEHAEEYLAPKLIqtEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHA--- 156
Cdd:cd07151 92 EWGAAMAITReaaTFPLRMEGRILPSDV--PGKENRVYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPAsdt 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTgnKIEELFLEAGFPEHLFQhlIVDNDGAA---KIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSD 233
Cdd:cd07151 170 PITGGL--LLAKIFEEAGLPKGVLN--VVVGAGSEigdAFVEHPVPRLISFTGSTPVGRHIGELAGRHLKKVALELGGNN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 234 PYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENL 313
Cdd:cd07151 246 PFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRIIVHEDVYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 314 HIQVEKSLKQGAKLLLGGiipEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFT 393
Cdd:cd07151 326 LDKIEQAVEEGATLLVGG---EAEGNVLEPTVLSDVTNDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFT 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498339450 394 RDLEKGEHIAtHEIEAGACFVNALVASD-PRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07151 403 SDLERGVQFA-RRIDAGMTHINDQPVNDePHVPFGGEKNSGLGRFNGEWALEEFTTDKWISV 463
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
3-454 |
3.46e-93 |
|
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: 289.86 E-value: 3.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKIT-SFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGK 81
Cdd:cd07082 18 IEVYSPIDGEVIGSVPALSALEILEAAETAYDAGRGWWPTmPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 82 AEINKCVWLCEHYAEHAEEYLAPKLI--QTEMKKAKVCHVS---LGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKha 156
Cdd:cd07082 98 KEVDRTIDYIRDTIEELKRLDGDSLPgdWFPGTKGKIAQVRrepLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFK-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSG--TGNKIEELFLEAGFPEHLFQhlIVDNDG---AAKIIENPHVIAVTLTGSGRAGSAVASHAGKflKKSVLELGG 231
Cdd:cd07082 176 PATQGvlLGIPLAEAFHDAGFPKGVVN--VVTGRGreiGDPLVTHGRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 232 SDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPL---ARSD 308
Cdd:cd07082 252 KDPAIVLPDADLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGVDITPLidpKSAD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 309 LRENLhiqVEKSLKQGAKLLLGGIIpEGKGFYYpPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLG 388
Cdd:cd07082 332 FVEGL---IDDAVAKGATVLNGGGR-EGGNLIY-PTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQ 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498339450 389 AAVFTRDLEKGEHIAtHEIEAGACFVNALVASDP-RLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07082 407 ASIFTKDINKARKLA-DALEVGTVNINSKCQRGPdHFPFLGRKDSGIGTQGIGDALRSMTRRKGIVI 472
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
6-454 |
4.84e-93 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 289.20 E-value: 4.84e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKP-ITAGKAEI 84
Cdd:cd07098 1 YDPATGQHLGSVPADTPEDVDEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTmVDASLGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 ----NKCVWLcehyAEHAEEYLAPKLIQTEM----KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLK-- 154
Cdd:cd07098 81 lvtcEKIRWT----LKHGEKALRPESRPGGLlmfyKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKvs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 155 -HAPVSSGT-GNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGS 232
Cdd:cd07098 157 eQVAWSSGFfLSIIRECLAACGHDPDLVQLVTCLPETAEALTSHPVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 233 DPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLREN 312
Cdd:cd07098 237 DPAIVLDDADLDQIASIIMRGTFQSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPLDGDVDVGAMISPARFDR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 313 LHIQVEKSLKQGAKLLLGGI----IPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLG 388
Cdd:cd07098 317 LEELVADAVEKGARLLAGGKryphPEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLG 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 389 AAVFTRDLEKGEHIAtHEIEAGACFVNALVAS--DPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07098 397 ASVFGKDIKRARRIA-SQLETGMVAINDFGVNyyVQQLPFGGVKGSGFGRFAGEEGLRGLCNPKSVTE 463
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
3-454 |
9.28e-93 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 288.10 E-value: 9.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNErlnkAHETYLAWK-ITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGK 81
Cdd:cd07146 1 LEVRNPYTGEVVGTVPAGTEEALRE----ALALAASYRsTLTRYQRSAILNKAAALLEARREEFARLITLESGLCLKDTR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 82 AEINKCVWLCEHYAEHAE----EYLAPKLIQT-EMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHA 156
Cdd:cd07146 77 YEVGRAADVLRFAAAEALrddgESFSCDLTANgKARKIFTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQHLIVD-NDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGkfLKKSVLELGGSDPY 235
Cdd:cd07146 157 EKTPLSAIYLADLLYEAGLPPDMLSVVTGEpGEIGDELITHPDVDLVTFTGGVAVGKAIAATAG--YKRQLLELGGNDPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 236 LVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHI 315
Cdd:cd07146 235 IVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDPATDMGTVIDEEAAIQIEN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 316 QVEKSLKQGAKLLLGGiipEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRD 395
Cdd:cd07146 315 RVEEAIAQGARVLLGN---QRQGALYAPTVLDHVPPDAELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTND 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498339450 396 LEKGEHIAThEIEAGACFVNALVASD-PRLPFGGIKESGYG-RELSREGILEFVNTKTVAV 454
Cdd:cd07146 392 LDTIKRLVE-RLDVGTVNVNEVPGFRsELSPFGGVKDSGLGgKEGVREAMKEMTNVKTYSL 451
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
2-453 |
2.02e-92 |
|
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: 289.12 E-value: 2.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 2 KIQTVNPA-TEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAG 80
Cdd:cd07124 47 KIESRNPAdPSEVLGTVQKATKEEAEAAVQAARAAFPTWRRTPPEERARLLLRAAALLRRRRFELAAWMVLEVGKNWAEA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 KAEINKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPFwqvfrfAVPTIM------AGNAAVLK 154
Cdd:cd07124 127 DADVAEAIDFLEYYAREMLRLRGFPVEMVPGEDNRYVYRPLGVGAVISPWNFPL------AILAGMttaalvTGNTVVLK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 155 HAPVSSGTGNKIEELFLEAGFPEHLFQHLIVDND--GAAkIIENPHVIAVTLTGSGRAG------SAVASHAGKFLKKSV 226
Cdd:cd07124 201 PAEDTPVIAAKLVEILEEAGLPPGVVNFLPGPGEevGDY-LVEHPDVRFIAFTGSREVGlriyerAAKVQPGQKWLKRVI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 227 LELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLAR 306
Cdd:cd07124 280 AEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVID 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 307 SDLRENLHIQVEKsLKQGAKLLLGGIIPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSR 384
Cdd:cd07124 360 KGARDRIRRYIEI-GKSEGRLLLGGEVLELaaEGYFVQPTIFADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTE 438
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 385 YGLGAAVFTRDLEKGEHiATHEIEAGACFVN-----ALVAsdpRLPFGGIKESGYGrelSREG----ILEFVNTKTVA 453
Cdd:cd07124 439 YGLTGGVFSRSPEHLER-ARREFEVGNLYANrkitgALVG---RQPFGGFKMSGTG---SKAGgpdyLLQFMQPKTVT 509
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
3-454 |
2.45e-91 |
|
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: 285.23 E-value: 2.45e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07086 15 FTSRNPANGEPIARVFPASPEDVEAAVAAAREAFKEWRKVPAPRRGEIVRQIGEALRKKKEALGRLVSLEMGKILPEGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEhYAEHAEEYLAPKLIQTEM--KKAKVCHVSLGIVFAIMPWNFPF----WQvfrfAVPTIMAGNAAVLKHA 156
Cdd:cd07086 95 EVQEMIDICD-YAVGLSRMLYGLTIPSERpgHRLMEQWNPLGVVGVITAFNFPVavpgWN----AAIALVCGNTVVWKPS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEA----GFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGS 232
Cdd:cd07086 170 ETTPLTAIAVTKILAEVleknGLPPGVVNLVTGGGDGGELLVHDPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 233 DPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLREN 312
Cdd:cd07086 250 NAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 313 LHIQVEKSLKQGAKLLLGGIIPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:cd07086 330 YLNAIEIAKSQGGTVLTGGKRIDGgePGNYVEPTIVTGVTDDARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSS 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 391 VFTRDLEKGEH-IATHEIEAGACFVN-----ALVAsdprLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07086 410 IFTEDLREAFRwLGPKGSDCGIVNVNiptsgAEIG----GAFGGEKETGGGRESGSDAWKQYMRRSTCTI 475
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
38-454 |
5.47e-91 |
|
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: 283.43 E-value: 5.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 38 AWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEYLAPKLIQTEM---KKA 114
Cdd:cd07101 33 AWAARPFAERAAVFLRFHDLVLERRDELLDLIQLETGKARRHAFEEVLDVAIVARYYARRAERLLKPRRRRGAIpvlTRT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 115 KVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---A 191
Cdd:cd07101 113 TVNRRPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAGLPRDLWQ--VVTGPGSevgG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 192 KIIEnpHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVL 271
Cdd:cd07101 191 AIVD--NADYVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVH 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 272 KSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGII-PEGKGFYYPPTLITQVK 350
Cdd:cd07101 269 ESVYDEFVRRFVARTRALRLGAALDYGPDMGSLISQAQLDRVTAHVDDAVAKGATVLAGGRArPDLGPYFYEPTVLTGVT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 351 PGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIATHeIEAGACFVN-ALVASDPRL--PFG 427
Cdd:cd07101 349 EDMELFAEETFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAAR-LRAGTVNVNeGYAAAWASIdaPMG 427
|
410 420
....*....|....*....|....*..
gi 498339450 428 GIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07101 428 GMKDSGLGRRHGAEGLLKYTETQTVAV 454
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
6-454 |
7.14e-90 |
|
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: 280.37 E-value: 7.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA-EI 84
Cdd:cd07092 2 VDPATGEEIATVPDASAADVDAAVAAAHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDdEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAE--------EYLA--PKLIQTEmkkakvchvSLGIVFAIMPWNFPFWQ-VFRFAvPTIMAGNAAVL 153
Cdd:cd07092 82 PGAVDNFRFFAGAARtlegpaagEYLPghTSMIRRE---------PIGVVAQIAPWNYPLMMaAWKIA-PALAAGNTVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 154 KHAPVSSGTGNKIEELfLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELG 230
Cdd:cd07092 152 KPSETTPLTTLLLAEL-AAEVLPPGVVN--VVCGGGAsagDALVAHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 231 GSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLR 310
Cdd:cd07092 229 GKAPVIVFDDADLDAAVAGIATAGYYNAGQDCTAACRVYVHESVYDEFVAALVEAVSAIRVGDPDDEDTEMGPLNSAAQR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKsLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:cd07092 309 ERVAGFVER-APAHARVLTGGRRAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASS 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498339450 391 VFTRDLEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07092 388 VWTRDVGRA-MRLSARLDFGTVWVNTHIPLAAEMPHGGFKQSGYGKDLSIYALEDYTRIKHVMV 450
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
3-452 |
9.98e-90 |
|
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: 280.09 E-value: 9.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07094 1 LDVHNPYDGEVIGKVPADDRADAEEALATARAGAENRRALPPHERMAILERAADLLKKRAEEFAKIIACEGGKPIKDARV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAEHAEEY---LAPKLIQT--EMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAP 157
Cdd:cd07094 81 EVDRAIDTLRLAAEEAERIrgeEIPLDATQgsDNRLAWTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 158 VSSGTGNKIEELFLEAGFPEHLFQHLIVDN-DGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKflKKSVLELGGSDPYL 236
Cdd:cd07094 161 KTPLSALELAKILVEAGVPEGVLQVVTGEReVLGDAFAADERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 237 VLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQ 316
Cdd:cd07094 239 VDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDVGPLISEEAAERVERW 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 317 VEKSLKQGAKLLLGGiipEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDL 396
Cdd:cd07094 319 VEEAVEAGARLLCGG---ERDGALFKPTVLEDVPRDTKLSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 498339450 397 EKGEHIATHeIEAGACFVNALVASD-PRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07094 396 NVAFKAAEK-LEVGGVMVNDSSAFRtDWMPFGGVKESGVGREGVPYAMEEMTEEKTV 451
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
21-437 |
1.41e-87 |
|
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: 274.51 E-value: 1.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 21 NEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAE- 99
Cdd:cd07147 19 GPDDIEEAIAAAVKAFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLEAGKPIKDARGEVARAIDTFRIAAEEATr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 100 ---EYLAPKLI-QTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGF 175
Cdd:cd07147 99 iygEVLPLDISaRGEGRQGLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 176 PEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKflKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRL 255
Cdd:cd07147 179 PKGAFSVLPCSRDDADLLVTDERIKLLSFTGSPAVGWDLKARAGK--KKVVLELGGNAAVIVDSDADLDFAAQRIIFGAF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 256 NNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGiipE 335
Cdd:cd07147 257 YQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPKDDATDVGPMISESEAERVEGWVNEAVDAGAKLLTGG---K 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 336 GKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHiATHEIEAGACFVN 415
Cdd:cd07147 334 RDGALLEPTILEDVPPDMEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDLEKALR-AWDELEVGGVVIN 412
|
410 420
....*....|....*....|....
gi 498339450 416 AL--VASDPrLPFGGIKESGYGRE 437
Cdd:cd07147 413 DVptFRVDH-MPYGGVKDSGIGRE 435
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
5-452 |
1.44e-87 |
|
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: 274.61 E-value: 1.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:cd07110 1 VINPATEATIGEIPAATAEDVDAAVRAARRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAE--EYLAPKLIQTEMK--KAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVLKHA 156
Cdd:cd07110 81 DDVAGCFEYYADLAEqlDAKAERAVPLPSEdfKARVRREPVGVVGLITPWNFPLlmaaWKV----APALAAGCTVVLKPS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSD 233
Cdd:cd07110 157 ELTSLTELELAEIAAEAGLPPGVLN--VVTGTGDeagAPLAAHPGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 234 PYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENL 313
Cdd:cd07110 235 PIIVFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGVRLGPLVSQAQYEKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 314 HIQVEKSLKQGAKLLLGGIIPE--GKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAV 391
Cdd:cd07110 315 LSFIARGKEEGARLLCGGRRPAhlEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAV 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498339450 392 FTRDLEKGEHIATHeIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07110 395 ISRDAERCDRVAEA-LEAGIVWINCSQPCFPQAPWGGYKRSGIGRELGEWGLDNYLEVKQI 454
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
2-454 |
3.25e-87 |
|
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: 274.70 E-value: 3.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 2 KIQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYL-AWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAG 80
Cdd:cd07113 16 RLDITNPATEQVIASVASATEADVDAAVASAWRAFVsAWAKTTPAERGRILLRLADLIEQHGEELAQLETLCSGKSIHLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 KA-EINKCVWLCEHYAEHAE----EYLAPKL--IQTEMKKAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGN 149
Cdd:cd07113 96 RAfEVGQSANFLRYFAGWATkingETLAPSIpsMQGERYTAFTRREPVGVVAGIVPWNFSVmiavWKI----GAALATGC 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 150 AAVLKHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDG--AAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVL 227
Cdd:cd07113 172 TIVIKPSEFTPLTLLRVAELAKEAGIPDGVLN--VVNGKGavGAQLISHPDVAKVSFTGSVATGKKIGRQAASDLTRVTL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 228 ELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLA-R 306
Cdd:cd07113 250 ELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQALSSFQVGSPMDESVMFGPLAnQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 307 SDLRENLHIqVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYG 386
Cdd:cd07113 330 PHFDKVCSY-LDDARAEGDEIVRGGEALAGEGYFVQPTLVLARSADSRLMREETFGPVVSFVPYEDEEELIQLINDTPFG 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 387 LGAAVFTRDLEKGEHIAThEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07113 409 LTASVWTNNLSKALRYIP-RIEAGTVWVNMHTFLDPAVPFGGMKQSGIGREFGSAFIDDYTELKSVMI 475
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
31-455 |
9.92e-87 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 274.83 E-value: 9.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 31 KAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEYLAPKLIQTE 110
Cdd:PRK09407 62 RARAAQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLETGKARRHAFEEVLDVALTARYYARRAPKLLAPRRRAGA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 111 ---MKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDN 187
Cdd:PRK09407 142 lpvLTKTTELRQPKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELLYEAGLPRDLWQ--VVTG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 188 DGA---AKIIEnpHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIA 264
Cdd:PRK09407 220 PGPvvgTALVD--NADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCIS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 265 AKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGII-PEGKGFYYPP 343
Cdd:PRK09407 298 IERIYVHESIYDEFVRAFVAAVRAMRLGAGYDYSADMGSLISEAQLETVSAHVDDAVAKGATVLAGGKArPDLGPLFYEP 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 344 TLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIATHeIEAGACFVN-------A 416
Cdd:PRK09407 378 TVLTGVTPDMELAREETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAAR-IRAGTVNVNegyaaawG 456
|
410 420 430
....*....|....*....|....*....|....*....
gi 498339450 417 LVASdprlPFGGIKESGYGRELSREGILEFVNTKTVAVS 455
Cdd:PRK09407 457 SVDA----PMGGMKDSGLGRRHGAEGLLKYTESQTIATQ 491
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
6-452 |
7.77e-86 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 271.01 E-value: 7.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAE-- 83
Cdd:PRK13473 22 YNPATGEVLAEIAEASAAQVDAAVAAADAAFPEWSQTTPKERAEALLKLADAIEENADEFARLESLNCGKPLHLALNDei 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 84 --INKCVWLCEHYAEHAE-----EYLAPkliqtemkkakvcHVS------LGIVFAIMPWNFPF----WQVfrfaVPTIM 146
Cdd:PRK13473 102 paIVDVFRFFAGAARCLEgkaagEYLEG-------------HTSmirrdpVGVVASIAPWNYPLmmaaWKL----APALA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 147 AGNAAVLKHAPVSSGTGNKIEELFLEAgFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLK 223
Cdd:PRK13473 165 AGNTVVLKPSEITPLTALKLAELAADI-LPPGVLN--VVTGRGAtvgDALVGHPKVRMVSLTGSIATGKHVLSAAADSVK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 224 KSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGP 303
Cdd:PRK13473 242 RTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 304 LARSDLRENLHIQVEKSLKQG-AKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQ 382
Cdd:PRK13473 322 LISAAHRDRVAGFVERAKALGhIRVVTGGEAPDGKGYYYEPTLLAGARQDDEIVQREVFGPVVSVTPFDDEDQAVRWAND 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498339450 383 SRYGLGAAVFTRDLEKGeHIATHEIEAGACFVNA---LVAsdpRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:PRK13473 402 SDYGLASSVWTRDVGRA-HRVSARLQYGCTWVNThfmLVS---EMPHGGQKQSGYGKDMSLYGLEDYTVVRHV 470
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
5-454 |
9.64e-85 |
|
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: 267.30 E-value: 9.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPI-TAGKAE 83
Cdd:cd07108 1 VINPATGQVIGEVPRSRAADVDRAVAAAKAAFPEWAATPARERGKLLARIADALEARSEELARLLALETGNALrTQARPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 84 INKCVWLCEHYAEHAEEY------LAPKLIQTEMKkakvchVSLGIVFAIMPWNFP-FWQVFRFAvPTIMAGNAAVLKHA 156
Cdd:cd07108 81 AAVLADLFRYFGGLAGELkgetlpFGPDVLTYTVR------EPLGVVGAILPWNAPlMLAALKIA-PALVAGNTVVLKAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELfLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSD 233
Cdd:cd07108 154 EDAPLAVLLLAEI-LAQVLPAGVLN--VITGYGEecgAALVDHPDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 234 PYLVLEDADLDLAAQCIVNS-RLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLarsdLREN 312
Cdd:cd07108 231 PMIVFPDADLDDAVDGAIAGmRFTRQGQSCTAGSRLFVHEDIYDAFLEKLVAKLSKLKIGDPLDEATDIGAI----ISEK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 313 LHIQVEKSLK-----QGAKLLLGGIIPE----GKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQS 383
Cdd:cd07108 307 QFAKVCGYIDlglstSGATVLRGGPLPGegplADGFFVQPTIFSGVDNEWRLAREEIFGPVLCAIPWKDEDEVIAMANDS 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498339450 384 RYGLGAAVFTRDLEKGEHiATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILE-FVNTKTVAV 454
Cdd:cd07108 387 HYGLAAYVWTRDLGRALR-AAHALEAGWVQVNQGGGQQPGQSYGGFKQSGLGREASLEGMLEhFTQKKTVNI 457
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
3-454 |
1.22e-84 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 268.29 E-value: 1.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPIT-AGK 81
Cdd:PRK13252 24 FEVINPATGEVLATVQAATPADVEAAVASAKQGQKIWAAMTAMERSRILRRAVDILRERNDELAALETLDTGKPIQeTSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 82 AEINKCVWLCEHYAEhaeeyLAPKL--IQTEMKKAKVCH---VSLGIVFAIMPWNFPF----WQvfrfAVPTIMAGNAAV 152
Cdd:PRK13252 104 VDIVTGADVLEYYAG-----LAPALegEQIPLRGGSFVYtrrEPLGVCAGIGAWNYPIqiacWK----SAPALAAGNAMI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 153 LKHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA--AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELG 230
Cdd:PRK13252 175 FKPSEVTPLTALKLAEIYTEAGLPDGVFN--VVQGDGRvgAWLTEHPDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 231 GSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLR 310
Cdd:PRK13252 253 GKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQKSIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKSLKQGAKLLLGGI-IPEG---KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYG 386
Cdd:PRK13252 333 DKVLGYIEKGKAEGARLLCGGErLTEGgfaNGAFVAPTVFTDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYG 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 387 LGAAVFTRDLEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:PRK13252 413 LAAGVFTADLSRA-HRVIHQLEAGICWINTWGESPAEMPVGGYKQSGIGRENGIATLEHYTQIKSVQV 479
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
3-454 |
1.78e-83 |
|
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: 265.16 E-value: 1.78e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAH---ETYLAWKITSFnQRKTLMLQLAELLKSKIDELAHLMAIEMGKPI-T 78
Cdd:cd07143 24 VKVYNPSTGKLITKIAEATEADVDIAVEVAHaafETDWGLKVSGS-KRGRCLSKLADLMERNLDYLASIEALDNGKTFgT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 79 AGKAEINKCVWLCEHYAEHAEEYLApKLIQTEMKK-AKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVL 153
Cdd:cd07143 103 AKRVDVQASADTFRYYGGWADKIHG-QVIETDIKKlTYTRHEPIGVCGQIIPWNFPLlmcaWKI----APALAAGNTIVL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 154 KHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDG---AAKIIENPHVIAVTLTGSGRAGSAVASHAGKF-LKKSVLEL 229
Cdd:cd07143 178 KPSELTPLSALYMTKLIPEAGFPPGVIN--VVSGYGrtcGNAISSHMDIDKVAFTGSTLVGRKVMEAAAKSnLKKVTLEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 230 GGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDL 309
Cdd:cd07143 256 GGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 310 RENLHIQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGA 389
Cdd:cd07143 336 YERIMSYIESGKAEGATVETGGKRHGNEGYFIEPTIFTDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAA 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498339450 390 AVFTRDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07143 416 AVFTNNINNAIRVA-NALKAGTVWVNCYNLLHHQVPFGGYKQSGIGRELGEYALENYTQIKAVHI 479
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
5-455 |
1.64e-82 |
|
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: 262.28 E-value: 1.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERL---NKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPI-TAG 80
Cdd:cd07141 26 TINPATGEKICEVQEGDKADVDKAVkaaRAAFKLGSPWRTMDASERGRLLNKLADLIERDRAYLASLETLDNGKPFsKSY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 KAEINKCVWLCEHYAEHAEEYLApKLIQTEMKK-AKVCHVSLGIVFAIMPWNFPF-WQVFRFAvPTIMAGNAAVLKHAPV 158
Cdd:cd07141 106 LVDLPGAIKVLRYYAGWADKIHG-KTIPMDGDFfTYTRHEPVGVCGQIIPWNFPLlMAAWKLA-PALACGNTVVLKPAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 159 SSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKF-LKKSVLELGGSDP 234
Cdd:cd07141 184 TPLTALYLASLIKEAGFPPGVVN--VVPGYGPtagAAISSHPDIDKVAFTGSTEVGKLIQQAAGKSnLKRVTLELGGKSP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 235 YLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLH 314
Cdd:cd07141 262 NIVFADADLDYAVEQAHEALFFNMGQCCCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKIL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 315 IQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTR 394
Cdd:cd07141 342 ELIESGKKEGAKLECGGKRHGDKGYFIQPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTK 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498339450 395 DLEKGEHIATHeIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAVS 455
Cdd:cd07141 422 DIDKAITFSNA-LRAGTVWVNCYNVVSPQAPFGGYKMSGNGRELGEYGLQEYTEVKTVTIK 481
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
5-454 |
2.97e-82 |
|
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: 261.16 E-value: 2.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:cd07107 1 VINPATGQVLARVPAASAADVDRAVAAARAAFPEWRATTPLERARMLRELATRLREHAEELALIDALDCGNPVSAMLGDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAeeylapkliqTEMKKAKV------CHVSL----GIVFAIMPWNFPF-WQVFRFAVPtIMAGNAAVL 153
Cdd:cd07107 81 MVAAALLDYFAGLV----------TELKGETIpvggrnLHYTLrepyGVVARIVAFNHPLmFAAAKIAAP-LAAGNTVVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 154 K---HAPVSSgtgNKIEELFLEAgFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVL 227
Cdd:cd07107 150 KppeQAPLSA---LRLAELAREV-LPPGVFN--ILPGDGAtagAALVRHPDVKRIALIGSVPTGRAIMRAAAEGIKHVTL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 228 ELGGSDPYLVLEDADLDLAAQCIVNS-RLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLAR 306
Cdd:cd07107 224 ELGGKNALIVFPDADPEAAADAAVAGmNFTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPATTMGPLVS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 307 SDLRENLHIQVEKSLKQGAKLLLGGIIPEG----KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQ 382
Cdd:cd07107 304 RQQYDRVMHYIDSAKREGARLVTGGGRPEGpaleGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANG 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498339450 383 SRYGLGAAVFTRDLEKGEHIAThEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07107 384 VEYGLTAAIWTNDISQAHRTAR-RVEAGYVWINGSSRHFLGAPFGGVKNSGIGREECLEELLSYTQEKNVNV 454
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
2-456 |
3.46e-82 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 262.36 E-value: 3.46e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 2 KIQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLA-----WKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKP 76
Cdd:PLN02467 24 RIPVVNPATEETIGDIPAATAEDVDAAVEAARKAFKRnkgkdWARTTGAVRAKYLRAIAAKITERKSELAKLETLDCGKP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 77 ITAGKAEINKCVWLCEHYAEHAEE-----YLAPKLIQTEMKkakvCHV---SLGIVFAIMPWNFPF----WQVfrfaVPT 144
Cdd:PLN02467 104 LDEAAWDMDDVAGCFEYYADLAEAldakqKAPVSLPMETFK----GYVlkePLGVVGLITPWNYPLlmatWKV----APA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 145 IMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEHLFQHLI-VDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLK 223
Cdd:PLN02467 176 LAAGCTAVLKPSELASVTCLELADICREVGLPPGVLNVVTgLGTEAGAPLASHPGVDKIAFTGSTATGRKIMTAAAQMVK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 224 KSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGP 303
Cdd:PLN02467 256 PVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 304 LARSDLRENLHIQVEKSLKQGAKLLLGGIIPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYAN 381
Cdd:PLN02467 336 VVSEGQYEKVLKFISTAKSEGATILCGGKRPEHlkKGFFIEPTIITDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELAN 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 382 QSRYGLGAAVFTRDLEKGEHIaTHEIEAGACFVNalvASDP---RLPFGGIKESGYGRELSREGILEFVNTKTVA--VSD 456
Cdd:PLN02467 416 DSHYGLAGAVISNDLERCERV-SEAFQAGIVWIN---CSQPcfcQAPWGGIKRSGFGRELGEWGLENYLSVKQVTkyISD 491
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
51-452 |
1.68e-81 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 257.74 E-value: 1.68e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 51 MLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEYLApKLIQTEMKKAK--VCHVSLGIVFAIM 128
Cdd:PRK10090 1 LRKIAAGIRERASEISALIVEEGGKIQQLAEVEVAFTADYIDYMAEWARRYEG-EIIQSDRPGENilLFKRALGVTTGIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 129 PWNFPFWQVFRFAVPTIMAGNAAVLKhaPVSSGTGNKIE--ELFLEAGFPEHLFQhlIVDNDGAA---KIIENPHVIAVT 203
Cdd:PRK10090 80 PWNFPFFLIARKMAPALLTGNTIVIK--PSEFTPNNAIAfaKIVDEIGLPKGVFN--LVLGRGETvgqELAGNPKVAMVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 204 LTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKII 283
Cdd:PRK10090 156 MTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 284 EHIDAFKMGDPLD-PKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFG 362
Cdd:PRK10090 236 EAMQAVQFGNPAErNDIAMGPLINAAALERVEQKVARAVEEGARVALGGKAVEGKGYYYPPTLLLDVRQEMSIMHEETFG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 363 PVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHiATHEIEAGACFVNalvasdpRLPF-------GGIKESGYG 435
Cdd:PRK10090 316 PVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVAMK-AIKGLKFGETYIN-------RENFeamqgfhAGWRKSGIG 387
|
410
....*....|....*..
gi 498339450 436 RELSREGILEFVNTKTV 452
Cdd:PRK10090 388 GADGKHGLHEYLQTQVV 404
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
5-454 |
1.86e-81 |
|
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: 258.81 E-value: 1.86e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETY--LAWKiTSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07120 1 SIDPATGEVIGTYADGGVAEAEAAIAAARRAFdeTDWA-HDPRLRARVLLELADAFEANAERLARLLALENGKILGEARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAE-------HAEEyLAPKLIQTEMKKAkvchvsLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKH 155
Cdd:cd07120 80 EISGAISELRYYAGlarteagRMIE-PEPGSFSLVLREP------MGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 156 APVSSGTGNKIEELFLEA-GFPEHLFqHLIVDN--DGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGS 232
Cdd:cd07120 153 AGQTAQINAAIIRILAEIpSLPAGVV-NLFTESgsEGAAHLVASPDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 233 DPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLREN 312
Cdd:cd07120 232 TPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVGPGLDPASDMGPLIDRANVDR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 313 LHIQVEKSLKQGAKLLL-GGIIPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGA 389
Cdd:cd07120 312 VDRMVERAIAAGAEVVLrGGPVTEGlaKGAFLRPTLLEVDDPDADIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498339450 390 AVFTRDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07120 392 SVWTRDLARAMRVA-RAIRAGTVWINDWNKLFAEAEEGGYRQSGLGRLHGVAALEDFIEYKHIYL 455
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
6-452 |
3.08e-81 |
|
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: 258.99 E-value: 3.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEIN 85
Cdd:cd07085 21 YNPATGEVIARVPLATAEEVDAAVAAAKAAFPAWSATPVLKRQQVMFKFRQLLEENLDELARLITLEHGKTLADARGDVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 86 KCVWLCEHYAEHAEEYLAPKL------IQTEMKKakvchVSLGIVFAIMPWNFP----FWqvfrFAVPTIMAGNAAVLKH 155
Cdd:cd07085 101 RGLEVVEFACSIPHLLKGEYLenvargIDTYSYR-----QPLGVVAGITPFNFPamipLW----MFPMAIACGNTFVLKP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 156 APVSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKsVLELGGS-DP 234
Cdd:cd07085 172 SERVPGAAMRLAELLQEAGLPDGVLNVVHGGKEAVNALLDHPDIKAVSFVGSTPVGEYIYERAAANGKR-VQALGGAkNH 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 235 YLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLH 314
Cdd:cd07085 251 AVVMPDADLEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 315 IQVEKSLKQGAKLLLGG--IIPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:cd07085 331 GLIESGVEEGAKLVLDGrgVKVPGyeNGNFVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANPYGNGAA 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498339450 391 VFTRDLEKGEHIAtHEIEAGACFVNALVASdPR--LPFGGIKESGYGrELS---REGILEFVNTKTV 452
Cdd:cd07085 411 IFTRSGAAARKFQ-REVDAGMVGINVPIPV-PLafFSFGGWKGSFFG-DLHfygKDGVRFYTQTKTV 474
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
5-447 |
2.63e-80 |
|
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: 256.55 E-value: 2.63e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGK-AE 83
Cdd:cd07111 41 TINPATGEVLASVLQAEEEDVDAAVAAARTAFESWSALPGHVRARHLYRIARHIQKHQRLFAVLESLDNGKPIRESRdCD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 84 INKCVWLCEHYAEHAEeylapkLIQTEMKKAKvchvSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVLKHAPVS 159
Cdd:cd07111 121 IPLVARHFYHHAGWAQ------LLDTELAGWK----PVGVVGQIVPWNFPLlmlaWKI----CPALAMGNTVVLKPAEYT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 160 SGTGNKIEELFLEAGFPEHLFQhlIVDNDGA--AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLV 237
Cdd:cd07111 187 PLTALLFAEICAEAGLPPGVLN--IVTGNGSfgSALANHPGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 238 LEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQV 317
Cdd:cd07111 265 FDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIRKLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 318 EKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLE 397
Cdd:cd07111 345 EEGRAEGADVFQPGADLPSKGPFYPPTLFTNVPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLS 424
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 498339450 398 KGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFV 447
Cdd:cd07111 425 LALEVA-LSLKAGVVWINGHNLFDAAAGFGGYRESGFGREGGKEGLYEYL 473
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
5-452 |
9.74e-79 |
|
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: 252.41 E-value: 9.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYL--AW-KITSFnQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGK 81
Cdd:cd07142 23 TIDPRNGEVIAHVAEGDAEDVDRAVKAARKAFDegPWpRMTGY-ERSRILLRFADLLEKHADELAALETWDNGKPYEQAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 82 -AEINKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVLKHA 156
Cdd:cd07142 102 yAEVPLAARLFRYYAGWADKIHGMTLPADGPHHVYTLHEPIGVVGQIIPWNFPLlmfaWKV----GPALACGNTIVLKPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKF-LKKSVLELGGS 232
Cdd:cd07142 178 EQTPLSALLAAKLAAEAGLPDGVLN--IVTGFGPtagAAIASHMDVDKVAFTGSTEVGKIIMQLAAKSnLKPVTLELGGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 233 DPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLREN 312
Cdd:cd07142 256 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHESIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 313 LHIQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVF 392
Cdd:cd07142 336 ILSYIEHGKEEGATLITGGDRIGSKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVF 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 393 TRDLEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07142 416 SKNIDTA-NTLSRALKAGTVWVNCYDVFDASIPFGGYKMSGIGREKGIYALNNYLQVKAV 474
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
2-453 |
8.31e-78 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 251.01 E-value: 8.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 2 KIQTVNPA-TEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAG 80
Cdd:PRK03137 51 KIVSINPAnKSEVVGRVSKATKELAEKAMQAALEAFETWKKWSPEDRARILLRAAAIIRRRKHEFSAWLVKEAGKPWAEA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 KAEINKCVWLCEHYAEHAEEYLAPK-LIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVS 159
Cdd:PRK03137 131 DADTAEAIDFLEYYARQMLKLADGKpVESRPGEHNRYFYIPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 160 SGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGK------FLKKSVLELG 230
Cdd:PRK03137 211 PVIAAKFVEVLEEAGLPAGVVN--FVPGSGSevgDYLVDHPKTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 231 GSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPkTKLGPLARSDLR 310
Cdd:PRK03137 289 GKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNPEDN-AYMGPVINQASF 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKSlKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:PRK03137 368 DKIMSYIEIG-KEEGRLVLGGEGDDSKGYFIQPTIFADVDPKARIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGA 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498339450 391 VFTRDLEKGEhIATHEIEAGACFVN-----ALVASDprlPFGGIKESGYGrelSREG----ILEFVNTKTVA 453
Cdd:PRK03137 447 VISNNREHLE-KARREFHVGNLYFNrgctgAIVGYH---PFGGFNMSGTD---SKAGgpdyLLLFLQAKTVS 511
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
4-454 |
1.11e-77 |
|
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: 250.10 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 4 QTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLA--WKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPIT-AG 80
Cdd:cd07140 24 NTINPTDGSVICKVSLATVEDVDRAVAAAKEAFENgeWGKMNARDRGRLMYRLADLMEEHQEELATIESLDSGAVYTlAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 KAEINKCVWLCEHYAEHAEEylapklIQTE---MKKAKVCHV-------SLGIVFAIMPWNFPFWQVFRFAVPTIMAGNA 150
Cdd:cd07140 104 KTHVGMSIQTFRYFAGWCDK------IQGKtipINQARPNRNltltkrePIGVCGIVIPWNYPLMMLAWKMAACLAAGNT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 151 AVLKHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAV-ASHAGKFLKKSV 226
Cdd:cd07140 178 VVLKPAQVTPLTALKFAELTVKAGFPKGVIN--ILPGSGSlvgQRLSDHPDVRKLGFTGSTPIGKHImKSCAVSNLKKVS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 227 LELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLAR 306
Cdd:cd07140 256 LELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPQNH 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 307 SDLRENLHIQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEE-EGI-KYANQSR 384
Cdd:cd07140 336 KAHLDKLVEYCERGVKEGATLVYGGKQVDRPGFFFEPTVFTDVEDHMFIAKEESFGPIMIISKFDDGDvDGVlQRANDTE 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 385 YGLGAAVFTRDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAV 454
Cdd:cd07140 416 YGLASGVFTKDINKALYVS-DKLEAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEEALNEYLKTKTVTI 484
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
4-455 |
2.73e-74 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 241.34 E-value: 2.73e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 4 QTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLA--WKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAG- 80
Cdd:PRK09847 38 ETVDPVTQAPLAKIARGKSVDIDRAVSAARGVFERgdWSLSSPAKRKAVLNKLADLMEAHAEELALLETLDTGKPIRHSl 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 KAEINKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPF----WQVFrfavPTIMAGNAAVLKHA 156
Cdd:PRK09847 118 RDDIPGAARAIRWYAEAIDKVYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLlltcWKLG----PALAAGNSVILKPS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHL------FQHlivdnDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSV-LEL 229
Cdd:PRK09847 194 EKSPLSAIRLAGLAKEAGLPDGVlnvvtgFGH-----EAGQALSRHNDIDAIAFTGSTRTGKQLLKDAGDSNMKRVwLEA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 230 GGSDPYLVLEDA-DLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSD 308
Cdd:PRK09847 269 GGKSANIVFADCpDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDPATTMGTLIDCA 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 309 LRENLHIQVEKSLKQGAKLLLGGiiPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLG 388
Cdd:PRK09847 349 HADSVHSFIREGESKGQLLLDGR--NAGLAAAIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLG 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498339450 389 AAVFTRDLEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAVS 455
Cdd:PRK09847 427 AAVWTRDLSRA-HRMSRRLKAGSVFVNNYNDGDMTVPFGGYKQSGNGRDKSLHALEKFTELKTIWIS 492
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
4-452 |
3.72e-74 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 241.26 E-value: 3.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 4 QTVNPATEQIIQNYDCLNEQHVNERLNKAHETYL--AWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGK 81
Cdd:PLN02766 39 ETRDPRTGEVIARIAEGDKEDVDLAVKAAREAFDhgPWPRMSGFERGRIMMKFADLIEEHIEELAALDTIDAGKLFALGK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 82 A-EINKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSS 160
Cdd:PLN02766 119 AvDIPAAAGLLRYYAGAADKIHGETLKMSRQLQGYTLKEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 161 GTGNKIEELFLEAGFPEHLFQhlIVDNDG---AAKIIENPHVIAVTLTGSGRAGSAVASHAGKF-LKKSVLELGGSDPYL 236
Cdd:PLN02766 199 LSALFYAHLAKLAGVPDGVIN--VVTGFGptaGAAIASHMDVDKVSFTGSTEVGRKIMQAAATSnLKQVSLELGGKSPLL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 237 VLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQ 316
Cdd:PLN02766 277 IFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSY 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 317 VEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDL 396
Cdd:PLN02766 357 IEHGKREGATLLTGGKPCGDKGYYIEPTIFTDVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDL 436
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 498339450 397 EKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:PLN02766 437 DVANTVS-RSIRAGTIWVNCYFAFDPDCPFGGYKMSGFGRDQGMDALDKYLQVKSV 491
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
3-455 |
1.69e-72 |
|
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: 236.47 E-value: 1.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPI--TAG 80
Cdd:cd07559 18 FDNYNPVNGKVLCEIPRSTAEDVDLAVDAAHEAFKTWGKTSVAERANILNKIADRIEENLELLAVAETLDNGKPIreTLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 kAEINKCVwlcEHY-----AEHAEEYLAPKLIQTEMkkAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAA 151
Cdd:cd07559 98 -ADIPLAI---DHFryfagVIRAQEGSLSEIDEDTL--SYHFHEPLGVVGQIIPWNFPLlmaaWKL----APALAAGNTV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 152 VLKhaPvSSGTGNKIEELFleagfpeHLFQHL-------IVDNDGAAK---IIENPHVIAVTLTGSGRAGSAVASHAGKF 221
Cdd:cd07559 168 VLK--P-ASQTPLSILVLM-------ELIGDLlpkgvvnVVTGFGSEAgkpLASHPRIAKLAFTGSTTVGRLIMQYAAEN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 222 LKKSVLELGGSDPYLVLEDA-----DLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLD 296
Cdd:cd07559 238 LIPVTLELGGKSPNIFFDDAmdaddDFDDKAEEGQLGFAFNQGEVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 297 PKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGIIPEG----KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDN 372
Cdd:cd07559 318 PETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLggldKGYFYEPTLIKGGNNDMRIFQEEIFGPVLAVITFKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 373 EEEGIKYANQSRYGLGAAVFTRDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRElSREGILE-FVNTKT 451
Cdd:cd07559 398 EEEAIAIANDTEYGLGGGVWTRDINRALRVA-RGIQTGRVWVNCYHQYPAHAPFGGYKKSGIGRE-THKMMLDhYQQTKN 475
|
....
gi 498339450 452 VAVS 455
Cdd:cd07559 476 ILVS 479
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
3-455 |
1.66e-69 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 228.64 E-value: 1.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:PRK11241 28 IDVTNPANGDKLGSVPKMGADETRAAIDAANRALPAWRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEAKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAEHAEEYLAPKLI--QTEmKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSS 160
Cdd:PRK11241 108 EISYAASFIEWFAEEGKRIYGDTIPghQAD-KRLIVIKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 161 GTGNKIEELFLEAGFPEHLFQhLIVDNDGA--AKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVL 238
Cdd:PRK11241 187 FSALALAELAIRAGIPAGVFN-VVTGSAGAvgGELTSNPLVRKLSFTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 239 EDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVE 318
Cdd:PRK11241 266 DDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 319 KSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEK 398
Cdd:PRK11241 346 DALEKGARVVCGGKAHELGGNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSR 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 498339450 399 GEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAVS 455
Cdd:PRK11241 426 VFRVG-EALEYGIVGINTGIISNEVAPFGGIKASGLGREGSKYGIEDYLEIKYMCIG 481
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
3-445 |
8.51e-68 |
|
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: 223.87 E-value: 8.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07117 18 IDSYNPANGETLSEITDATDADVDRAVKAAQEAFKTWRKTTVAERANILNKIADIIDENKELLAMVETLDNGKPIRETRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 -EINKCVWLCEHYAE--HAEEYLAPKLIQTEMkkAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVLKh 155
Cdd:cd07117 98 vDIPLAADHFRYFAGviRAEEGSANMIDEDTL--SIVLREPIGVVGQIIPWNFPFlmaaWKL----APALAAGNTVVIK- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 156 aPvSSGTGNKIEELFleagfpeHLFQHL-------IVDNDGAAK---IIENPHVIAVTLTGSGRAGSAVASHAGKFLKKS 225
Cdd:cd07117 171 -P-SSTTSLSLLELA-------KIIQDVlpkgvvnIVTGKGSKSgeyLLNHPGLDKLAFTGSTEVGRDVAIAAAKKLIPA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 226 VLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLA 305
Cdd:cd07117 242 TLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVCCAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 306 RSDLRENLHIQVEKSLKQGAKLLLGGI-IPEG---KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYAN 381
Cdd:cd07117 322 NKDQLDKILSYVDIAKEEGAKILTGGHrLTENgldKGFFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMAN 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498339450 382 QSRYGLGAAVFTRDLEKGEHIAtHEIEAGACFVNALVASDPRLPFGGIKESGYGRElSREGILE 445
Cdd:cd07117 402 DSEYGLGGGVFTKDINRALRVA-RAVETGRVWVNTYNQIPAGAPFGGYKKSGIGRE-THKSMLD 463
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
24-436 |
2.19e-65 |
|
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: 216.37 E-value: 2.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 24 HVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAE----INKCVWLCEHYAEhae 99
Cdd:cd07095 1 QVDAAVAAARAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQTEvaamAGKIDISIKAYHE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 100 eYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEHL 179
Cdd:cd07095 78 -RTGERATPMAQGRAVLRHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWEEAGLPPGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 180 FQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASH-AGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNS 258
Cdd:cd07095 157 LNLVQGGRETGEALAAHEGIDGLLFTGSAATGLLLHRQfAGRPGKILALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 259 GQVCIAAKRIIVLKSIE-EELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKSLKQGAKLLLGGIIPEGK 337
Cdd:cd07095 237 GQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPFMGPLIIAAAAARYLLAQQDLLALGGEPLLAMERLVAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 338 GFYYPPTLItQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIATHeIEAGacFVNA- 416
Cdd:cd07095 317 TAFLSPGII-DVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLAR-IRAG--IVNWn 392
|
410 420
....*....|....*....|..
gi 498339450 417 --LVASDPRLPFGGIKESGYGR 436
Cdd:cd07095 393 rpTTGASSTAPFGGVGLSGNHR 414
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
27-452 |
3.30e-64 |
|
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: 213.16 E-value: 3.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 27 ERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKP-ITAGKAEINKCVWLCEHYAEHAEEYLAPK 105
Cdd:cd07087 2 ELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPpAEAYLTEIAVVLGEIDHALKHLKKWMKPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 106 LIQTEMK----KAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLK---HAPVSSgtgNKIEELFLEAgFPEH 178
Cdd:cd07087 82 RVSVPLLlqpaKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKpseLAPATS---ALLAKLIPKY-FDPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 179 LFQHLIVDNDGAAKIIENP--HVIavtLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLN 256
Cdd:cd07087 158 AVAVVEGGVEVATALLAEPfdHIF---FTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 257 NSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFkMGDPLDPKTKLGPLARSDlrenlHIQVEKSLKQGAKLLLGG-IIPE 335
Cdd:cd07087 235 NAGQTCIAPDYVLVHESIKDELIEELKKAIKEF-YGEDPKESPDYGRIINER-----HFDRLASLLDDGKVVIGGqVDKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 336 GKgfYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAtHEIEAGACFVN 415
Cdd:cd07087 309 ER--YIAPTILDDVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVL-AETSSGGVCVN 385
|
410 420 430
....*....|....*....|....*....|....*....
gi 498339450 416 ALV--ASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07087 386 DVLlhAAIPNLPFGGVGNSGMGAYHGKAGFDTFSHLKSV 424
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
6-455 |
7.23e-64 |
|
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: 214.75 E-value: 7.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPA-TEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:cd07125 51 IDPAdHERTIGEVSLADAEDVDAALAIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGKTLADADAEV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAEEYLA-PKLIQ-TEMKKAKVCHvSLGIVFAIMPWNFPFwqvfrfAVPT------IMAGNAAVLKHA 156
Cdd:cd07125 131 REAIDFCRYYAAQARELFSdPELPGpTGELNGLELH-GRGVFVCISPWNFPL------AIFTgqiaaaLAAGNTVIAKPA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAK-IIENPHVIAVTLTGSGRAG----SAVASHAGKFLKKSVlELGG 231
Cdd:cd07125 204 EQTPLIAARAVELLHEAGVPRDVLQLVPGDGEEIGEaLVAHPRIDGVIFTGSTETAklinRALAERDGPILPLIA-ETGG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 232 SDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRE 311
Cdd:cd07125 283 KNAMIVDSTALPEQAVKDVVQSAFGSAGQRCSALRLLYLQEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLIDKPAGK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 312 NLHIQVEKSLKQgAKLLLGGIIPEGKGFYYPPTLITQVkpGMPAFDEELFGPVIAIITVDNE--EEGIKYANQSRYGLGA 389
Cdd:cd07125 363 LLRAHTELMRGE-AWLIAPAPLDDGNGYFVAPGIIEIV--GIFDLTTEVFGPILHVIRFKAEdlDEAIEDINATGYGLTL 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498339450 390 AVFTRDLEKGEHIAtHEIEAGACFVN-----ALVAsdpRLPFGGIKESGYGrelSREG----ILEFVNTKTVAVS 455
Cdd:cd07125 440 GIHSRDEREIEYWR-ERVEAGNLYINrnitgAIVG---RQPFGGWGLSGTG---PKAGgpnyLLRFGNEKTVSLN 507
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
3-437 |
1.51e-62 |
|
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: 210.14 E-value: 1.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:cd07130 14 VTSISPANGEPIARVRQATPEDYESTIKAAQEAFKEWRDVPAPKRGEIVRQIGDALRKKKEALGKLVSLEMGKILPEGLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEhYAEHAEEYLAPKLIQTEMKKakvcHV------SLGIVFAIMPWNFPF----WQVFRFAVptimAGNAAV 152
Cdd:cd07130 94 EVQEMIDICD-FAVGLSRQLYGLTIPSERPG----HRmmeqwnPLGVVGVITAFNFPVavwgWNAAIALV----CGNVVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 153 LKHAP----VSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLE 228
Cdd:cd07130 165 WKPSPttplTAIAVTKIVARVLEKNGLPGAIASLVCGGADVGEALVKDPRVPLVSFTGSTAVGRQVGQAVAARFGRSLLE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 229 LGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSD 308
Cdd:cd07130 245 LGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLHTKA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 309 LRENLHIQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITqVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLG 388
Cdd:cd07130 325 AVDNYLAAIEEAKSQGGTVLFGGKVIDGPGNYVEPTIVE-GLSDAPIVKEETFAPILYVLKFDTLEEAIAWNNEVPQGLS 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498339450 389 AAVFTRDLEKGEH---------------IATHEIEAGACfvnalvasdprlpFGGIKESGYGRE 437
Cdd:cd07130 404 SSIFTTDLRNAFRwlgpkgsdcgivnvnIGTSGAEIGGA-------------FGGEKETGGGRE 454
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
5-452 |
1.33e-61 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 209.28 E-value: 1.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 5 TVNPATEQIIQNYDCLNEQHVNERLNKAHETYL--AW-KITSFnQRKTLMLQLAELLKSKIDELAHLMAIEMGKPI-TAG 80
Cdd:PLN02466 77 TLDPRTGEVIAHVAEGDAEDVNRAVAAARKAFDegPWpKMTAY-ERSRILLRFADLLEKHNDELAALETWDNGKPYeQSA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 81 KAEINKCVWLCEHYAEHAEEYLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVLKHA 156
Cdd:PLN02466 156 KAELPMFARLFRYYAGWADKIHGLTVPADGPHHVQTLHEPIGVAGQIIPWNFPLlmfaWKV----GPALACGNTIVLKTA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGA---AKIIENPHVIAVTLTGSGRAGSAVASHAGKF-LKKSVLELGGS 232
Cdd:PLN02466 232 EQTPLSALYAAKLLHEAGLPPGVLN--VVSGFGPtagAALASHMDVDKLAFTGSTDTGKIVLELAAKSnLKPVTLELGGK 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 233 DPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLREN 312
Cdd:PLN02466 310 SPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 313 LHIQVEKSLKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVF 392
Cdd:PLN02466 390 ILRYIKSGVESGATLECGGDRFGSKGYYIQPTVFSNVQDDMLIAQDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVF 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 393 TRDLEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:PLN02466 470 TQNLDTA-NTLSRALRVGTVWVNCFDVFDAAIPFGGYKMSGIGREKGIYSLNNYLQVKAV 528
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
31-453 |
3.53e-61 |
|
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: 205.53 E-value: 3.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 31 KAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGK-AEINKCVWLCEHYAEHAEEYLAPKLIQT 109
Cdd:cd07135 13 RLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLlTEVSGVKNDILHMLKNLKKWAKDEKVKD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 110 -----EMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELfLEAGFPEHLFQhli 184
Cdd:cd07135 93 gplafMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAEL-VPKYLDPDAFQ--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 185 VDNDGAA---KIIENP--HVIavtLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSG 259
Cdd:cd07135 169 VVQGGVPettALLEQKfdKIF---YTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 260 QVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTklgpLARsdLRENLHIQVEKSL--KQGAKLLLGGIIPEGK 337
Cdd:cd07135 246 QICVAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASPD----YTR--IVNPRHFNRLKSLldTTKGKVVIGGEMDEAT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 338 GFyYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAThEIEAGACFVN-- 415
Cdd:cd07135 320 RF-IPPTIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILT-RTRSGGVVINdt 397
|
410 420 430
....*....|....*....|....*....|....*...
gi 498339450 416 ALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVA 453
Cdd:cd07135 398 LIHVGVDNAPFGGVGDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
6-453 |
2.50e-55 |
|
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: 191.64 E-value: 2.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNP-ATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:cd07083 37 VSPfAPSEVVGTTAKADKAEAEAALEAAWAAFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIDDV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAEEYL--APKLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGT 162
Cdd:cd07083 117 AEAIDFIRYYARAALRLRypAVEVVPYPGEDNESFYVGLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 163 GNKIEELFLEAGFPEHLFQHLivDNDGA---AKIIENPHVIAVTLTGSGRAG----SAVASHAGKF--LKKSVLELGGSD 233
Cdd:cd07083 197 GYKVFEIFHEAGFPPGVVQFL--PGVGEevgAYLTEHERIRGINFTGSLETGkkiyEAAARLAPGQtwFKRLYVETGGKN 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 234 PYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENL 313
Cdd:cd07083 275 AIIVDETADFELVVEGVVVSAFGFQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 314 HIQVEKSlKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEE--EGIKYANQSRYGLGAAV 391
Cdd:cd07083 355 LSYIEHG-KNEGQLVLGGKRLEGEGYFVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGV 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498339450 392 FTRdleKGEHI--ATHEIEAGACFVN-----ALVASDprlPFGGIKESGYGrelSREG----ILEFVNTKTVA 453
Cdd:cd07083 434 YSR---KREHLeeARREFHVGNLYINrkitgALVGVQ---PFGGFKLSGTN---AKTGgphyLRRFLEMKAVA 497
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
3-451 |
7.82e-55 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 190.35 E-value: 7.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:PLN00412 33 VAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAVT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAEHAEEYLAP-KLIQTEM----KKAKVCHVS---LGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLK 154
Cdd:PLN00412 113 EVVRSGDLISYTAEEGVRILGEgKFLVSDSfpgnERNKYCLTSkipLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 155 haPVSSG--TGNKIEELFLEAGFPEHLFQhlIVDNDGAA---KIIENPHVIAVTLTGsGRAGSAVASHAGKFLKKsvLEL 229
Cdd:PLN00412 193 --PPTQGavAALHMVHCFHLAGFPKGLIS--CVTGKGSEigdFLTMHPGVNCISFTG-GDTGIAISKKAGMVPLQ--MEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 230 GGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPK--TKLGPLARS 307
Cdd:PLN00412 266 GGKDACIVLEDADLDLAAANIIKGGFSYSGQRCTAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCdiTPVVSESSA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 308 DLRENLhiqVEKSLKQGAKLLL-----GGIIpegkgfyyPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQ 382
Cdd:PLN00412 346 NFIEGL---VMDAKEKGATFCQewkreGNLI--------WPLLLDNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNA 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 383 SRYGLGAAVFTRDLEKGEHIAtHEIEAGACFVNALVASDP-RLPFGGIKESGYGRELSREGILEFVNTKT 451
Cdd:PLN00412 415 SNFGLQGCVFTRDINKAILIS-DAMETGTVQINSAPARGPdHFPFQGLKDSGIGSQGITNSINMMTKVKS 483
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
21-455 |
4.04e-54 |
|
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: 188.04 E-value: 4.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 21 NEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPI-TAGKAEINKCVwlcEHYAEHAE 99
Cdd:cd07116 36 TAEDIELALDAAHAAKEAWGKTSVAERANILNKIADRMEANLEMLAVAETWDNGKPVrETLAADIPLAI---DHFRYFAG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 100 EYLAPKLIQTEMKKAKVC---HVSLGIVFAIMPWNFPF----WQVfrfaVPTIMAGNAAVLKHA---PVS---------- 159
Cdd:cd07116 113 CIRAQEGSISEIDENTVAyhfHEPLGVVGQIIPWNFPLlmatWKL----APALAAGNCVVLKPAeqtPASilvlmeligd 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 160 ---SGTGNKIEELFLEAGFPehlfqhlivdndgaakIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYL 236
Cdd:cd07116 189 llpPGVVNVVNGFGLEAGKP----------------LASSKRIAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPNI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 237 VLE------DADLDLAAQCIVNSRLNnSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLR 310
Cdd:cd07116 253 FFAdvmdadDAFFDKALEGFVMFALN-QGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKSLKQGAKLLLGG----IIPEGKGFYYPPTLItqvKPG--MPAFDEELFGPVIAIITVDNEEEGIKYANQSR 384
Cdd:cd07116 332 EKILSYIDIGKEEGAEVLTGGerneLGGLLGGGYYVPTTF---KGGnkMRIFQEEIFGPVLAVTTFKDEEEALEIANDTL 408
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498339450 385 YGLGAAVFTRDLEKGeHIATHEIEAGACFVNALVASDPRLPFGGIKESGYGRELSREGILEFVNTKTVAVS 455
Cdd:cd07116 409 YGLGAGVWTRDGNTA-YRMGRGIQAGRVWTNCYHLYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVS 478
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
3-441 |
1.16e-52 |
|
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: 183.39 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYL---AWkiTSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITA 79
Cdd:cd07148 1 LEVVNPFDLKPIGEVPTVDWAAIDKALDTAHALFLdrnNW--LPAHERIAILERLADLMEERADELALLIAREGGKPLVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 80 GKAE----INKCVWLCEHYAEHAEEYLAPKLIQT-EMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLK 154
Cdd:cd07148 79 AKVEvtraIDGVELAADELGQLGGREIPMGLTPAsAGRIAFTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 155 HAPVSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAG----SAVASHAgkflkKSVLELG 230
Cdd:cd07148 159 PALATPLSCLAFVDLLHEAGLPEGWCQAVPCENAVAEKLVTDPRVAFFSFIGSARVGwmlrSKLAPGT-----RCALEHG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 231 GSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLR 310
Cdd:cd07148 234 GAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIRPREV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKSLKQGAKLLLGGiIPEGKGFyYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:cd07148 314 DRVEEWVNEAVAAGARLLCGG-KRLSDTT-YAPTVLLDPPRDAKVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAA 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498339450 391 VFTRDLEKGEHiATHEIEAGACFVNALVA--SDpRLPFGGIKESGYG--------RELSRE 441
Cdd:cd07148 392 VFTKDLDVALK-AVRRLDATAVMVNDHTAfrVD-WMPFAGRRQSGYGtggipytmHDMTQE 450
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
37-452 |
4.06e-51 |
|
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: 178.57 E-value: 4.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 37 LAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKP-ITAGKAEINKCVWLCEHYAEHAEEYLAPKLIQTEM---- 111
Cdd:cd07134 12 LALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPaAEVDLTEILPVLSEINHAIKHLKKWMKPKRVRTPLllfg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 112 KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPEH--LFQHlivDNDG 189
Cdd:cd07134 92 TKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEvaVFEG---DAEV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 190 AAKIIENP--HVIavtLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKR 267
Cdd:cd07134 169 AQALLELPfdHIF---FTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCIAPDY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 268 IIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKlgPLAR----------SDLrenlhiqVEKSLKQGAKLLLGGIIPEGk 337
Cdd:cd07134 246 VFVHESVKDAFVEHLKAEIEKFYGKDAARKASP--DLARivndrhfdrlKGL-------LDDAVAKGAKVEFGGQFDAA- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 338 GFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAThEIEAGACFVNAL 417
Cdd:cd07134 316 QRYIAPTVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLA-RTSSGGVVVNDV 394
|
410 420 430
....*....|....*....|....*....|....*..
gi 498339450 418 VA--SDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07134 395 VLhfLNPNLPFGGVNNSGIGSYHGVYGFKAFSHERAV 431
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
3-437 |
2.32e-50 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 178.49 E-value: 2.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:PLN02315 36 VSSVNPANNQPIAEVVEASLEDYEEGLRACEEAAKIWMQVPAPKRGEIVRQIGDALRAKLDYLGRLVSLEMGKILAEGIG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEhYAEHAEEYLAPKLIQTEMKKAKVCHV--SLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAP--- 157
Cdd:PLN02315 116 EVQEIIDMCD-FAVGLSRQLNGSIIPSERPNHMMMEVwnPLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPttp 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 158 -VSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYL 236
Cdd:PLN02315 195 lITIAMTKLVAEVLEKNNLPGAIFTSFCGGAEIGEAIAKDTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAII 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 237 VLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQ 316
Cdd:PLN02315 275 VMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 317 VEKSLKQGAKLLLGGIIPEGKGFYYPPTlITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDL 396
Cdd:PLN02315 355 IEIIKSQGGKILTGGSAIESEGNFVQPT-IVEISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNP 433
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 498339450 397 EK-GEHIATHEIEAGACFVNALV-ASDPRLPFGGIKESGYGRE 437
Cdd:PLN02315 434 ETiFKWIGPLGSDCGIVNVNIPTnGAEIGGAFGGEKATGGGRE 476
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
3-452 |
2.94e-48 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 174.55 E-value: 2.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKA 82
Cdd:PLN02419 131 IDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 83 EINKCVWLCEHYAEHAE----EYLaPKLiqTEMKKAKVCHVSLGIVFAIMPWNFP-FWQVFRFAVpTIMAGNAAVLKHAP 157
Cdd:PLN02419 211 DIFRGLEVVEHACGMATlqmgEYL-PNV--SNGVDTYSIREPLGVCAGICPFNFPaMIPLWMFPV-AVTCGNTFILKPSE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 158 VSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLV 237
Cdd:PLN02419 287 KDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLV 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 238 LEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVL---KSIEEelvnKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLH 314
Cdd:PLN02419 367 LPDANIDATLNALLAAGFGAAGQRCMALSTVVFVgdaKSWED----KLVERAKALKVTCGSEPDADLGPVISKQAKERIC 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 315 IQVEKSLKQGAKLLLGG--IIPEG--KGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:PLN02419 443 RLIQSGVDDGAKLLLDGrdIVVPGyeKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAA 522
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498339450 391 VFTRDLEKGEHIAThEIEAGACFVNALVASD-PRLPFGGIKESGYG--RELSREGILEFVNTKTV 452
Cdd:PLN02419 523 IFTSSGAAARKFQM-DIEAGQIGINVPIPVPlPFFSFTGNKASFAGdlNFYGKAGVDFFTQIKLV 586
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
29-435 |
7.03e-48 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 171.37 E-value: 7.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 29 LNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGK-PITAGKAEINKCVWLCEHYAEHAEEYLAPKLI 107
Cdd:PTZ00381 13 VKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRhPFETKMTEVLLTVAEIEHLLKHLDEYLKPEKV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 108 QTEM----KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAgFPEHLFQHL 183
Cdd:PTZ00381 93 DTVGvfgpGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKY-LDPSYVRVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 184 IVDNDGAAKIIENP--HVIavtLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQV 261
Cdd:PTZ00381 172 EGGVEVTTELLKEPfdHIF---FTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 262 CIAAKRIIVLKSIEEELVNKIIEHIDAFkMGDplDPKTKlGPLARsdLRENLHIQVEKSL--KQGAKLLLGGIIPEGKGf 339
Cdd:PTZ00381 249 CVAPDYVLVHRSIKDKFIEALKEAIKEF-FGE--DPKKS-EDYSR--IVNEFHTKRLAELikDHGGKVVYGGEVDIENK- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 340 YYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIaTHEIEAGACFVNALV- 418
Cdd:PTZ00381 322 YVAPTIIVNPDLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELV-LENTSSGAVVINDCVf 400
|
410
....*....|....*...
gi 498339450 419 -ASDPRLPFGGIKESGYG 435
Cdd:PTZ00381 401 hLLNPNLPFGGVGNSGMG 418
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
3-433 |
3.77e-45 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 163.98 E-value: 3.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 3 IQTVNPATEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPI----T 78
Cdd:PRK09457 17 FESRNPVSGEVLWQGNDATAAQVDAAVRAARAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLweaaT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 79 AGKAEINKCVWLCEHYAEHAEEylapklIQTEMKKAKVC--HVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHA 156
Cdd:PRK09457 97 EVTAMINKIAISIQAYHERTGE------KRSEMADGAAVlrHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 157 PVSSGTGNKIEELFLEAGFPEHLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAV----ASHAGKFLkksVLELGGS 232
Cdd:PRK09457 171 ELTPWVAELTVKLWQQAGLPAGVLNLVQGGRETGKALAAHPDIDGLLFTGSANTGYLLhrqfAGQPEKIL---ALEMGGN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 233 DPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIE-EELVNKIIEHIDAFKMGDPL-DPKTKLGPLARSDLR 310
Cdd:PRK09457 248 NPLVIDEVADIDAAVHLIIQSAFISAGQRCTCARRLLVPQGAQgDAFLARLVAVAKRLTVGRWDaEPQPFMGAVISEQAA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 311 ENLHIQVEKSLKQGAKLLLGGIIPE-GKGFYYPPTL-ITQVKpGMPafDEELFGPVIAIITVDNEEEGIKYANQSRYGLG 388
Cdd:PRK09457 328 QGLVAAQAQLLALGGKSLLEMTQLQaGTGLLTPGIIdVTGVA-ELP--DEEYFGPLLQVVRYDDFDEAIRLANNTRFGLS 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 498339450 389 AAVFTRDLEKGEHIATHeIEAGacFVN---ALVASDPRLPFGGIKESG 433
Cdd:PRK09457 405 AGLLSDDREDYDQFLLE-IRAG--IVNwnkPLTGASSAAPFGGVGASG 449
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
26-452 |
2.42e-43 |
|
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: 158.03 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 26 NERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMG-KPITAGK-AEINKCVWLCEHYAEHAEEYLA 103
Cdd:cd07133 1 QALLERQKAAFLANPPPSLEERRDRLDRLKALLLDNQDALAEAISADFGhRSRHETLlAEILPSIAGIKHARKHLKKWMK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 104 PKLIQTEMK----KAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAgFPEHL 179
Cdd:cd07133 81 PSRRHVGLLflpaKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEY-FDEDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 180 FQHLIVDNDGAAKIIENP--HVIavtLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNN 257
Cdd:cd07133 160 VAVVTGGADVAAAFSSLPfdHLL---FTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 258 SGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFkMGDPLDPKtKLGPLARSDLRENLHIQVEKSLKQGAKL--LLGGIIPE 335
Cdd:cd07133 237 AGQTCVAPDYVLVPEDKLEEFVAAAKAAVAKM-YPTLADNP-DYTSIINERHYARLQGLLEDARAKGARVieLNPAGEDF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 336 GKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIATHEIEAGACFVN 415
Cdd:cd07133 315 AATRKLPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTIND 394
|
410 420 430
....*....|....*....|....*....|....*....
gi 498339450 416 AL--VASDpRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07133 395 TLlhVAQD-DLPFGGVGASGMGAYHGKEGFLTFSHAKPV 432
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
44-452 |
5.42e-41 |
|
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: 151.89 E-value: 5.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 44 FNQRKTL-------MLQ-LAELLKSKIDELAHlmaiemgkpitAGKAEINKC---VWLCE---------HYAEHAEEYLA 103
Cdd:cd07136 11 FKTGATKdvefrieQLKkLKQAIKKYENEILE-----------ALKKDLGKSefeAYMTEigfvlseinYAIKHLKKWMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 104 PKLIQTEM----KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAgFPEhl 179
Cdd:cd07136 80 PKRVKTPLlnfpSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEET-FDE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 180 fQHLIVDNDGAAkiiENPHVIA-----VTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSR 254
Cdd:cd07136 157 -EYVAVVEGGVE---ENQELLDqkfdyIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 255 LNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTkLGplarsdlrenlHIQVEK------SLKQGAKLL 328
Cdd:cd07136 233 FLNAGQTCVAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPD-YG-----------RIINEKhfdrlaGLLDNGKIV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 329 LGGIIPEgKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDlEKGEHIATHEIE 408
Cdd:cd07136 301 FGGNTDR-ETLYIEPTILDNVTWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSED-KKVEKKVLENLS 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 498339450 409 -AGACFVNALV-ASDPRLPFGGIKESGYGRELSREGILEFVNTKTV 452
Cdd:cd07136 379 fGGGCINDTIMhLANPYLPFGGVGNSGMGSYHGKYSFDTFSHKKSI 424
|
|
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
29-436 |
1.35e-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: 150.45 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 29 LNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKP-ITAGKAEINKCVWLCEHYAEHAEEYLAP--- 104
Cdd:cd07132 4 VRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPkFEAVLSEILLVKNEIKYAISNLPEWMKPepv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 105 -KLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFleagfPEHLfqhl 183
Cdd:cd07132 84 kKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELI-----PKYL---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 184 ivDNDGAAKIIENPHVIAVTL---------TGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSR 254
Cdd:cd07132 155 --DKECYPVVLGGVEETTELLkqrfdyifyTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 255 LNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPldpktKLGP-LARsdLRENLHIQVEKSLKQGAKLLLGGII 333
Cdd:cd07132 233 FINAGQTCIAPDYVLCTPEVQEKFVEALKKTLKEFYGEDP-----KESPdYGR--IINDRHFQRLKKLLSGGKVAIGGQT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 334 PEgKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDlEKGEHIATHEIEAGACF 413
Cdd:cd07132 306 DE-KERYIAPTVLTDVKPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNN-KKVINKILSNTSSGGVC 383
|
410 420
....*....|....*....|....*
gi 498339450 414 VNALV--ASDPRLPFGGIKESGYGR 436
Cdd:cd07132 384 VNDTImhYTLDSLPFGGVGNSGMGA 408
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
34-436 |
1.00e-39 |
|
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: 147.94 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 34 ETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPIT-AGKAEINKCVWLCEHYAEHAEEYLAPKLIQTEM- 111
Cdd:cd07137 10 ETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAeSFRDEVSVLVSSCKLAIKELKKWMAPEKVKTPLt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 112 ---KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNkieelFLEAGFPEHLfqhlivDND 188
Cdd:cd07137 90 tfpAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSA-----LLAKLIPEYL------DTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 189 gAAKIIE-NPHVIAVTL---------TGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLN-N 257
Cdd:cd07137 159 -AIKVIEgGVPETTALLeqkwdkiffTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWGcN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 258 SGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTklgpLARsdLRENLHIQVEKSL----KQGAKLLLGGII 333
Cdd:cd07137 238 NGQACIAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKD----LSR--IVNSHHFQRLSRLlddpSVADKIVHGGER 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 334 PEgKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGEHIAThEIEAGACF 413
Cdd:cd07137 312 DE-KNLYIEPTILLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVA-ETSSGGVT 389
|
410 420
....*....|....*....|....*
gi 498339450 414 VN--ALVASDPRLPFGGIKESGYGR 436
Cdd:cd07137 390 FNdtVVQYAIDTLPFGGVGESGFGA 414
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
6-435 |
2.71e-35 |
|
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: 136.96 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPATEQIIQNY-DCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:TIGR01238 56 TNPADRRDIVGQvFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMALCVREAGKTIHNAIAEV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAEEYLApkliqtemkkaKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGN 164
Cdd:TIGR01238 136 REAVDFCRYYAKQVRDVLG-----------EFSVESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSLIAY 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 165 KIEELFLEAGFPEHLFQHLI-VDNDGAAKIIENPHVIAVTLTGSgragSAVASHAGKFLKKS-------VLELGGSDPYL 236
Cdd:TIGR01238 205 RAVELMQEAGFPAGTIQLLPgRGADVGAALTSDPRIAGVAFTGS----TEVAQLINQTLAQRedapvplIAETGGQNAMI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 237 VLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENL--H 314
Cdd:TIGR01238 281 VDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAMQELKVGVPHLLTTDVGPVIDAEAKQNLlaH 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 315 IQVEKSL-KQGAKLLLGGIIPEGKGFYYPPTLITQvkPGMPAFDEELFGPVIAIITVDNEE--EGIKYANQSRYGLGAAV 391
Cdd:TIGR01238 361 IEHMSQTqKKIAQLTLDDSRACQHGTFVAPTLFEL--DDIAELSEEVFGPVLHVVRYKAREldQIVDQINQTGYGLTMGV 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 498339450 392 FTRDLEKGEHIATHeIEAGACFVN-----ALVASDprlPFGGIKESGYG 435
Cdd:TIGR01238 439 HSRIETTYRWIEKH-ARVGNCYVNrnqvgAVVGVQ---PFGGQGLSGTG 483
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
21-454 |
4.85e-31 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 126.85 E-value: 4.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 21 NEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEE 100
Cdd:PRK11904 583 DAEQVEQALAAARAAFPAWSRTPVEERAAILERAADLLEANRAELIALCVREAGKTLQDAIAEVREAVDFCRYYAAQARR 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 101 YLA-PKLIQ--TEMKKAKVCHvSLGIVFAIMPWNFP---FW-QVfrfaVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEA 173
Cdd:PRK11904 663 LFGaPEKLPgpTGESNELRLH-GRGVFVCISPWNFPlaiFLgQV----AAALAAGNTVIAKPAEQTPLIAAEAVKLLHEA 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 174 GFPEHLFQHLIvdNDGA---AKIIENPHVIAVTLTGS------------GRAGSAVASHAgkflkksvlELGGSDPYLVL 238
Cdd:PRK11904 738 GIPKDVLQLLP--GDGAtvgAALTADPRIAGVAFTGStetariinrtlaARDGPIVPLIA---------ETGGQNAMIVD 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 239 EDADLDLAAQCIVNSRLNNSGQVCiAAKRIIVLksiEEELVNKIIEHI----DAFKMGDPLDPKTKLGPLARSDLRENL- 313
Cdd:PRK11904 807 STALPEQVVDDVVTSAFRSAGQRC-SALRVLFV---QEDIADRVIEMLkgamAELKVGDPRLLSTDVGPVIDAEAKANLd 882
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 314 -HIQvekSLKQGAKLLLGGIIPEG--KGFYYPPTL-----ITQVKpgmpafdEELFGPVIAIITVDNEE-----EGIkya 380
Cdd:PRK11904 883 aHIE---RMKREARLLAQLPLPAGteNGHFVAPTAfeidsISQLE-------REVFGPILHVIRYKASDldkviDAI--- 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 381 NQSRYGLGAAVFTRDLEKGEHIATHeIEAGACFVN-----ALVASDprlPFGGIKESGYG------RELSRegileFVNT 449
Cdd:PRK11904 950 NATGYGLTLGIHSRIEETADRIADR-VRVGNVYVNrnqigAVVGVQ---PFGGQGLSGTGpkaggpHYLLR-----FATE 1020
|
....*
gi 498339450 450 KTVAV 454
Cdd:PRK11904 1021 KTVTV 1025
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
22-435 |
2.61e-29 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 121.51 E-value: 2.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 22 EQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEY 101
Cdd:PRK11905 589 AEDVERALAAAQAAFPEWSATPAAERAAILERAADLMEAHMPELFALAVREAGKTLANAIAEVREAVDFLRYYAAQARRL 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 102 LAPkliqtemkkakVCHVSLGIVFAIMPWNFP---FW-QVfrfaVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAGFPE 177
Cdd:PRK11905 669 LNG-----------PGHKPLGPVVCISPWNFPlaiFTgQI----AAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGVPK 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 178 HLFQHLIVDND--GAAkIIENPHVIAVTLTGSgragSAVAshagKFLKKSVLELGGSDPYLVLEDADLD--------LAA 247
Cdd:PRK11905 734 DALQLLPGDGRtvGAA-LVADPRIAGVMFTGS----TEVA----RLIQRTLAKRSGPPVPLIAETGGQNamivdssaLPE 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 248 QC---IVNSRLNNSGQVCiAAKRIIVL-KSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENL--HIQvekSL 321
Cdd:PRK11905 805 QVvadVIASAFDSAGQRC-SALRVLCLqEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIeaHIE---AM 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 322 KQGAKLLLGGIIPEG--KGFYYPPTLItQVKpGMPAFDEELFGPVIAIITVDNEE--EGIKYANQSRYGLGAAVFTRDLE 397
Cdd:PRK11905 881 RAAGRLVHQLPLPAEteKGTFVAPTLI-EID-SISDLEREVFGPVLHVVRFKADEldRVIDDINATGYGLTFGLHSRIDE 958
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 498339450 398 KGEHIATHeIEAGACFVN-----ALVASDprlPFGGIKESGYG 435
Cdd:PRK11905 959 TIAHVTSR-IRAGNIYVNrniigAVVGVQ---PFGGEGLSGTG 997
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
6-428 |
8.98e-29 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 120.04 E-value: 8.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPA-TEQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEI 84
Cdd:COG4230 575 RNPAdHSDVVGTVVEATAADVEAALAAAQAAFPAWSATPVEERAAILERAADLLEAHRAELMALLVREAGKTLPDAIAEV 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 85 NKCVWLCEHYAEHAEEYLApkliqtemkkAKVCHVSLGIVFAIMPWNFP---FW-QVfrfaVPTIMAGNAAVLKHAPVSS 160
Cdd:COG4230 655 REAVDFCRYYAAQARRLFA----------APTVLRGRGVFVCISPWNFPlaiFTgQV----AAALAAGNTVLAKPAEQTP 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 161 GTGNKIEELFLEAGFPEHLFQHLIvdNDGA---AKIIENPHVIAVTLTGSgragSAVASHagkfLKKSVLELGGSDPYLV 237
Cdd:COG4230 721 LIAARAVRLLHEAGVPADVLQLLP--GDGEtvgAALVADPRIAGVAFTGS----TETARL----INRTLAARDGPIVPLI 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 238 LE---------D--AdldLAAQC---IVNSRLNNSGQVCiAAKRIIVLksiEEELVNKIIEHI----DAFKMGDPLDPKT 299
Cdd:COG4230 791 AEtggqnamivDssA---LPEQVvddVLASAFDSAGQRC-SALRVLCV---QEDIADRVLEMLkgamAELRVGDPADLST 863
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 300 KLGPLARSDLRENLHIQVEKsLKQGAKLLLGGIIPEG--KGFYYPPTLItQVkPGMPAFDEELFGPVIAIITVDNEE--- 374
Cdd:COG4230 864 DVGPVIDAEARANLEAHIER-MRAEGRLVHQLPLPEEcaNGTFVAPTLI-EI-DSISDLEREVFGPVLHVVRYKADEldk 940
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498339450 375 --EGIkyaNQSRYGLGAAVFTRDLEKGEHIATHeIEAGACFVN-----ALVASDprlPFGG 428
Cdd:COG4230 941 viDAI---NATGYGLTLGVHSRIDETIDRVAAR-ARVGNVYVNrniigAVVGVQ---PFGG 994
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
6-433 |
2.46e-28 |
|
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: 117.30 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 6 VNPAT-EQIIQNYDCLNEQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKI-DELahLMAIEMGKPITAGKAE 83
Cdd:cd07123 51 VMPHDhAHVLATYHYADAALVEKAIEAALEARKEWARMPFEDRAAIFLKAADLLSGKYrYEL--NAATMLGQGKNVWQAE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 84 INKCVWLCE------HYAEHAEEYLAPKliQTEMKKAKVCHVSL-GIVFAIMPWNF-------PfwqvfrfAVPTIMaGN 149
Cdd:cd07123 129 IDAACELIDflrfnvKYAEELYAQQPLS--SPAGVWNRLEYRPLeGFVYAVSPFNFtaiggnlA-------GAPALM-GN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 150 AAVLKHAPVSSGTGNKIEELFLEAGFPEHLFQhlIVDNDGAA---KIIENPHVIAVTLTGS--------GRAGSAVasHA 218
Cdd:cd07123 199 VVLWKPSDTAVLSNYLVYKILEEAGLPPGVIN--FVPGDGPVvgdTVLASPHLAGLHFTGStptfkslwKQIGENL--DR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 219 GKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPK 298
Cdd:cd07123 275 YRTYPRIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 299 TKLGPL--ARSDLRENLHIQVEKSlKQGAKLLLGGIIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNE--E 374
Cdd:cd07123 355 NFMGAVidEKAFDRIKGYIDHAKS-DPEAEIIAGGKCDDSVGYFVEPTVIETTDPKHKLMTEEIFGPVLTVYVYPDSdfE 433
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 375 EGIKYANQ-SRYGLGAAVFTRD---LEKGEHIATHeiEAGACFVN-----ALVAsdpRLPFGGIKESG 433
Cdd:cd07123 434 ETLELVDTtSPYALTGAIFAQDrkaIREATDALRN--AAGNFYINdkptgAVVG---QQPFGGARASG 496
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
25-436 |
1.29e-26 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 112.13 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 25 VNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGK-PITAGKAEINKCVWLCEHYAEHAEEYLA 103
Cdd:PLN02203 8 LEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKhRVEAYRDEVGVLTKSANLALSNLKKWMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 104 PKLIQTEM----KKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNkieelFLEAGFPEHL 179
Cdd:PLN02203 88 PKKAKLPLvafpATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSA-----FLAANIPKYL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 180 fqhlivdNDGAAKIIENPHVIA----------VTLTGSGRAGSAVASHAGKFLKKSVLELGGSDPYLV---LEDADLDLA 246
Cdd:PLN02203 163 -------DSKAVKVIEGGPAVGeqllqhkwdkIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVdslSSSRDTKVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 247 AQCIVNSRLNN-SGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTklgpLAR----------SDLRENLHI 315
Cdd:PLN02203 236 VNRIVGGKWGScAGQACIAIDYVLVEERFAPILIELLKSTIKKFFGENPRESKS----MARilnkkhfqrlSNLLKDPRV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 316 QvekslkqgAKLLLGGIIPEgKGFYYPPTLITQvkpgmPAFD-----EELFGPVIAIITVDNEEEGIKYANQSRYGLGAA 390
Cdd:PLN02203 312 A--------ASIVHGGSIDE-KKLFIEPTILLN-----PPLDsdimtEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIY 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 498339450 391 VFTRDLEKGEHIATHEIEAGACFVNALV--ASDPrLPFGGIKESGYGR 436
Cdd:PLN02203 378 AFTNNEKLKRRILSETSSGSVTFNDAIIqyACDS-LPFGGVGESGFGR 424
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
99-435 |
3.81e-25 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 107.82 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 99 EEYLAPKLIQTEMK----KAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKH---APVSSGTGNKIEELFL 171
Cdd:PLN02174 87 KNWMAPEKAKTSLTtfpaSAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPselAPASSALLAKLLEQYL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 172 EAGfpehlfqhlivdndgAAKIIENPHVIAVTL----------TGSGRAGSAVASHAGKFLKKSVLELGGSDPYLVLEDA 241
Cdd:PLN02174 167 DSS---------------AVRVVEGAVTETTALleqkwdkifyTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 242 DLDLAAQCIVNSRLN-NSGQVCIAAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKtKLGPLARSDLRENLHIQVEKS 320
Cdd:PLN02174 232 DLKVTVRRIIAGKWGcNNGQACISPDYILTTKEYAPKVIDAMKKELETFYGKNPMESK-DMSRIVNSTHFDRLSKLLDEK 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 321 lKQGAKLLLGGiIPEGKGFYYPPTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDLEKGE 400
Cdd:PLN02174 311 -EVSDKIVYGG-EKDRENLKIAPTILLDVPLDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKE 388
|
330 340 350
....*....|....*....|....*....|....*..
gi 498339450 401 HIAThEIEAGACFVN--ALVASDPRLPFGGIKESGYG 435
Cdd:PLN02174 389 RFAA-TVSAGGIVVNdiAVHLALHTLPFGGVGESGMG 424
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
122-438 |
1.17e-21 |
|
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: 97.34 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 122 GIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAG-FPEHLFQhLIVDndGAAKIIEnpHVI 200
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGlLPEGALQ-LICG--SVGDLLD--HLG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 201 ---AVTLTGSGRAGSAVASHAGkFLKKSV---LE--------LGgsdPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAK 266
Cdd:cd07128 221 eqdVVAFTGSAATAAKLRAHPN-IVARSIrfnAEadslnaaiLG---PDATPGTPEFDLFVKEVAREMTVKAGQKCTAIR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 267 RIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKsLKQGAKLLLGG-------IIPEGKGF 339
Cdd:cd07128 297 RAFVPEARVDAVIEALKARLAKVVVGDPRLEGVRMGPLVSREQREDVRAAVAT-LLAEAEVVFGGpdrfevvGADAEKGA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 340 YYPPTLITQVKP-GMPAF-DEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRDlekgEHIATHEIEAGACFVNAL 417
Cdd:cd07128 376 FFPPTLLLCDDPdAATAVhDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTND----PAFARELVLGAAPYHGRL 451
|
330 340 350
....*....|....*....|....*....|....*
gi 498339450 418 VASD--------------PRLPFGGIKESGYGREL 438
Cdd:cd07128 452 LVLNrdsakestghgsplPQLVHGGPGRAGGGEEL 486
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
25-375 |
1.66e-19 |
|
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: 90.37 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 25 VNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKP------ITAGKAEINKCVWLCEHYAEHA 98
Cdd:cd07084 1 PERALLAADISTKAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGwmfaenICGDQVQLRARAFVIYSYRIPH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 99 EeyLAPKLIQTEMKKAKVCHVSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAG-FPE 177
Cdd:cd07084 81 E--PGNHLGQGLKQQSHGYRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYAGlLPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 178 HLFQHLIVDNDGAAKIIENPHVIAVTLTGSGRAGSAVASHAgKFLKKSVlELGGSDPYLVLEDADL--DLAAQCiVNSRL 255
Cdd:cd07084 159 EDVTLINGDGKTMQALLLHPNPKMVLFTGSSRVAEKLALDA-KQARIYL-ELAGFNWKVLGPDAQAvdYVAWQC-VQDMT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 256 NNSGQVCIAAKRIIVLKSIE-EELVNKIIEHIDAFKMGDPLdpktkLGP------LARSDLRENLHIQVeksLKQGAKLL 328
Cdd:cd07084 236 ACSGQKCTAQSMLFVPENWSkTPLVEKLKALLARRKLEDLL-----LGPvqtfttLAMIAHMENLLGSV---LLFSGKEL 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 498339450 329 LGGIIPEGKGFYYPPTLITQVKPGM---PAFDEELFGPVIAIITVDNEEE 375
Cdd:cd07084 308 KNHSIPSIYGACVASALFVPIDEILktyELVTEEIFGPFAIVVEYKKDQL 357
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
122-395 |
6.12e-16 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 80.13 E-value: 6.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 122 GIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEAG-FPEhlfqhlivdndGAAKIIENP--- 197
Cdd:PRK11903 150 GVALFINAFNFPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGiLPA-----------GALSVVCGSsag 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 198 ---HVIA---VTLTGSGRAGSAVASHAGkFLKKSV---LELGGSDPYLVLEDAD-----LDLAAQCIVNSRLNNSGQVCI 263
Cdd:PRK11903 219 lldHLQPfdvVSFTGSAETAAVLRSHPA-VVQRSVrvnVEADSLNSALLGPDAApgseaFDLFVKEVVREMTVKSGQKCT 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 264 AAKRIIVLKSIEEELVNKIIEHIDAFKMGDPLDPKTKLGPLARSDLRENLHIQVEKsLKQGAKLLLGG------IIPEGK 337
Cdd:PRK11903 298 AIRRIFVPEALYDAVAEALAARLAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAA-LRAQAEVLFDGggfalvDADPAV 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 338 GFYYPPTLITQVKP-GMPAF-DEELFGPVIAIITVDNEEEGIKYANQSRYGLGAAVFTRD 395
Cdd:PRK11903 377 AACVGPTLLGASDPdAATAVhDVEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDD 436
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
22-435 |
1.13e-15 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 80.02 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 22 EQHVNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEEY 101
Cdd:PRK11809 681 PAEVEQALESAVNAAPIWFATPPAERAAILERAADLMEAQMQTLMGLLVREAGKTFSNAIAEVREAVDFLRYYAGQVRDD 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 102 LAPKliqtemkkakvCHVSLGIVFAIMPWNFPFwQVFRFAVPTIMA-GNAAVLKHA---PVSSGTGNKIeelFLEAGFPE 177
Cdd:PRK11809 761 FDND-----------THRPLGPVVCISPWNFPL-AIFTGQVAAALAaGNSVLAKPAeqtPLIAAQAVRI---LLEAGVPA 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 178 HLFQHLIVDND--GAAkIIENPHVIAVTLTGSgragSAVAshagKFLKKSV--------------LELGGSDPYLVLEDA 241
Cdd:PRK11809 826 GVVQLLPGRGEtvGAA-LVADARVRGVMFTGS----TEVA----RLLQRNLagrldpqgrpipliAETGGQNAMIVDSSA 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 242 dldLAAQC---IVNSRLNNSGQVCiAAKRIIVLksiEEELVNKIIEHI----DAFKMGDPLDPKTKLGPLARSDLRENL- 313
Cdd:PRK11809 897 ---LTEQVvadVLASAFDSAGQRC-SALRVLCL---QDDVADRTLKMLrgamAECRMGNPDRLSTDIGPVIDAEAKANIe 969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 314 -HIQVEKS---------LKQGAKLLLGGIIpegkgfyyPPTLITqvkpgMPAFDE---ELFGPVIAIITVDNEE-----E 375
Cdd:PRK11809 970 rHIQAMRAkgrpvfqaaRENSEDWQSGTFV--------PPTLIE-----LDSFDElkrEVFGPVLHVVRYNRNQldeliE 1036
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498339450 376 GIkyaNQSRYGLGAAVFTRDLEKGEHIaTHEIEAGACFVN-----ALVASDprlPFGGIKESGYG 435
Cdd:PRK11809 1037 QI---NASGYGLTLGVHTRIDETIAQV-TGSAHVGNLYVNrnmvgAVVGVQ---PFGGEGLSGTG 1094
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
25-375 |
1.54e-11 |
|
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: 66.03 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 25 VNERLNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAHLMAIEMGKPITAGKAEINKCVWLCEHYAEHAEE--YL 102
Cdd:cd07129 1 VDAAAAAAAAAFESYRALSPARRAAFLEAIADEIEALGDELVARAHAETGLPEARLQGELGRTTGQLRLFADLVREgsWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 103 APkLIQTEMKKAKV--------CHVSLG--IVFAimPWNFPFwqvfRFAVP------TIMAGNAAVLKHAPVSSGTGNKI 166
Cdd:cd07129 81 DA-RIDPADPDRQPlprpdlrrMLVPLGpvAVFG--ASNFPL----AFSVAggdtasALAAGCPVVVKAHPAHPGTSELV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 167 EELFLEA----GFPEHLFQhLIVDNDGAA--KIIENPHVIAVTLTGSGRAGSAVASHAGK-------FLkksvlELGGSD 233
Cdd:cd07129 154 ARAIRAAlratGLPAGVFS-LLQGGGREVgvALVKHPAIKAVGFTGSRRGGRALFDAAAArpepipfYA-----ELGSVN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 234 PYLVLEDA---DLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKSIE-EELVNKIIEHIDAFkmgdplDPKTKLGPLARSDL 309
Cdd:cd07129 228 PVFILPGAlaeRGEAIAQGFVGSLTLGAGQFCTNPGLVLVPAGPAgDAFIAALAEALAAA------PAQTMLTPGIAEAY 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 310 REnlhiQVEKSLKQ-GAKLLLGGIIPEGkGFYYPPTLIT---QVKPGMPAFDEELFGPVIAIITVDNEEE 375
Cdd:cd07129 302 RQ----GVEALAAApGVRVLAGGAAAEG-GNQAAPTLFKvdaAAFLADPALQEEVFGPASLVVRYDDAAE 366
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
122-403 |
1.66e-11 |
|
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: 65.72 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 122 GIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAP----VSSGTGNKIEELFLEAGFPEHLFqhLIVDN---DGAAKII 194
Cdd:cd07121 99 GVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPgakkVSAYAVELINKAIAEAGGPDNLV--VTVEEptiETTNELM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 195 ENPHVIAVTLTGsgraGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVN--SRLNNsgQVCIAAKRIIVLK 272
Cdd:cd07121 177 AHPDINLLVVTG----GPAVVKAALSSGKKAIGAGAGNPPVVVDETADIEKAARDIVQgaSFDNN--LPCIAEKEVIAVD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 273 SIEEELVNKIIEHiDAFKMGDP-LDPKTKLGPLARSDLRENlhiqveKSL--KQGAKLL--LGGIIPEGkgfyyPPTLIT 347
Cdd:cd07121 251 SVADYLIAAMQRN-GAYVLNDEqAEQLLEVVLLTNKGATPN------KKWvgKDASKILkaAGIEVPAD-----IRLIIV 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 348 QVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGL--GAAVFTRDLEKGEHIA 403
Cdd:cd07121 319 ETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAVELEHGNrhTAIIHSKNVENLTKMA 376
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
145-380 |
3.28e-10 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 61.84 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 145 IMAGNAAVLKHAP----VSSGTGNKIEELFLEAGFPEHLFqhLIVDN---DGAAKIIENPHVIAVTLTGsgraGSAVASH 217
Cdd:PRK15398 154 LAAGNSVVFSPHPgakkVSLRAIELLNEAIVAAGGPENLV--VTVAEptiETAQRLMKHPGIALLVVTG----GPAVVKA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 218 AGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVN--SRLNNsgQVCIAAKRIIVLKSIEEELVNKIIEHiDAFKmgdpL 295
Cdd:PRK15398 228 AMKSGKKAIGAGAGNPPVVVDETADIEKAARDIVKgaSFDNN--LPCIAEKEVIVVDSVADELMRLMEKN-GAVL----L 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 296 DPK--TKLGPLArsdLRENLHIQ---VEKSlkqgAKLLLGGI-IPEGKGfyyPPTLITQVKPGMPAFDEELFGPVIAIIT 369
Cdd:PRK15398 301 TAEqaEKLQKVV---LKNGGTVNkkwVGKD----AAKILEAAgINVPKD---TRLLIVETDANHPFVVTELMMPVLPVVR 370
|
250
....*....|.
gi 498339450 370 VDNEEEGIKYA 380
Cdd:PRK15398 371 VKDVDEAIALA 381
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
121-402 |
1.20e-09 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 59.97 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 121 LGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVSSGTGNKIEELFLEA----GFPEHLFqhLIVDN---DGAAKI 193
Cdd:cd07081 96 IGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLLLQAavaaGAPENLI--GWIDNpsiELAQRL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 194 IENPHVIAVTLTGsgraGSAVASHAGKFLKKSVLELGGSDPYLVLEDADLDLAAQCIVNSRLNNSGQVCIAAKRIIVLKS 273
Cdd:cd07081 174 MKFPGIGLLLATG----GPAVVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICASEQSVIVVDS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 274 IEEELVNKIIEHIDAFKMGDPLDpktKLGPLARSDLRENLHIqveksLKQGAklllgGIIPEGKGFYYPPT---LITQVK 350
Cdd:cd07081 250 VYDEVMRLFEGQGAYKLTAEELQ---QVQPVILKNGDVNRDI-----VGQDA-----YKIAAAAGLKVPQEtriLIGEVT 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 498339450 351 PG--MPAFDEELFGPVIAIITVDNEEEGIKYA----NQSRYGLGAAVFTRDLEKGEHI 402
Cdd:cd07081 317 SLaeHEPFAHEKLSPVLAMYRAANFADADAKAlalkLEGGCGHTSAMYSDNIKAIENM 374
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
29-421 |
2.34e-08 |
|
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: 56.33 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 29 LNKAHETYLAWKITSFNQRKTLMLQLAELLKSKIDELAH----------LMAIEMGKPITAGKA-EINKCVWLCEHYAEH 97
Cdd:cd07127 90 LAAARAAMPGWRDAGARARAGVCLEILQRLNARSFEMAHavmhttgqafMMAFQAGGPHAQDRGlEAVAYAWREMSRIPP 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 98 AEEYLAPKLIQTEMKKAKVCH-VSLGIVFAIMPWNFPFWQVFRFAVPTIMAGNAAVLKHAPVS----SGTGNKIEELFLE 172
Cdd:cd07127 170 TAEWEKPQGKHDPLAMEKTFTvVPRGVALVIGCSTFPTWNGYPGLFASLATGNPVIVKPHPAAilplAITVQVAREVLAE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 173 AGFPEHLFQhLIVDNDG---AAKIIENPHVIAVTLTGSGRAGSAVASHAGKflKKSVLELGGSDPYLVLEDADLDLAAQC 249
Cdd:cd07127 250 AGFDPNLVT-LAADTPEepiAQTLATRPEVRIIDFTGSNAFGDWLEANARQ--AQVYTEKAGVNTVVVDSTDDLKAMLRN 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 250 IVNSRLNNSGQVCIAAKRIIVLKS-IE--------EELVNKIIEHIDAFkMGDPLDPKTKLGPlarsdlrenlhIQVEKS 320
Cdd:cd07127 327 LAFSLSLYSGQMCTTPQNIYVPRDgIQtddgrksfDEVAADLAAAIDGL-LADPARAAALLGA-----------IQSPDT 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498339450 321 LKQGAKL-LLGGIIPEGKGFYYP---------PTLITQVKPGMPAFDEELFGPVIAIITVDNEEEGIKYANQSRYGLGA- 389
Cdd:cd07127 395 LARIAEArQLGEVLLASEAVAHPefpdarvrtPLLLKLDASDEAAYAEERFGPIAFVVATDSTDHSIELARESVREHGAm 474
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 498339450 390 --AVFTRD---LEKGEHIATHEIEA------GACFVNALVA-SD 421
Cdd:cd07127 475 tvGVYSTDpevVERVQEAALDAGVAlsinltGGVFVNQSAAfSD 518
|
|
| DUF268 |
pfam03269 |
Caenorhabditis protein of unknown function, DUF268; |
283-337 |
9.59e-03 |
|
Caenorhabditis protein of unknown function, DUF268;
Pssm-ID: 367429 Cd Length: 176 Bit Score: 36.91 E-value: 9.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 498339450 283 IEHIDAFKMGDPLDPKtklgplarSDLRENLHIQVekSLKQGAKLLLGgiIPEGK 337
Cdd:pfam03269 72 IEHSGLGRYGDPLDPI--------GDLREMLKIKC--VLKKGGLLFLG--LPLGT 114
|
|
| |
