|
Name |
Accession |
Description |
Interval |
E-value |
| PaaN-DH |
TIGR02278 |
phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening ... |
5-675 |
0e+00 |
|
phenylacetic acid degradation protein paaN; This enzyme is proposed to act in the ring-opening step of phenylacetic acid degradation which follows ligation of the acid with coenzyme A (by PaaF) and hydroxylation by a multicomponent non-heme iron hydroxylase complex (PaaGHIJK). Gene symbols have been standardized in. This enzyme is related to aldehyde dehydrogenases and has domains which are members of the pfam00171 and pfam01575 families. This family includes paaN genes from Pseudomonas, Sinorhizobium, Rhodopseudomonas, Escherichia, Deinococcus and Corynebacterium. Another homology family (TIGR02288) includes several other species.
Pssm-ID: 131331 [Multi-domain] Cd Length: 663 Bit Score: 931.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 5 LESYVSGKWIAPEGESIPLINASTGEEVARFASGSLDVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRKEEFY 84
Cdd:TIGR02278 1 LQSYLSGEWRTGQGEGVPVRDASTGEVLARVTSEGLDVAAAVAWAREVGGPALRALTFHERARMLKALAQYLSERKEALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 85 PSSTATGATAKDSGIDIDGGIGTLLSYASKGTRELPNDTIYLDGGLEPLGRGGTFVGQHIYTSRPGVAVQINAFNFPVWG 164
Cdd:TIGR02278 81 ALAATTGATRRDNWVDIDGGIGTLFTYSSLGRRELPDANLIPEDEFEPLSKDGSFQGRHILTPKGGVAVQINAFNFPVWG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 165 MLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLLPEGSIQLLCASPRALLDHLDGQDTVLFTGSASTASKLRGH 244
Cdd:TIGR02278 161 LLEKFAPAFLAGVPTLAKPATPTAYVAEALVRTMVESGLLPEGSLQLICGSAGDLLDHLDHRDVVAFTGSAATADRLRAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 245 PNVVEGGVRFNAEADSLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVV 324
Cdd:TIGR02278 241 PNVLERGIRFNAEADSLNAAILGEDATPDEPEFDLFAQEIVRELTIKAGQKCTAIRRVIVPKALLEAVLKALQARLAKVV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 325 VGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDPDDFsvegadasSGAFLPPLLLRAQDSAAAAIHEVEAFG 403
Cdd:TIGR02278 321 LGDPREEGVDMGPLVSLEQRADVEAAVAALLAAgAEVRLGGPGRL--------DGAFFPPTLLLAEDPWAGAVHATEAFG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 404 PISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGVAPFHGRILILDRDDAKESTGHGSPLPTLIHGGPGRA 483
Cdd:TIGR02278 393 PVATFFPYGDRAEAARLAARGGGSLVATLATSDPEEARQFILGLAPYHGRLHILNRDDAAESTGHGSPLPRLLHGGPGRA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 484 GGGEELGGIRGVLHFMQRTAIQASPDMLTAITGRWTTGSARTNTDVHPFRKHLEELQIGDTVVGGPRVVSLEDIDHFAEF 563
Cdd:TIGR02278 473 GGGEELGGLRSVKHYMQRTAIQGSPWLLAALTGQWARGAEVPGAEVHPFRKPYEDLEIGDSLTTHRRTVTEADIALFAAL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 564 TGDTFYAHTDPKAAAENpLFGGIVAHGYLVVSLAAGLFVEPNPGPVLANFGVDGLRFLTPVKAGDALTVTLTAKQVTPRL 643
Cdd:TIGR02278 553 SGDHFYAHMDEIAARES-FFGKRVAHGYFVLSAAAGLFVDPAPGPVLANYGLENLRFLEPVGPGDTIQVRLTVKRKTPRD 631
|
650 660 670
....*....|....*....|....*....|..
gi 1816981345 644 SADYGEVRWDAVVANQNDDPVATYDVLTLVAK 675
Cdd:TIGR02278 632 EKTYGVVEWAAEVVNQNGEPVATYDVLTLVAR 663
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
5-516 |
0e+00 |
|
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: 824.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 5 LESYVSGKWIAPEGESIPLINASTGEEVARFASGSLDVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRKEEFY 84
Cdd:cd07128 1 LQSYVAGQWHAGTGDGRTLHDAVTGEVVARVSSEGLDFAAAVAYAREKGGPALRALTFHERAAMLKALAKYLMERKEDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 85 PSSTATGATAKDSGIDIDGGIGTLLSYASKGTRELPNDTIYLDGGLEPLGRGGTFVGQHIYTSRPGVAVQINAFNFPVWG 164
Cdd:cd07128 81 ALSAATGATRRDSWIDIDGGIGTLFAYASLGRRELPNAHFLVEGDVEPLSKDGTFVGQHILTPRRGVAVHINAFNFPVWG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 165 MLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLLPEGSIQLLCASPRALLDHLDGQDTVLFTGSASTASKLRGH 244
Cdd:cd07128 161 MLEKFAPALLAGVPVIVKPATATAYLTEAVVKDIVESGLLPEGALQLICGSVGDLLDHLGEQDVVAFTGSAATAAKLRAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 245 PNVVEGGVRFNAEADSLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVV 324
Cdd:cd07128 241 PNIVARSIRFNAEADSLNAAILGPDATPGTPEFDLFVKEVAREMTVKAGQKCTAIRRAFVPEARVDAVIEALKARLAKVV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 325 VGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPDDFSVEGADASSGAFLPPLLLRAQD-SAAAAIHEVEAFG 403
Cdd:cd07128 321 VGDPRLEGVRMGPLVSREQREDVRAAVATLLAEAEVVFGGPDRFEVVGADAEKGAFFPPTLLLCDDpDAATAVHDVEAFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 404 PISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGVAPFHGRILILDRDDAKESTGHGSPLPTLIHGGPGRA 483
Cdd:cd07128 401 PVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELVLGAAPYHGRLLVLNRDSAKESTGHGSPLPQLVHGGPGRA 480
|
490 500 510
....*....|....*....|....*....|...
gi 1816981345 484 GGGEELGGIRGVLHFMQRTAIQASPDMLTAITG 516
Cdd:cd07128 481 GGGEELGGLRGVKHYMQRTAVQGSPTMLTAITG 513
|
|
| PRK11903 |
PRK11903 |
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase; |
1-516 |
0e+00 |
|
3,4-dehydroadipyl-CoA semialdehyde dehydrogenase;
Pssm-ID: 237016 [Multi-domain] Cd Length: 521 Bit Score: 553.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 1 MTAVLESYVSGKWIAPEGESIPLINASTGEEVARFASGSLDVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRK 80
Cdd:PRK11903 1 MTELLANYVAGRWQAGSGAGTPLFDPVTGEELVRVSATGLDLAAAFAFAREQGGAALRALTYAQRAALLAAIVKVLQANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 81 EEFYPSSTA-TGATAKDSGIDIDGGIGTLLSYASKGtRELPNDTIYLDGGLEPLGRGGTFVGQHIYTSRPGVAVQINAFN 159
Cdd:PRK11903 81 DAYYDIATAnSGTTRNDSAVDIDGGIFTLGYYAKLG-AALGDARLLRDGEAVQLGKDPAFQGQHVLVPTRGVALFINAFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 160 FPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLLPEGSIQLLCASPRALLDHLDGQDTVLFTGSASTAS 239
Cdd:PRK11903 160 FPAWGLWEKAAPALLAGVPVIVKPATATAWLTQRMVKDVVAAGILPAGALSVVCGSSAGLLDHLQPFDVVSFTGSAETAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 240 KLRGHPNVVEGGVRFNAEADSLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTR 319
Cdd:PRK11903 240 VLRSHPAVVQRSVRVNVEADSLNSALLGPDAAPGSEAFDLFVKEVVREMTVKSGQKCTAIRRIFVPEALYDAVAEALAAR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 320 LSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFgDPDDFSVEGADASSGAFLPPLLLRAQDS-AAAAIHE 398
Cdd:PRK11903 320 LAKTTVGNPRNDGVRMGPLVSRAQLAAVRAGLAALRAQAEVLF-DGGGFALVDADPAVAACVGPTLLGASDPdAATAVHD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 399 VEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGVAPFHGRILILDRDDAKESTGHGSPLPTLIHG 478
Cdd:PRK11903 399 VEVFGPVATLLPYRDAAHALALARRGQGSLVASVYSDDAAFLAAAALELADSHGRVHVISPDVAALHTGHGNVMPQSLHG 478
|
490 500 510
....*....|....*....|....*....|....*...
gi 1816981345 479 GPGRAGGGEELGGIRGVLHFMQRTAIQASPDMLTAITG 516
Cdd:PRK11903 479 GPGRAGGGEELGGLRALAFYHRRSAVQASPAVLDALTQ 516
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
1-505 |
8.72e-97 |
|
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: 306.28 E-value: 8.72e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 1 MTAV-LESYVSGKWIAP-EGESIPLINASTGEEVARFASGS-LDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLM 77
Cdd:COG1012 1 MTTPeYPLFIGGEWVAAaSGETFDVINPATGEVLARVPAATaEDVDAAVAAARA-AFPAWAATPPAERAAILLRAADLLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 78 SRKEEFYPSSTA-TGATAKDSGIDIDGGIGTLLSYASKGTRelpndtiyLDGGLEPLGRGGTfvgqHIYTSR-P-GVAVQ 154
Cdd:COG1012 80 ERREELAALLTLeTGKPLAEARGEVDRAADFLRYYAGEARR--------LYGETIPSDAPGT----RAYVRRePlGVVGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 155 INAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPR----ALLDHlDGQDTVL 230
Cdd:COG1012 148 ITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAGL-PAGVLNVVTGDGSevgaALVAH-PDVDKIS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 231 FTGSASTASKLRGHPNvvEGGVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVD 310
Cdd:COG1012 226 FTGSTAVGRRIAAAAA--ENLKRVTLELGGKNPAIVLDDA-----DLDAAVEAAVRGAFGNAGQRCTAASRLLVHESIYD 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 311 DVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDpddfsvEGADASSGAFLPPLLLRAQ 389
Cdd:COG1012 299 EFVERLVAAAKALKVGDPLDPGTDMGPLISEAQLERVLAYIEDAVAEgAELLTGG------RRPDGEGGYFVEPTVLADV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 390 DSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGVApfHGRILILD----RDDA--- 462
Cdd:COG1012 373 TPDMRIARE-EIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLE--AGMVWINDgttgAVPQapf 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1816981345 463 ---KEStGHGSPlptlihggpgragggeelGGIRGVLHFMQRTAIQ 505
Cdd:COG1012 450 ggvKQS-GIGRE------------------GGREGLEEYTETKTVT 476
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
42-506 |
1.95e-68 |
|
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: 230.59 E-value: 1.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 42 VAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTATGATAKDSGIDIDGGIGTLLSYASKGtrelpN 121
Cdd:cd07084 1 PERALLAADIST-KAARRLALPKRADFLARIIQRLAAKSYDIAAGAVLVTGKGWMFAENICGDQVQLRARAFVI-----Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 122 DTIYLDGGLEPLGRGGTFVGQHiYTSRPGVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVES 201
Cdd:cd07084 75 SYRIPHEPGNHLGQGLKQQSHG-YRWPYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 202 GLLPEGSIQLLCASPR---ALLDHLDgQDTVLFTGSASTASKLRGHPNVveggVRFNAEADSLNCSILGPDAakdtPEFE 278
Cdd:cd07084 154 GLLPPEDVTLINGDGKtmqALLLHPN-PKMVLFTGSSRVAEKLALDAKQ----ARIYLELAGFNWKVLGPDA----QAVD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 279 LYIKQLVAEMTTKAGQKCTAIRRALVPNEL-VDDVVEATRTRLSKVVVGhpnaegvrmGPLASLDQREEVLRSLKSLR-D 356
Cdd:cd07084 225 YVAWQCVQDMTACSGQKCTAQSMLFVPENWsKTPLVEKLKALLARRKLE---------DLLLGPVQTFTTLAMIAHMEnL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 357 SATVVFGDPDDFSVEGADASSGAFLPPLLLRAQDSAAAA--IHEVEAFGPISTVIGYSD--VDDAIQLAARGKGSLVGSL 432
Cdd:cd07084 296 LGSVLLFSGKELKNHSIPSIYGACVASALFVPIDEILKTyeLVTEEIFGPFAIVVEYKKdqLALVLELLERMHGSLTAAI 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816981345 433 VTHDPAVARQVTLGVApFHGRILILDRddakestGHGSPLPTLIH-GGPGRAGGGEELGGIRGVLHFMQRTAIQA 506
Cdd:cd07084 376 YSNDPIFLQELIGNLW-VAGRTYAILR-------GRTGVAPNQNHgGGPAADPRGAGIGGPEAIKLVWRCHAEQA 442
|
|
| MaoC_C |
cd03452 |
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ... |
536-676 |
7.08e-68 |
|
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.
Pssm-ID: 239536 [Multi-domain] Cd Length: 142 Bit Score: 218.42 E-value: 7.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 536 LEELQIGDTVVGGPRVVSLEDIDHFAEFTGDTFYAHTDPKAAAENpLFGGIVAHGYLVVSLAAGLFVEPNPGPVLANFGV 615
Cdd:cd03452 2 LEQLRPGDSLLTHRRTVTEADIVNFACLTGDHFYAHMDEIAAKAS-FFGKRVAHGYFVLSAAAGLFVDPAPGPVLANYGL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816981345 616 DGLRFLTPVKAGDALTVTLTAKQVTPRLSADYGEVRWDAVVANQNDDPVATYDVLTLVAKK 676
Cdd:cd03452 81 ENLRFLEPVYPGDTIQVRLTCKRKIPRDGQDYGVVRWDAEVTNQNGELVASYDILTLVAKK 141
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
44-444 |
9.20e-60 |
|
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: 207.06 E-value: 9.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 44 AAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDSGIDIDGGIGTLLSYASKGTRelpnd 122
Cdd:cd07078 2 AAVAAARAAF-KAWAALPPAERAAILRKLADLLEERREELAALETLeTGKPIEEALGEVARAADTFRYYAGLARR----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 123 tiyLDGGLEPLGRGGTfvgQHIYTSRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVES 201
Cdd:cd07078 76 ---LHGEVIPSPDPGE---LAIVRREPlGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 202 GLlPEGSIQLLCASPR----ALLDHlDGQDTVLFTGSASTASKLRGhpNVVEGGVRFNAEADSLNCSILGPDAakdtpEF 277
Cdd:cd07078 150 GL-PPGVLNVVTGDGDevgaALASH-PRVDKISFTGSTAVGKAIMR--AAAENLKRVTLELGGKSPLIVFDDA-----DL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 278 ELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS 357
Cdd:cd07078 221 DAAVKGAVFGAFGNAGQVCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDTDMGPLISAAQLDRVLAYIEDAKAE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 358 -ATVVFGDpddfsvEGADASSGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07078 301 gAKLLCGG------KRLEGGKGYFVPPTVL-TDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRD 373
|
....*...
gi 1816981345 437 PAVARQVT 444
Cdd:cd07078 374 LERALRVA 381
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
13-443 |
5.59e-57 |
|
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: 200.06 E-value: 5.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 13 WIAPEGESIPLINASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEF-YPSSTAT 90
Cdd:pfam00171 1 WVDSESETIEVINPATGEVIATVPAATAeDVDAAIAAARA-AFPAWRKTPAAERAAILRKAADLLEERKDELaELETLEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 91 GATAKDSGIDIDGGIGTLLSYASKGTRelpndtiyLDGGLEPLGRGGTfvgqhIYTSR-P-GVAVQINAFNFPVWGMLEK 168
Cdd:pfam00171 80 GKPLAEARGEVDRAIDVLRYYAGLARR--------LDGETLPSDPGRL-----AYTRRePlGVVGAITPWNFPLLLPAWK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 169 LAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPR----ALLDHlDGQDTVLFTGSASTASKLrgH 244
Cdd:pfam00171 147 IAPALAAGNTVVLKPSELTPLTALLLAELFEEAGL-PAGVLNVVTGSGAevgeALVEH-PDVRKVSFTGSTAVGRHI--A 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 245 PNVVEGGVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVV 324
Cdd:pfam00171 223 EAAAQNLKRVTLELGGKNPLIVLEDA-----DLDAAVEAAVFGAFGNAGQVCTATSRLLVHESIYDEFVEKLVEAAKKLK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 325 VGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDPDDFsvegadaSSGAFLPPLLLRAQDSAAAAIHEvEAFG 403
Cdd:pfam00171 298 VGDPLDPDTDMGPLISKAQLERVLKYVEDAKEEgAKLLTGGEAGL-------DNGYFVEPTVLANVTPDMRIAQE-EIFG 369
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1816981345 404 PISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:pfam00171 370 PVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRV 409
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
8-447 |
1.23e-45 |
|
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: 168.91 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPEG-ESIPLINASTGEEVARFASGSL-DVAAAIAYGREV-GGPALRALTFHQRAGALKALGKLLMSRKEEFY 84
Cdd:cd07139 2 FIGGRWVAPSGsETIDVVSPATEEVVGRVPEATPaDVDAAVAAARRAfDNGPWPRLSPAERAAVLRRLADALEARADELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 85 PSSTA-TGATAKDSGIDIDGGIGTLLSYASKGTRELPNDTIyldggleplgRGGTFVGQHIYTSRP-GVAVQINAFNFPV 162
Cdd:cd07139 82 RLWTAeNGMPISWSRRAQGPGPAALLRYYAALARDFPFEER----------RPGSGGGHVLVRREPvGVVAAIVPWNAPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 163 WGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASpRALLDHL---DGQDTVLFTGS----- 234
Cdd:cd07139 152 FLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAAEEAGL-PPGVVNVVPAD-REVGEYLvrhPGVDKVSFTGStaagr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 235 ---ASTASKLRghpnvveggvRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDD 311
Cdd:cd07139 230 riaAVCGERLA----------RVTLELGGKSAAIVLDDA-----DLDAAVPGLVPASLMNNGQVCVALTRILVPRSRYDE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 312 VVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSL-KSLRDSATVVFG--DPDDFsvegadaSSGAFLPPLLLRA 388
Cdd:cd07139 295 VVEALAAAVAALKVGDPLDPATQIGPLASARQRERVEGYIaKGRAEGARLVTGggRPAGL-------DRGWFVEPTLFAD 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816981345 389 QDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDP----AVARQVTLGV 447
Cdd:cd07139 368 VDNDMRIAQE-EIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVerglAVARRIRTGT 429
|
|
| MaoC |
COG2030 |
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism]; |
535-677 |
2.88e-42 |
|
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
Pssm-ID: 441633 [Multi-domain] Cd Length: 140 Bit Score: 149.65 E-value: 2.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 535 HLEELQIGDTVVGGPRVVSLEDIDHFAEFTGDTFYAHTDPKAAAENPlFGGIVAHGYLVVSLAAGLFVEPNPGPVLANFG 614
Cdd:COG2030 1 YFEDLEVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATG-FGGRIAHGMLTLSLASGLLVDDLPGTAVANLG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816981345 615 VDGLRFLTPVKAGDALTVTLTAKQVTPrlSADYGEVRWDAVVANQNDDPVATYDVLTLVAKKN 677
Cdd:COG2030 80 LQEVRFLRPVRVGDTLRARVEVLEKRE--SKSRGIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
6-421 |
3.37e-41 |
|
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: 156.64 E-value: 3.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 6 ESYVSGKWIAPeGESIPLIN-ASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEF 83
Cdd:cd07097 2 RNYIDGEWVAG-GDGEENRNpSDTSDVVGKYARASAeDADAAIAAAAA-AFPAWRRTSPEARADILDKAGDELEARKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 ypSSTAT---GATAKDSGIDIDGGIGTLLSYASKGTRelpndtiyLDGGLEPLGRGGTFVgqhiYTSRP--GVAVQINAF 158
Cdd:cd07097 80 --ARLLTreeGKTLPEARGEVTRAGQIFRYYAGEALR--------LSGETLPSTRPGVEV----ETTREplGVVGLITPW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 159 NFPV----WgmleKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPR----ALLDHlDGQDTVL 230
Cdd:cd07097 146 NFPIaipaW----KIAPALAYGNTVVFKPAELTPASAWALVEILEEAGL-PAGVFNLVMGSGSevgqALVEH-PDVDAVS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 231 FTGSASTASKLrgHPNVVEGGVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVD 310
Cdd:cd07097 220 FTGSTAVGRRI--AAAAAARGARVQLEMGGKNPLVVLDDA-----DLDLAVECAVQGAFFSTGQRCTASSRLIVTEGIHD 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 311 DVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLR-DSATVVF-GDPddfsVEGADasSGAFLPPLLLrA 388
Cdd:cd07097 293 RFVEALVERTKALKVGDALDEGVDIGPVVSERQLEKDLRYIEIARsEGAKLVYgGER----LKRPD--EGYYLAPALF-A 365
|
410 420 430
....*....|....*....|....*....|...
gi 1816981345 389 QDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLA 421
Cdd:cd07097 366 GVTNDMRIAREEIFGPVAAVIRVRDYDEALAIA 398
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
8-443 |
4.78e-41 |
|
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: 156.12 E-value: 4.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPEG-ESIPLINASTGEEVARFASGSL-DVAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEFY- 84
Cdd:cd07138 2 YIDGAWVAPAGtETIDVINPATEEVIGTVPLGTAaDVDRAVAAARRAF-PAWSATSVEERAALLERIAEAYEARADELAq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 85 --------PSSTATGATAkdsgidiDGGIGTLLSYAS-----KGTRELPNDTIYLdgglEPLGrggtfvgqhiytsrpgV 151
Cdd:cd07138 81 aitlemgaPITLARAAQV-------GLGIGHLRAAADalkdfEFEERRGNSLVVR----EPIG----------------V 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 152 AVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPR----ALLDHLDgQD 227
Cdd:cd07138 134 CGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAGL-PAGVFNLVNGDGPvvgeALSAHPD-VD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 228 TVLFTGSASTASKlrghpnVVEggvrfnAEADSL----------NCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCT 297
Cdd:cd07138 212 MVSFTGSTRAGKR------VAE------AAADTVkrvalelggkSANIILDDA-----DLEKAVPRGVAACFANSGQSCN 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 298 AIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKS-LRDSATVVFGDPDdfSVEGADas 376
Cdd:cd07138 275 APTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATTLGPLASAAQFDRVQGYIQKgIEEGARLVAGGPG--RPEGLE-- 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816981345 377 SGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07138 351 RGYFVKPTVF-ADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAV 416
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
8-444 |
1.07e-38 |
|
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: 149.34 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPE-GESIPLINASTGEEVARFASGSL-DVAAAIAyGREVGGPALRALTFHQRAGALKALGKLLMSRKEEFYP 85
Cdd:cd07088 1 YINGEFVPSSsGETIDVLNPATGEVVATVPAATAeDADRAVD-AAEAAQKAWERLPAIERAAYLRKLADLIRENADELAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 SSTA-TGATAKDSGIDIDGGIgTLLSYASKGTR---------ELPNDTIYLDGglEPLGrggtfvgqhiytsrpgVAVQI 155
Cdd:cd07088 80 LIVEeQGKTLSLARVEVEFTA-DYIDYMAEWARriegeiipsDRPNENIFIFK--VPIG----------------VVAGI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 156 NAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHLDGQ---DTVLFT 232
Cdd:cd07088 141 LPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFAELVDEAGL-PAGVLNIVTGRGSVVGDALVAHpkvGMISLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 233 GSASTASKL--RGHPNVVE-----GGvrfNAEAdslncsILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVP 305
Cdd:cd07088 220 GSTEAGQKImeAAAENITKvslelGG---KAPA------IVMKDA-----DLDLAVKAIVDSRIINCGQVCTCAERVYVH 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 306 NELVDDVVEATRTRLSKVVVGHPNAEGVRMGPL---ASLDQREEVLRslKSLRDSATVVFGdpddfsveGADAS--SGAF 380
Cdd:cd07088 286 EDIYDEFMEKLVEKMKAVKVGDPFDAATDMGPLvneAALDKVEEMVE--RAVEAGATLLTG--------GKRPEgeKGYF 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816981345 381 LPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07088 356 YEPTVLTNVRQDMEIVQE-EIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRAT 418
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
55-444 |
2.39e-38 |
|
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: 145.84 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 55 PALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDSGIDIDGGIGTLLSYASKGTRELPNDTIYLDGGlepl 133
Cdd:cd06534 8 KAWAALPPAERAAILRKIADLLEERREELAALETLeTGKPIEEALGEVARAIDTFRYAAGLADKLGGPELPSPDPG---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 134 grggtfvGQHIYTSRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGlLPEGSIQLL 212
Cdd:cd06534 84 -------GEAYVRREPlGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAG-LPPGVVNVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 213 CASPR----ALLDHlDGQDTVLFTGSASTASKLRGHPNvvEGGVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEM 288
Cdd:cd06534 156 PGGGDevgaALLSH-PRVDKISFTGSTAVGKAIMKAAA--ENLKPVTLELGGKSPVIVDEDA-----DLDAAVEGAVFGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 289 TTKAGQKCTAIRRALVPNELVDDVVEatrtRLskvvvghpnaegvrmgplasldqreevlrslkslrdsATVVFGDPDDF 368
Cdd:cd06534 228 FFNAGQICTAASRLLVHESIYDEFVE----KL-------------------------------------VTVLVDVDPDM 266
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816981345 369 SvegadassgaflpplllraqdsaaaaIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd06534 267 P--------------------------IAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVA 316
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
4-443 |
3.03e-38 |
|
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: 148.10 E-value: 3.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 4 VLESYVSGKWIAPEGESIPLINASTGEEVARFAS-GSLDVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRKEE 82
Cdd:cd07082 1 QFKYLINGEWKESSGKTIEVYSPIDGEVIGSVPAlSALEILEAAETAYDAGRGWWPTMPLEERIDCLHKFADLLKENKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 83 FYPS-STATGATAKDSGIDIDGGIgTLLSYASKGTRELPNDTIYLDGGLEPLGRGGTFvgqhiytSR-P-GVAVQINAFN 159
Cdd:cd07082 81 VANLlMWEIGKTLKDALKEVDRTI-DYIRDTIEELKRLDGDSLPGDWFPGTKGKIAQV-------RRePlGVVLAIGPFN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 160 FPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHL--DGQ-DTVLFTGSAS 236
Cdd:cd07082 153 YPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHDAGF-PKGVVNVVTGRGREIGDPLvtHGRiDVISFTGSTE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 237 TASKL-RGHPnvvegGVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEA 315
Cdd:cd07082 232 VGNRLkKQHP-----MKRLVLELGGKDPAIVLPDA-----DLELAAKEIVKGALSYSGQRCTAIKRVLVHESVADELVEL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 316 TRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGDpddfsvegaDASSGAFLPPLLLRAQDSAAA 394
Cdd:cd07082 302 LKEEVAKLKVGMPWDNGVDITPLIDPKSADFVEGLIDdAVAKGATVLNGG---------GREGGNLIYPTLLDPVTPDMR 372
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1816981345 395 AIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07082 373 LAWE-EPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDINKARKL 420
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
8-444 |
4.03e-38 |
|
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: 147.84 E-value: 4.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAP-EGESIPLINASTGEEVARFASGSL-DVAAAIAYGREV-GGPALRALTFHQRAGALKALGKLLMSRKEEFY 84
Cdd:cd07119 1 YIDGEWVEAaSGKTRDIINPANGEVIATVPEGTAeDAKRAIAAARRAfDSGEWPHLPAQERAALLFRIADKIREDAEELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 85 PSSTA-TGATAKDSGIDIDGGIGTLLSYASKGTRElpndtiylDGGLEPlgrggtfVGQHI--YTSRP--GVAVQINAFN 159
Cdd:cd07119 81 RLETLnTGKTLRESEIDIDDVANCFRYYAGLATKE--------TGEVYD-------VPPHVisRTVREpvGVCGLITPWN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 160 FP----VWgmleKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHLDGQ---DTVLFT 232
Cdd:cd07119 146 YPllqaAW----KLAPALAAGNTVVIKPSEVTPLTTIALFELIEEAGL-PAGVVNLVTGSGATVGAELAESpdvDLVSFT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 233 GSAST-ASKLRGHPNVVEggvRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDD 311
Cdd:cd07119 221 GGTATgRSIMRAAAGNVK---KVALELGGKNPNIVFADA-----DFETAVDQALNGVFFNAGQVCSAGSRLLVEESIHDK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 312 VVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGD--PDDfsvegADASSGAFLPPLLLRA 388
Cdd:cd07119 293 FVAALAERAKKIKLGNGLDADTEMGPLVSAEHREKVLSYIQlGKEEGARLVCGGkrPTG-----DELAKGYFVEPTIFDD 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1816981345 389 QDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07119 368 VDRTMRIVQE-EIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVA 422
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
7-421 |
5.44e-36 |
|
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: 141.55 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 7 SYVSGKWIAPEGESIPLINASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEfyp 85
Cdd:cd07086 1 GVIGGEWVGSGGETFTSRNPANGEPIARVFPASPeDVEAAVAAARE-AFKEWRKVPAPRRGEIVRQIGEALRKKKEA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 sstatgatakdsgididggIGTLLSY-ASKGTRELPN------DTIYLDGGLeplGRggTFVGQHIYTSRPG-------- 150
Cdd:cd07086 77 -------------------LGRLVSLeMGKILPEGLGevqemiDICDYAVGL---SR--MLYGLTIPSERPGhrlmeqwn 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 151 ----VAVqINAFNFP--VWGMleKLAPAFLAGVPSIVKPAHQTAY----LTELVVRAIVESGLlPEGSIQLLC--ASPRA 218
Cdd:cd07086 133 plgvVGV-ITAFNFPvaVPGW--NAAIALVCGNTVVWKPSETTPLtaiaVTKILAEVLEKNGL-PPGVVNLVTggGDGGE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 219 LLDHLDGQDTVLFTGS-------ASTASKLRGHPNVVEGGvrfNaeadslNCSILGPDAakdtpEFELYIKQ-LVAEMTT 290
Cdd:cd07086 209 LLVHDPRVPLVSFTGStevgrrvGETVARRFGRVLLELGG---N------NAIIVMDDA-----DLDLAVRAvLFAAVGT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 291 kAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDPddfS 369
Cdd:cd07086 275 -AGQRCTTTRRLIVHESVYDEFLERLVKAYKQVRIGDPLDEGTLVGPLINQAAVEKYLNAIEIAKSQgGTVLTGGK---R 350
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1816981345 370 VEGADAssGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLA 421
Cdd:cd07086 351 IDGGEP--GNYVEPTIVTGVTDDARIVQE-ETFAPILYVIKFDSLEEAIAIN 399
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
24-421 |
7.28e-36 |
|
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: 140.76 E-value: 7.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFASGSL-DVAAAIAYGRE-VGGPALRALTFHQRAGALKALGKLLMSRKEEFYP-SSTATGATAKDSGID 100
Cdd:cd07114 2 INPATGEPWARVPEASAaDVDRAVAAARAaFEGGAWRKLTPTERGKLLRRLADLIEANAEELAElETRDNGKLIRETRAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 101 IDGGIGTLLSYASKGtrelpnDTIylDGGLEPLGRGGTFVgqhiYTSR-P-GVAVQINAFNFPVWGMLEKLAPAFLAGVP 178
Cdd:cd07114 82 VRYLAEWYRYYAGLA------DKI--EGAVIPVDKGDYLN----FTRRePlGVVAAITPWNSPLLLLAKKLAPALAAGNT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 179 SIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLC----ASPRALLDHLDgQDTVLFTGSASTASKLrgHPNVVEGGVRF 254
Cdd:cd07114 150 VVLKPSEHTPASTLELAKLAEEAGF-PPGVVNVVTgfgpETGEALVEHPL-VAKIAFTGGTETGRHI--ARAAAENLAPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 255 NAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVR 334
Cdd:cd07114 226 TLELGGKSPNIVFDDA-----DLDAAVNGVVAGIFAAAGQTCVAGSRLLVQRSIYDEFVERLVARARAIRVGDPLDPETQ 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 335 MGPLASLDQREEVLRSLK-SLRDSATVVFGDPDdfsVEGADASSGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIGYSD 413
Cdd:cd07114 301 MGPLATERQLEKVERYVArAREEGARVLTGGER---PSGADLGAGYFFEPTIL-ADVTNDMRIAQEEVFGPVLSVIPFDD 376
|
....*...
gi 1816981345 414 VDDAIQLA 421
Cdd:cd07114 377 EEEAIALA 384
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
24-446 |
6.03e-35 |
|
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: 138.25 E-value: 6.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFASGSL-DVAAAIAYGRE-------VGGPALRALTFHQRAGALKA----LGKLLmsrkeefypsSTATG 91
Cdd:cd07120 2 IDPATGEVIGTYADGGVaEAEAAIAAARRafdetdwAHDPRLRARVLLELADAFEAnaerLARLL----------ALENG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 92 ATAKDSGIDIDGGIGTLLSYASKgTRELPNDTIyldgGLEPlGRGGTFVGQHIytsrpGVAVQINAFNFPVWGMLEKLAP 171
Cdd:cd07120 72 KILGEARFEISGAISELRYYAGL-ARTEAGRMI----EPEP-GSFSLVLREPM-----GVAGIIVPWNSPVVLLVRSLAP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 172 AFLAGVPSIVKPAHQTAYLTELVVRAIVESGLLPEGSIQLLCASPRALLDHLDGQ---DTVLFTGSASTASKLR--GHPN 246
Cdd:cd07120 141 ALAAGCTVVVKPAGQTAQINAAIIRILAEIPSLPAGVVNLFTESGSEGAAHLVASpdvDVISFTGSTATGRAIMaaAAPT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 247 VveggVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVG 326
Cdd:cd07120 221 L----KRLGLELGGKTPCIVFDDA-----DLDAALPKLERALTIFAGQFCMAGSRVLVQRSIADEVRDRLAARLAAVKVG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 327 HPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVF--GDPDDfsvegaDASSGAFLPPLLLRAQDSAAAAIHEvEAFG 403
Cdd:cd07120 292 PGLDPASDMGPLIDRANVDRVDRMVErAIAAGAEVVLrgGPVTE------GLAKGAFLRPTLLEVDDPDADIVQE-EIFG 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1816981345 404 PISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPA----VARQVTLG 446
Cdd:cd07120 365 PVLTLETFDDEAEAVALANDTDYGLAASVWTRDLAramrVARAIRAG 411
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
21-421 |
1.77e-34 |
|
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: 136.96 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 21 IPLINASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYPS-STATGATAKDSG 98
Cdd:cd07149 1 IEVISPYDGEVIGRVPVASEeDVEKAIAAAKE-GAKEMKSLPAYERAEILERAAQLLEERREEFARTiALEAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 99 IDIDGGIGTLlSYASKGTRELPNDTIYLDGGLEPLGRGGtfvgqhiYTSR-P-GVAVQINAFNFPVWGMLEKLAPAFLAG 176
Cdd:cd07149 80 KEVDRAIETL-RLSAEEAKRLAGETIPFDASPGGEGRIG-------FTIRePiGVVAAITPFNFPLNLVAHKVGPAIAAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 177 VPSIVKPAHQTAYLTELVVRAIVESGlLPEGSIQLLCASP----RALLDHLDGQdTVLFTGSASTASKLRGhpnvvEGGV 252
Cdd:cd07149 152 NAVVLKPASQTPLSALKLAELLLEAG-LPKGALNVVTGSGetvgDALVTDPRVR-MISFTGSPAVGEAIAR-----KAGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 253 RFNA-EADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAE 331
Cdd:cd07149 225 KKVTlELGSNAAVIVDADA-----DLEKAVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 332 GVRMGPLASLDQREEVLRSLK-SLRDSATVVFGDPDDfsvegadassGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIG 410
Cdd:cd07149 300 DTDVGPMISEAEAERIEEWVEeAVEGGARLLTGGKRD----------GAILEPTVLTDVPPDMKVVCE-EVFAPVVSLNP 368
|
410
....*....|.
gi 1816981345 411 YSDVDDAIQLA 421
Cdd:cd07149 369 FDTLDEAIAMA 379
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
24-446 |
2.55e-34 |
|
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: 136.60 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFASGSL-DVAAAIAYGREV--GGPAlrALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGAT-AKDSG 98
Cdd:cd07089 2 INPATEEVIGTAPDAGAaDVDAAIAAARRAfdTGDW--STDAEERARCLRQLHEALEARKEELRALLVAeVGAPvMTARA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 99 IDIDGGIGTLLSYASKGTRELpnDTIYLDGGLEPLGRGGTFVGQHIYtsrpGVAVQINAFNFPVWGMLEKLAPAFLAGVP 178
Cdd:cd07089 80 MQVDGPIGHLRYFADLADSFP--WEFDLPVPALRGGPGRRVVRREPV----GVVAAITPWNFPFFLNLAKLAPALAAGNT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 179 SIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHLD---GQDTVLFTGS--------ASTASKLRghPNV 247
Cdd:cd07089 154 VVLKPAPDTPLSALLLGEIIAETDL-PAGVVNVVTGSDNAVGEALTtdpRVDMVSFTGStavgrrimAQAAATLK--RVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 248 VE-GGvrfnaeaDSLNcsILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVG 326
Cdd:cd07089 231 LElGG-------KSAN--IVLDDA-----DLAAAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 327 HPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFG--DPDDFSVegadassGAFLPPLLLRAQDSaAAAIHEVEAFG 403
Cdd:cd07089 297 DPADPGTVMGPLISAAQRDRVEGYIARGRDEgARLVTGggRPAGLDK-------GFYVEPTLFADVDN-DMRIAQEEIFG 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1816981345 404 PISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDP----AVARQVTLG 446
Cdd:cd07089 369 PVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVdrayRVARRIRTG 415
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
24-443 |
2.65e-34 |
|
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: 136.33 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYP-SSTATGATAKDSGIDI 101
Cdd:cd07110 2 INPATEATIGEIPAATAeDVDAAVRAARR-AFPRWKKTTGAERAKYLRAIAEGVRERREELAElEARDNGKPLDEAAWDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 102 DGGIGTLLSYASKGTRelpndtiyLDGGLE---PLGRGGtfVGQHIYTSRPGVAVQINAFNFPVWGMLEKLAPAFLAGVP 178
Cdd:cd07110 81 DDVAGCFEYYADLAEQ--------LDAKAEravPLPSED--FKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 179 SIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLC---ASPRALLDHLDGQDTVLFTGSASTASKlrghpnvveggVRFN 255
Cdd:cd07110 151 VVLKPSELTS-LTELELAEIAAEAGLPPGVLNVVTgtgDEAGAPLAAHPGIDKISFTGSTATGSQ-----------VMQA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 256 AEADSLNCSI-LGPDAA---KDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAE 331
Cdd:cd07110 219 AAQDIKPVSLeLGGKSPiivFDDADLEKAVEWAMFGCFWNNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 332 GVRMGPLASLDQREEVLRSLK-SLRDSATVVFGdpddfSVEGADASSGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIG 410
Cdd:cd07110 299 GVRLGPLVSQAQYEKVLSFIArGKEEGARLLCG-----GRRPAHLEKGYFIAPTVF-ADVPTDSRIWREEIFGPVLCVRS 372
|
410 420 430
....*....|....*....|....*....|...
gi 1816981345 411 YSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07110 373 FATEDEAIALANDSEYGLAAAVISRDAERCDRV 405
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
21-440 |
9.13e-34 |
|
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: 134.87 E-value: 9.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 21 IPLINASTGEEVARF-ASGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDSG 98
Cdd:cd07094 1 LDVHNPYDGEVIGKVpADDRADAEEALATARA-GAENRRALPPHERMAILERAADLLKKRAEEFAKIIACeGGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 99 IDIDGGIGTLlSYASKGTRELPNDTIYLDGGLEPLGRGGTFVGQHIytsrpGVAVQINAFNFPVWGMLEKLAPAFLAGVP 178
Cdd:cd07094 80 VEVDRAIDTL-RLAAEEAERIRGEEIPLDATQGSDNRLAWTIREPV-----GVVLAITPFNFPLNLVAHKLAPAIATGCP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 179 SIVKPAHQTAYLTELVVRAIVESGlLPEGSIQLLCASPRALLDHL---DGQDTVLFTGSASTASKLRGHpnvvEGGVRFN 255
Cdd:cd07094 154 VVLKPASKTPLSALELAKILVEAG-VPEGVLQVVTGEREVLGDAFaadERVAMLSFTGSAAVGEALRAN----AGGKRIA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 256 AEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRM 335
Cdd:cd07094 229 LELGGNAPVIVDRDA-----DLDAAIEALAKGGFYHAGQVCISVQRIYVHEELYDEFIEAFVAAVKKLKVGDPLDEDTDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 336 GPLASLDQREEVLRSL-KSLRDSATVVFGDPDDfsvegadassGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDV 414
Cdd:cd07094 304 GPLISEEAAERVERWVeEAVEAGARLLCGGERD----------GALFKPTVLEDVPRDTKLSTE-ETFGPVVPIIRYDDF 372
|
410 420
....*....|....*....|....*.
gi 1816981345 415 DDAIQLAARGKGSLVGSLVTHDPAVA 440
Cdd:cd07094 373 EEAIRIANSTDYGLQAGIFTRDLNVA 398
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
24-443 |
3.47e-33 |
|
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: 132.94 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFASGSL-DVAAAIAYGrEVGGPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDSGIDI 101
Cdd:cd07103 2 INPATGEVIGEVPDAGAaDADAAIDAA-AAAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLeQGKPLAEARGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 102 DGGIGTLLSYASKGTRelpndtIYldGGLEPLGRGGTfvgQHIYTSRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSI 180
Cdd:cd07103 81 DYAASFLEWFAEEARR------IY--GRTIPSPAPGK---RILVIKQPvGVVAAITPWNFPAAMITRKIAPALAAGCTVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 181 VKPAHQTAYLTELVVRAIVESGlLPEGSIQLLCASPRALLDHLDGQDTV---LFTGS-----------ASTASK----LR 242
Cdd:cd07103 150 LKPAEETPLSALALAELAEEAG-LPAGVLNVVTGSPAEIGEALCASPRVrkiSFTGStavgkllmaqaADTVKRvsleLG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 243 GH-PNVVeggvrFnAEADslncsilgPDAAkdtpefelyIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLS 321
Cdd:cd07103 229 GNaPFIV-----F-DDAD--------LDKA---------VDGAIASKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVK 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 322 KVVVGHPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGDpddfsveGADASSGAFLPPLLLRAQDSAAAAIHEvE 400
Cdd:cd07103 286 KLKVGNGLDEGTDMGPLINERAVEKVEALVEdAVAKGAKVLTGG-------KRLGLGGYFYEPTVLTDVTDDMLIMNE-E 357
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1816981345 401 AFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07103 358 TFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRV 400
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
21-443 |
1.12e-32 |
|
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: 131.33 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 21 IPLINASTGE---EVARFASGSLDVAAAIAYGREvggpalRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKD 96
Cdd:cd07146 1 LEVRNPYTGEvvgTVPAGTEEALREALALAASYR------STLTRYQRSAILNKAAALLEARREEFARLITLeSGLCLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 97 SGIDIDGGIGTLLSYASKGTRElpndtiylDGGLEPLGRGGTFVGQHIYTSRP--GVAVQINAFNFPVWGMLEKLAPAFL 174
Cdd:cd07146 75 TRYEVGRAADVLRFAAAEALRD--------DGESFSCDLTANGKARKIFTLREplGVVLAITPFNHPLNQVAHKIAPAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 175 AGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHL--DGQ-DTVLFTGSASTASKLRGhpnvVEGG 251
Cdd:cd07146 147 ANNRIVLKPSEKTPLSAIYLADLLYEAGL-PPDMLSVVTGEPGEIGDELitHPDvDLVTFTGGVAVGKAIAA----TAGY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 252 VRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAE 331
Cdd:cd07146 222 KRQLLELGGNDPLIVMDDA-----DLERAATLAVAGSYANSGQRCTAVKRILVHESVADEFVDLLVEKSAALVVGDPMDP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 332 GVRMGPLASLDQREEV-LRSLKSLRDSATVVFGDPDDfsvegadassGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIG 410
Cdd:cd07146 297 ATDMGTVIDEEAAIQIeNRVEEAIAQGARVLLGNQRQ----------GALYAPTVLDHVPPDAELVTE-ETFGPVAPVIR 365
|
410 420 430
....*....|....*....|....*....|...
gi 1816981345 411 YSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07146 366 VKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRL 398
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
24-443 |
2.78e-30 |
|
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: 124.18 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFASGSLD-----VAAAIAygrevGGPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDS 97
Cdd:cd07106 2 INPATGEVFASAPVASEAqldqaVAAAKA-----AFPGWSATPLEERRAALLAIADAIEANAEELARLLTLeQGKPLAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 98 GIDIDGGIGTLLSYASkgtRELPNDTIYLDggleplgRGGTFVGQHiytsRP-GVAVQINAFNFPVWGMLEKLAPAFLAG 176
Cdd:cd07106 77 QFEVGGAVAWLRYTAS---LDLPDEVIEDD-------DTRRVELRR----KPlGVVAAIVPWNFPLLLAAWKIAPALLAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 177 VPSIVKPAHQTAYLTELVVRAIVEsgLLPEGSIQLLCASPR---ALLDHlDGQDTVLFTGSASTASKlrghpnVVEggvr 253
Cdd:cd07106 143 NTVVLKPSPFTPLCTLKLGELAQE--VLPPGVLNVVSGGDElgpALTSH-PDIRKISFTGSTATGKK------VMA---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 254 fnAEADSL----------NCSILGPDAakDTPEFelyIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKV 323
Cdd:cd07106 210 --SAAKTLkrvtlelggnDAAIVLPDV--DIDAV---APKLFWGAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 324 VVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVF-GDPDDfsvegadaSSGAFLPPLLLRAQDSAAAAIHEvEA 401
Cdd:cd07106 283 VVGDGLDPGTTLGPVQNKMQYDKVKELVEDAKAKgAKVLAgGEPLD--------GPGYFIPPTIVDDPPEGSRIVDE-EQ 353
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1816981345 402 FGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07106 354 FGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAV 395
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
7-436 |
4.73e-30 |
|
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: 124.00 E-value: 4.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 7 SYVSGKWIAPE-GESIPLINASTGEE-VARF-ASGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEF 83
Cdd:cd07131 1 NYIGGEWVDSAsGETFDSRNPADLEEvVGTFpLSTASDVDAAVEAARE-AFPEWRKVPAPRRAEYLFRAAELLKKRKEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 YPSST-ATGATAKDSGIDIDGGIGTLLSYASKGTR--------ELPNDTIYldggleplgrggTFvgqhiytSRP-GVAV 153
Cdd:cd07131 80 ARLVTrEMGKPLAEGRGDVQEAIDMAQYAAGEGRRlfgetvpsELPNKDAM------------TR-------RQPiGVVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 154 QINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLC----ASPRALLDHLDgQDTV 229
Cdd:cd07131 141 LITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAGL-PPGVVNVVHgrgeEVGEALVEHPD-VDVV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 230 LFTGSASTASKlrghpnVVEGGVRFN----AEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVP 305
Cdd:cd07131 219 SFTGSTEVGER------IGETCARPNkrvaLEMGGKNPIIVMDDA-----DLDLALEGALWSAFGTTGQRCTATSRLIVH 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 306 NELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPDDFSVEGADAssGAFLPPLL 385
Cdd:cd07131 288 ESVYDEFLKRFVERAKRLRVGDGLDEETDMGPLINEAQLEKVLNYNEIGKEEGATLLLGGERLTGGGYEK--GYFVEPTV 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1816981345 386 LRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07131 366 FTDVTPDMRIAQE-EIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTED 415
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
23-444 |
6.96e-30 |
|
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: 123.21 E-value: 6.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 23 LINASTGEEVARF-ASGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TG----ATAKD 96
Cdd:cd07092 1 VVDPATGEEIATVpDASAADVDAAVAAAHA-AFPSWRRTTPAERSKALLKLADAIEENAEELAALESRnTGkplhLVRDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 97 sgiDIDGGIGTLLSYASkGTRELPNdtiyldggleplGRGGTFVGQHIYTSR--P-GVAVQINAFNFPVWGMLEKLAPAF 173
Cdd:cd07092 80 ---ELPGAVDNFRFFAG-AARTLEG------------PAAGEYLPGHTSMIRrePiGVVAQIAPWNYPLMMAAWKIAPAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 174 LAGVPSIVKPAHQTAyLTELVVRAIVESGLlPEGSIQLLC----ASPRALLDHLDgQDTVLFTGSASTASKL-------- 241
Cdd:cd07092 144 AAGNTVVLKPSETTP-LTTLLLAELAAEVL-PPGVVNVVCgggaSAGDALVAHPR-VRMVSLTGSVRTGKKVaraaadtl 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 242 -RGH-------PNVVEGGVRFNAEADSLNcsilgpdaakdtpEFELYikqlvaemttKAGQKCTAIRRALVPNELVDDVV 313
Cdd:cd07092 221 kRVHlelggkaPVIVFDDADLDAAVAGIA-------------TAGYY----------NAGQDCTAACRVYVHESVYDEFV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 314 EATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGdpddfsveGADAS-SGAFLPPLLLRAQDSA 392
Cdd:cd07092 278 AALVEAVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVERAPAHARVLTG--------GRRAEgPGYFYEPTVVAGVAQD 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1816981345 393 AAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07092 350 DEIVQE-EIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLS 400
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
21-436 |
1.76e-29 |
|
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: 122.07 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 21 IPLINASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDSG 98
Cdd:cd07145 1 IEVRNPANGEVIDTVPSLSReEVREAIEVAEK-AKDVMSNLPAYKRYKILMKVAELIERRKEELAKLLTIeVGKPIKQSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 99 IDIDGGIgTLLSYASKGTRELPNDTIYLDGGLEPLGRggtfvgqHIYTSR-P-GVAVQINAFNFPVWGMLEKLAPAFLAG 176
Cdd:cd07145 80 VEVERTI-RLFKLAAEEAKVLRGETIPVDAYEYNERR-------IAFTVRePiGVVGAITPFNFPANLFAHKIAPAIAVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 177 VPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCASPRALLDHLDGQDTV---LFTGSASTASKLRGhpNVVEGGVR 253
Cdd:cd07145 152 NSVVVKPSSNTP-LTAIELAKILEEAGLPPGVINVVTGYGSEVGDEIVTNPKVnmiSFTGSTAVGLLIAS--KAGGTGKK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 254 FNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGV 333
Cdd:cd07145 229 VALELGGSDPMIVLKDA-----DLERAVSIAVRGRFENAGQVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPLDEST 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 334 RMGPLASLDQREEVLRSL-KSLRDSATVVFGdpddfsVEGADassGAFLPPLLLRAqDSAAAAIHEVEAFGPISTVIGYS 412
Cdd:cd07145 304 DLGPLISPEAVERMENLVnDAVEKGGKILYG------GKRDE---GSFFPPTVLEN-DTPDMIVMKEEVFGPVLPIAKVK 373
|
410 420
....*....|....*....|....
gi 1816981345 413 DVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07145 374 DDEEAVEIANSTEYGLQASVFTND 397
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
8-456 |
2.59e-29 |
|
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: 122.07 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPE-GESIPLINASTGEEVARFA-SGSLDVAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEFyp 85
Cdd:cd07559 4 FINGEWVAPSkGEYFDNYNPVNGKVLCEIPrSTAEDVDLAVDAAHEAF-KTWGKTSVAERANILNKIADRIEENLELL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 sstatgATAK--DSG--------IDIDGGIGTLLSYAS-----KGT-RELPNDTIYLDGGlEPLGrggtfvgqhiytsrp 149
Cdd:cd07559 81 ------AVAEtlDNGkpiretlaADIPLAIDHFRYFAGviraqEGSlSEIDEDTLSYHFH-EPLG--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 gVAVQINAFNFP----VWgmleKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESgLLPEGSIQLLCA----SPRALLD 221
Cdd:cd07559 139 -VVGQIIPWNFPllmaAW----KLAPALAAGNTVVLKPASQTP-LSILVLMELIGD-LLPKGVVNVVTGfgseAGKPLAS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 222 HlDGQDTVLFTGSAST-------ASKlRGHPNVVE-GGVRFNaeadslncsILGPDAAKDTPEFELYIKQLVAEMTTKAG 293
Cdd:cd07559 212 H-PRIAKLAFTGSTTVgrlimqyAAE-NLIPVTLElGGKSPN---------IFFDDAMDADDDFDDKAEEGQLGFAFNQG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 294 QKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPDDFSVEGA 373
Cdd:cd07559 281 EVCTCPSRALVQESIYDEFIERAVERFEAIKVGNPLDPETMMGAQVSKDQLEKILSYVDIGKEEGAEVLTGGERLTLGGL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 374 DAssGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGVAPfhGR 453
Cdd:cd07559 361 DK--GYFYEPTLIKGGNNDMRIFQE-EIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDINRALRVARGIQT--GR 435
|
...
gi 1816981345 454 ILI 456
Cdd:cd07559 436 VWV 438
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
23-447 |
7.08e-29 |
|
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: 120.17 E-value: 7.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 23 LINASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEF-YPSSTATGATAKDSGID 100
Cdd:cd07107 1 VINPATGQVLARVPAASAaDVDRAVAAARA-AFPEWRATTPLERARMLRELATRLREHAEELaLIDALDCGNPVSAMLGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 101 IDGGIGTLLSYASKGTrELPNDTIYLDGGleplgrggtfvGQHIYTSRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPS 179
Cdd:cd07107 80 VMVAAALLDYFAGLVT-ELKGETIPVGGR-----------NLHYTLREPyGVVARIVAFNHPLMFAAAKIAAPLAAGNTV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 180 IVKPAHQTAyLTELVVRAIVEsGLLPEGSIQLLCASPR----ALLDHLDgQDTVLFTGSASTASK-LRGhpnVVEGGVRF 254
Cdd:cd07107 148 VVKPPEQAP-LSALRLAELAR-EVLPPGVFNILPGDGAtagaALVRHPD-VKRIALIGSVPTGRAiMRA---AAEGIKHV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 255 NAEADSLNCSILGPDAakdtpEFELYIKQLVAEMT-TKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGV 333
Cdd:cd07107 222 TLELGGKNALIVFPDA-----DPEAAADAAVAGMNfTWCGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPTDPAT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 334 RMGPLASLDQREEVLRSLKS-LRDSATVVFGD--PddfsvEGADASSGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIG 410
Cdd:cd07107 297 TMGPLVSRQQYDRVMHYIDSaKREGARLVTGGgrP-----EGPALEGGFYVEPTVF-ADVTPGMRIAREEIFGPVLSVLR 370
|
410 420 430
....*....|....*....|....*....|....*..
gi 1816981345 411 YSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGV 447
Cdd:cd07107 371 WRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRV 407
|
|
| R_hydratase_like |
cd03441 |
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ... |
548-672 |
2.60e-28 |
|
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.
Pssm-ID: 239525 [Multi-domain] Cd Length: 127 Bit Score: 110.05 E-value: 2.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 548 GPRVVSLEDIDHFAEFTGDTFYAHTDPKAAAENPlFGGIVAHGYLVVSLAAGLFVEPNPGPVLANFGVDGLRFLTPVKAG 627
Cdd:cd03441 6 SGRTVTEADIALFARLSGDPNPIHVDPEYAKAAG-FGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLAPVFPG 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1816981345 628 DALTVTLTAKQVTPrlSADYGEVRWDAVVANQNDDPVATYDVLTL 672
Cdd:cd03441 85 DTLRVEVEVLGKRP--SKGRGVVTVRTEARNQGGEVVLSGEATVL 127
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
21-436 |
5.51e-28 |
|
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: 117.73 E-value: 5.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 21 IPLINASTGEEVAR-FASGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDSG 98
Cdd:cd07147 1 LEVTNPYTGEVVARvALAGPDDIEEAIAAAVK-AFRPMRALPAHRRAAILLHCVARLEERFEELAETIVLeAGKPIKDAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 99 IDIDGGIGTLLSYASKGTRelpNDTIYLDGGLEPLGRGgtFVGqhiYTSR-P-GVAVQINAFNFPVWGMLEKLAPAFLAG 176
Cdd:cd07147 80 GEVARAIDTFRIAAEEATR---IYGEVLPLDISARGEG--RQG---LVRRfPiGPVSAITPFNFPLNLVAHKVAPAIAAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 177 VPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLL-CASPRALLDHLDGQDTVL-FTGSASTASKLR---GHPNVV-E- 249
Cdd:cd07147 152 CPFVLKPASRTP-LSALILGEVLAETGLPKGAFSVLpCSRDDADLLVTDERIKLLsFTGSPAVGWDLKaraGKKKVVlEl 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 250 GGvrfNAEAdslncsILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPN 329
Cdd:cd07147 231 GG---NAAV------IVDSDA-----DLDFAAQRIIFGAFYQAGQSCISVQRVLVHRSVYDEFKSRLVARVKALKTGDPK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 330 AEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDPDDfsvegadassGAFLPPLLLrAQDSAAAAIHEVEAFGPISTV 408
Cdd:cd07147 297 DDATDVGPMISESEAERVEGWVNEAVDAgAKLLTGGKRD----------GALLEPTIL-EDVPPDMEVNCEEVFGPVVTV 365
|
410 420
....*....|....*....|....*...
gi 1816981345 409 IGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07147 366 EPYDDFDEALAAVNDSKFGLQAGVFTRD 393
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
8-421 |
1.10e-27 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 116.93 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPEGESIPLINASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEF-YP 85
Cdd:PRK13473 6 LINGELVAGEGEKQPVYNPATGEVLAEIAEASAaQVDAAVAAADA-AFPEWSQTTPKERAEALLKLADAIEENADEFaRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 SSTATG----ATAKDsgiDIDGGIGTLLSYASkGTRELPndtiyldgGLeplgRGGTFVGQHIYTSR--P-GVAVQINAF 158
Cdd:PRK13473 85 ESLNCGkplhLALND---EIPAIVDVFRFFAG-AARCLE--------GK----AAGEYLEGHTSMIRrdPvGVVASIAPW 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 159 NFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVEsgLLPEGSIQLLCASPR----ALLDHlDGQDTVLFTGS 234
Cdd:PRK13473 149 NYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAAD--ILPPGVLNVVTGRGAtvgdALVGH-PKVRMVSLTGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 235 ASTASKL---------RGH-------PNVVeggvrFNaEADslncsilgPDAAkdtpefelyIKQLVAEMTTKAGQKCTA 298
Cdd:PRK13473 226 IATGKHVlsaaadsvkRTHlelggkaPVIV-----FD-DAD--------LDAV---------VEGIRTFGYYNAGQDCTA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 299 IRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRD--SATVVFGdpddfsveGADAS 376
Cdd:PRK13473 283 ACRIYAQRGIYDDLVAKLAAAVATLKVGDPDDEDTELGPLISAAHRDRVAGFVERAKAlgHIRVVTG--------GEAPD 354
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1816981345 377 -SGAFLPPLLLR--AQDSaaaAIHEVEAFGPISTVIGYSDVDDAIQLA 421
Cdd:PRK13473 355 gKGYYYEPTLLAgaRQDD---EIVQREVFGPVVSVTPFDDEDQAVRWA 399
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
43-443 |
1.17e-27 |
|
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: 116.41 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 43 AAAIAYgrevggPALRALTFHQRAGALKALGKLLMSRKEEFypSSTAT---GATAKDSGIDIDGGIGTLLSYASKGTREL 119
Cdd:cd07100 7 RAHAAF------LAWRKTSFAERAALLRKLADLLRERKDEL--ARLITlemGKPIAEARAEVEKCAWICRYYAENAEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 120 PNDTIYLDGGleplgrggtfvgQHIYTSRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAI 198
Cdd:cd07100 79 ADEPIETDAG------------KAYVRYEPlGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 199 VESGLlPEGSIQLLCASPR---ALLDH--LDGqdtVLFTGS-------ASTASK-LRghPNVVE-GGvrfnaeADSLncs 264
Cdd:cd07100 147 REAGF-PEGVFQNLLIDSDqveAIIADprVRG---VTLTGSeragravAAEAGKnLK--KSVLElGG------SDPF--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 265 ILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQR 344
Cdd:cd07100 212 IVLDDA-----DLDKAVKTAVKGRLQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPMDEDTDLGPLARKDLR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 345 EEVLRSL-KSLRDSATVVFGDPddfsvegADASSGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAAR 423
Cdd:cd07100 287 DELHEQVeEAVAAGATLLLGGK-------RPDGPGAFYPPTVLTDVTPGMPAYDE-ELFGPVAAVIKVKDEEEAIALAND 358
|
410 420
....*....|....*....|
gi 1816981345 424 GKGSLVGSLVTHDPAVARQV 443
Cdd:cd07100 359 SPFGLGGSVFTTDLERAERV 378
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
8-438 |
1.51e-27 |
|
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: 116.94 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIaPEGESIPLIN-ASTGEEVARFASGSLDVA-AAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFyp 85
Cdd:cd07124 36 VIGGKEV-RTEEKIESRNpADPSEVLGTVQKATKEEAeAAVQAARA-AFPTWRRTPPEERARLLLRAAALLRRRRFEL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 SSTATGATAK---DSGIDIDGGIGTLLSYAskgtRELpndtIYLDGglEPLGRGGTFVGQHIYTSRpGVAVQINAFNFPV 162
Cdd:cd07124 112 AAWMVLEVGKnwaEADADVAEAIDFLEYYA----REM----LRLRG--FPVEMVPGEDNRYVYRPL-GVGAVISPWNFPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 163 WGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASP----RALLDHLDgQDTVLFTGSasta 238
Cdd:cd07124 181 AILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAGL-PPGVVNFLPGPGeevgDYLVEHPD-VRFIAFTGS---- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 239 sklrghpnvVEGGVRFNAEAdslncsilgpdaAKDTPEfELYIKQLVAEMTTK-------------------------AG 293
Cdd:cd07124 255 ---------REVGLRIYERA------------AKVQPG-QKWLKRVIAEMGGKnaiivdedadldeaaegivrsafgfQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 294 QKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPDDfsvegA 373
Cdd:cd07124 313 QKCSACSRVIVHESVYDEFLERLVERTKALKVGDPEDPEVYMGPVIDKGARDRIRRYIEIGKSEGRLLLGGEVL-----E 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816981345 374 DASSGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPA 438
Cdd:cd07124 388 LAAEGYFVQPTIF-ADVPPDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPE 451
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
41-442 |
1.98e-27 |
|
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: 115.45 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 41 DVAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEFYPS----------STATGATAKDSGIDIdggigTLLS 110
Cdd:cd07095 1 QVDAAVAAARAAF-PGWAALSLEERAAILRRFAELLKANKEELARLisretgkplwEAQTEVAAMAGKIDI-----SIKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 111 YASK-GTRELPNDtiyldggleplgrGGTFVGQHiytsRP-GVAVQINAFNFPvwGMLEK--LAPAFLAGVPSIVKPAHQ 186
Cdd:cd07095 75 YHERtGERATPMA-------------QGRAVLRH----RPhGVMAVFGPFNFP--GHLPNghIVPALLAGNTVVFKPSEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 187 TAYLTELVVRAIVESGlLPEGSIQLL---CASPRALLDHlDGQDTVLFTGSASTASKLR----GHPNVV----EGGvrfN 255
Cdd:cd07095 136 TPAVAELMVELWEEAG-LPPGVLNLVqggRETGEALAAH-EGIDGLLFTGSAATGLLLHrqfaGRPGKIlaleMGG---N 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 256 aeadslNCSILGPDAAKDTpefELYIKQLVAEMTtkAGQKCTAIRRALVPNELV-DDVVEATRTRLSKVVVGHPNAEGVR 334
Cdd:cd07095 211 ------NPLVVWDVADIDA---AAYLIVQSAFLT--AGQRCTCARRLIVPDGAVgDAFLERLVEAAKRLRIGAPDAEPPF 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 335 MGPLASLDQREEVLRSlkslrdsatvvfgdPDDFSVEGADAS--------SGAFLPPLLLraQDSAAAAIHEVEAFGPIS 406
Cdd:cd07095 280 MGPLIIAAAAARYLLA--------------QQDLLALGGEPLlamerlvaGTAFLSPGII--DVTDAADVPDEEIFGPLL 343
|
410 420 430
....*....|....*....|....*....|....*.
gi 1816981345 407 TVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQ 442
Cdd:cd07095 344 QVYRYDDFDEAIALANATRFGLSAGLLSDDEALFER 379
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
8-444 |
7.46e-27 |
|
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: 114.51 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWI-APEGESIPLINASTGEEVARFASG-SLDVAAAIAYGREV--GGPALRaLTFHQRAGALKALGKLLMSRKEEF 83
Cdd:cd07142 7 FINGQFVdAASGKTFPTIDPRNGEVIAHVAEGdAEDVDRAVKAARKAfdEGPWPR-MTGYERSRILLRFADLLEKHADEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 YPSSTATGATAKDSG--IDIDGGIGTLLSYASKGTReLPNDTIYLDGGLeplgrggtfvgqHIYT-SRP-GVAVQINAFN 159
Cdd:cd07142 86 AALETWDNGKPYEQAryAEVPLAARLFRYYAGWADK-IHGMTLPADGPH------------HVYTlHEPiGVVGQIIPWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 160 FPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGlLPEGSIQLLCA----SPRALLDHLDgQDTVLFTGSA 235
Cdd:cd07142 153 FPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAG-LPDGVLNIVTGfgptAGAAIASHMD-VDKVAFTGST 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 236 STASKlrghpnVVEGGVRFNAEADSLN---------CSILGPDAAKDTPEFELYIKQlvaemttkaGQKCTAIRRALVPN 306
Cdd:cd07142 231 EVGKI------IMQLAAKSNLKPVTLElggkspfivCEDADVDKAVELAHFALFFNQ---------GQCCCAGSRTFVHE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 307 ELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDpddfsveGADASSGAFLPPLL 385
Cdd:cd07142 296 SIYDEFVEKAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKEEgATLITGG-------DRIGSKGYYIQPTI 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 386 LR-AQDSAAAAIHEVeaFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07142 369 FSdVKDDMKIARDEI--FGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTANTLS 426
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
8-438 |
9.64e-27 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 114.29 E-value: 9.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPEGESIPLINASTGEEV--ARFASGSlDVAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEFYP 85
Cdd:PRK09457 4 WINGDWIAGQGEAFESRNPVSGEVLwqGNDATAA-QVDAAVRAARAAF-PAWARLSFEERQAIVERFAALLEENKEELAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 S----------STATGATAKDSGIDIdggigTLLSYASK-GTRElpndtiyldgglEPLGrGGTFVGQHiytsRP-GVAV 153
Cdd:PRK09457 82 ViaretgkplwEAATEVTAMINKIAI-----SIQAYHERtGEKR------------SEMA-DGAAVLRH----RPhGVVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 154 QINAFNFPvwGMLEK--LAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASP---RALLDHlDGQDT 228
Cdd:PRK09457 140 VFGPYNFP--GHLPNghIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAGL-PAGVLNLVQGGRetgKALAAH-PDIDG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 229 VLFTGSASTASKLR----GHPNVV----EGGvrfNaeadslncsilGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIR 300
Cdd:PRK09457 216 LLFTGSANTGYLLHrqfaGQPEKIlaleMGG---N-----------NPLVIDEVADIDAAVHLIIQSAFISAGQRCTCAR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 301 RALVPN-----ELVDDVVEATrtrlSKVVVGHPNAEGVR-MGPLASLDQREEVLRSLKSLRDSATVVFgdpddfsVEGAD 374
Cdd:PRK09457 282 RLLVPQgaqgdAFLARLVAVA----KRLTVGRWDAEPQPfMGAVISEQAAQGLVAAQAQLLALGGKSL-------LEMTQ 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816981345 375 ASSG-AFLPPLLLRAqdSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPA 438
Cdd:PRK09457 351 LQAGtGLLTPGIIDV--TGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDRE 413
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
23-443 |
1.23e-26 |
|
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: 113.48 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 23 LINASTGEEVARFASGSL-DVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRKEEFYP-SSTATGATAKDSGID 100
Cdd:cd07109 1 VFDPSTGEVFARIARGGAaDVDRAVQAARRAFESGWLRLSPAERGRLLLRIARLIREHADELARlESLDTGKPLTQARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 101 IDGGIGTLLSYASKGTReLPNDTIyldgglePLGRGgtfvgQHIYTSRP--GVAVQINAFNFPVWGMLEKLAPAFLAGVP 178
Cdd:cd07109 81 VEAAARYFEYYGGAADK-LHGETI-------PLGPG-----YFVYTVREphGVTGHIIPWNYPLQITGRSVAPALAAGNA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 179 SIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLC----ASPRALLDHlDGQDTVLFTGSAST------ASKLRGHPNVV 248
Cdd:cd07109 148 VVVKPAEDAPLTALRLAELAEEAGL-PAGALNVVTglgaEAGAALVAH-PGVDHISFTGSVETgiavmrAAAENVVPVTL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 249 E-GGvrfnaeaDSLNcsILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGH 327
Cdd:cd07109 226 ElGG-------KSPQ--IVFADA-----DLEAALPVVVNAIIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 328 PnAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDpddfSVEGADASSGAFLPPLLLRAQDSAAAAIHEvEAFGPIS 406
Cdd:cd07109 292 G-LEDPDLGPLISAKQLDRVEGFVARARARgARIVAGG----RIAEGAPAGGYFVAPTLLDDVPPDSRLAQE-EIFGPVL 365
|
410 420 430
....*....|....*....|....*....|....*..
gi 1816981345 407 TVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07109 366 AVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRV 402
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
8-436 |
1.39e-26 |
|
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: 113.69 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPEGESIP-LINASTGEEVARFASGS-LDVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRKEEFYP 85
Cdd:cd07113 3 FIDGRPVAGQSEKRLdITNPATEQVIASVASATeADVDAAVASAWRAFVSAWAKTTPAERGRILLRLADLIEQHGEELAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 SSTA-TGATAKDS-GIDIDGGIGTLLSYASKGTReLPNDTIYLDgglEPLGRGGTFVGqhiYTSRP--GVAVQINAFNFP 161
Cdd:cd07113 83 LETLcSGKSIHLSrAFEVGQSANFLRYFAGWATK-INGETLAPS---IPSMQGERYTA---FTRREpvGVVAGIVPWNFS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 162 VWGMLEKLAPAFLAGVPSIVKPAhQTAYLTELVVRAIVESGLLPEGSIQLLCAS---PRALLDHLDGQdTVLFTGSASTA 238
Cdd:cd07113 156 VMIAVWKIGAALATGCTIVIKPS-EFTPLTLLRVAELAKEAGIPDGVLNVVNGKgavGAQLISHPDVA-KVSFTGSVATG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 239 SKLRghPNVVEGGVRFNAEADSLNCSILGPDAAKDTpefelYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRT 318
Cdd:cd07113 234 KKIG--RQAASDLTRVTLELGGKNAAAFLKDADIDW-----VVEGLLTAGFLHQGQVCAAPERFYVHRSKFDELVTKLKQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 319 RLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLR-DSATVVFGDpddfsveGADASSGAFLPPLLLRAQDSAAAAIH 397
Cdd:cd07113 307 ALSSFQVGSPMDESVMFGPLANQPHFDKVCSYLDDARaEGDEIVRGG-------EALAGEGYFVQPTLVLARSADSRLMR 379
|
410 420 430
....*....|....*....|....*....|....*....
gi 1816981345 398 EvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07113 380 E-ETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNN 417
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
6-444 |
1.70e-26 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 113.63 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 6 ESYVSGKWI-APEGESIPLINASTGEEVARFAS-GSLDVAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEF 83
Cdd:PLN02278 26 QGLIGGKWTdAYDGKTFPVYNPATGEVIANVPCmGRAETNDAIASAHDAF-PSWSKLTASERSKILRRWYDLIIANKEDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 YPSSTA-TGATAKDSGIDIDGGIGTLLSYASKGTRelpndtIYLDGGLEPLGRGGTFVgqhiyTSRP-GVAVQINAFNFP 161
Cdd:PLN02278 105 AQLMTLeQGKPLKEAIGEVAYGASFLEYFAEEAKR------VYGDIIPSPFPDRRLLV-----LKQPvGVVGAITPWNFP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 162 VWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCASPRALLDHLDGQDTV---LFTGSASTA 238
Cdd:PLN02278 174 LAMITRKVGPALAAGCTVVVKPSELTP-LTALAAAELALQAGIPPGVLNVVMGDAPEIGDALLASPKVrkiTFTGSTAVG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 239 SKL-RGHPNVVE------GGvrfNAEadslncSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDD 311
Cdd:PLN02278 253 KKLmAGAAATVKrvslelGG---NAP------FIVFDDA-----DLDVAVKGALASKFRNSGQTCVCANRILVQEGIYDK 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 312 VVEATRTRLSKVVVGHPNAEGVRMGPL---ASLDQREEVLRSlkSLRDSATVVFGdpddfsveGADASSG-AFLPPLLLR 387
Cdd:PLN02278 319 FAEAFSKAVQKLVVGDGFEEGVTQGPLineAAVQKVESHVQD--AVSKGAKVLLG--------GKRHSLGgTFYEPTVLG 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1816981345 388 AQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:PLN02278 389 DVTEDMLIFRE-EVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVS 444
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
24-453 |
1.76e-26 |
|
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: 113.09 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFASGSLD-VAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFY-PSSTATGATAKDSGIDI 101
Cdd:cd07099 1 RNPATGEVLGEVPVTDPAeVAAAVARARA-AQRAWAALGVEGRAQRLLRWKRALADHADELAeLLHAETGKPRADAGLEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 102 DGGIGTLLSYASKGTRELPNdtiyldgglEPLGRGGTFVGQHI---YTSRPGVAVqINAFNFPVWGMLEKLAPAFLAGVP 178
Cdd:cd07099 80 LLALEAIDWAARNAPRVLAP---------RKVPTGLLMPNKKAtveYRPYGVVGV-ISPWNYPLLTPMGDIIPALAAGNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 179 SIVKPAHQTAYLTELVVRAIvESGLLPEGSIQLLC---ASPRALLDHldGQDTVLFTGSASTASKL------RGHPNVVE 249
Cdd:cd07099 150 VVLKPSEVTPLVGELLAEAW-AAAGPPQGVLQVVTgdgATGAALIDA--GVDKVAFTGSVATGRKVmaaaaeRLIPVVLE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 250 GGvrfnaeadslncsilGPDAA--KDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGH 327
Cdd:cd07099 227 LG---------------GKDPMivLADADLERAAAAAVWGAMVNAGQTCISVERVYVHESVYDEFVARLVAKARALRPGA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 328 PNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGdpddfsveGADASSGA-FLPPLLLRAQDSAAAAIHEvEAFGPI 405
Cdd:cd07099 292 DDIGDADIGPMTTARQLDIVRRHVDdAVAKGAKALTG--------GARSNGGGpFYEPTVLTDVPHDMDVMRE-ETFGPV 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1816981345 406 STVIGYSDVDDAIQLAARGKGSLVGSLVTHDP----AVARQVTLGV--------------APFHGR 453
Cdd:cd07099 363 LPVMPVADEDEAIALANDSRYGLSASVFSRDLaraeAIARRLEAGAvsindvlltagipaLPFGGV 428
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
8-444 |
4.73e-26 |
|
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: 112.12 E-value: 4.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAP-EGESIPLINASTGEEVARF-ASGSLDVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRKEefyp 85
Cdd:cd07144 11 FINNEFVKSsDGETIKTVNPSTGEVIASVyAAGEEDVDKAVKAARKAFESWWSKVTGEERGELLDKLADLVEKNRD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 ssTATGATAKDSGI--------DIDGGIgTLLSYASKGTRELPNDTIYLDGGleplgrggtfvgQHIYTSR-P-GVAVQI 155
Cdd:cd07144 87 --LLAAIEALDSGKpyhsnalgDLDEII-AVIRYYAGWADKIQGKTIPTSPN------------KLAYTLHePyGVCGQI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 156 NAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCA----SPRALLDHLDgQDTVLF 231
Cdd:cd07144 152 IPWNYPLAMAAWKLAPALAAGNTVVIKPAENTP-LSLLYFANLVKEAGFPPGVVNIIPGygavAGSALAEHPD-VDKIAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 232 TGSASTASKlrghpnvVEGGVRFNAEADSLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVP----NE 307
Cdd:cd07144 230 TGSTATGRL-------VMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIMYNSGQNCTATSRIYVQesiyDK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 308 LVDDVVEATRTRLSkvvVGHPNAEGVRMGPLASLDQREEVLRSL-KSLRDSATVVFGDpddfSVEGADASSGAFLPPLLL 386
Cdd:cd07144 303 FVEKFVEHVKQNYK---VGSPFDDDTVVGPQVSKTQYDRVLSYIeKGKKEGAKLVYGG----EKAPEGLGKGYFIPPTIF 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816981345 387 rAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07144 376 -TDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVA 432
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
24-447 |
1.37e-25 |
|
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: 110.35 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEF-YPSSTATGATAKD-SGID 100
Cdd:cd07093 2 FNPATGEVLAKVPEGGAaEVDAAVAAAKE-AFPGWSRMSPAERARILHKVADLIEARADELaLLESLDTGKPITLaRTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 101 IDGGIGTLLSYASK----GTRELPNDTIYLDggleplgrggtfvgqhiYTSRP--GVAVQINAFNFPVwgMLE--KLAPA 172
Cdd:cd07093 81 IPRAAANFRFFADYilqlDGESYPQDGGALN-----------------YVLRQpvGVAGLITPWNLPL--MLLtwKIAPA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 173 FLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCAS-PRA---LLDHLDgQDTVLFTGSASTASKLRghPNVV 248
Cdd:cd07093 142 LAFGNTVVLKPSEWTPLTAWLLAELANEAGL-PPGVVNVVHGFgPEAgaaLVAHPD-VDLISFTGETATGRTIM--RAAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 249 EGGVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHP 328
Cdd:cd07093 218 PNLKPVSLELGGKNPNIVFADA-----DLDRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 329 NAEGVRMGPLASLDQREEVLRSLKS-LRDSATVVFGDPDDfsvEGADASSGAFLPPLLLRAQDSAAAAIHEvEAFGPIST 407
Cdd:cd07093 293 LDPDTEVGPLISKEHLEKVLGYVELaRAEGATILTGGGRP---ELPDLEGGYFVEPTVITGLDNDSRVAQE-EIFGPVVT 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1816981345 408 VIGYSDVDDAIQLAARGKGSLVGSLVTHDPA----VARQVTLGV 447
Cdd:cd07093 369 VIPFDDEEEAIELANDTPYGLAAYVWTRDLGrahrVARRLEAGT 412
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
8-456 |
1.51e-25 |
|
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: 110.62 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWI-APEGESIPLINASTGEEVARFASGS-LDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYP 85
Cdd:cd07117 4 FINGEWVkGSSGETIDSYNPANGETLSEITDATdADVDRAVKAAQE-AFKTWRKTTVAERANILNKIADIIDENKELLAM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 SSTA-TGATAKDS-GIDIDGGIGTLLSYAS-----KGT-RELPNDTIYLDGGlEPLGrggtfvgqhiytsrpgVAVQINA 157
Cdd:cd07117 83 VETLdNGKPIRETrAVDIPLAADHFRYFAGviraeEGSaNMIDEDTLSIVLR-EPIG----------------VVGQIIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 158 FNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESgLLPEGSIQLLCA----SPRALLDHlDGQDTVLFTG 233
Cdd:cd07117 146 WNFPFLMAAWKLAPALAAGNTVVIKPSSTTS-LSLLELAKIIQD-VLPKGVVNIVTGkgskSGEYLLNH-PGLDKLAFTG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 234 SA--------STASKLRghPNVVE-GGVRFNaeadslncsILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALV 304
Cdd:cd07117 223 STevgrdvaiAAAKKLI--PATLElGGKSAN---------IIFDDA-----NWDKALEGAQLGILFNQGQVCCAGSRIFV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 305 PNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGDPddfSVEGADASSGAFLPP 383
Cdd:cd07117 287 QEGIYDEFVAKLKEKFENVKVGNPLDPDTQMGAQVNKDQLDKILSYVDiAKEEGAKILTGGH---RLTENGLDKGFFIEP 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816981345 384 LLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGVAPfhGRILI 456
Cdd:cd07117 364 TLIVNVTNDMRVAQE-EIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDINRALRVARAVET--GRVWV 433
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
63-421 |
1.51e-25 |
|
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: 110.20 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 63 HQRAGALKALGKLLMSRKEEF-YPSSTATGATAKDSGIDIDGGIGTLlsyaskgtrELPNDTIYLDGGLE-PLGRGGTFV 140
Cdd:cd07148 44 HERIAILERLADLMEERADELaLLIAREGGKPLVDAKVEVTRAIDGV---------ELAADELGQLGGREiPMGLTPASA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 141 GQHIYTSRP--GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGlLPEGSIQ-LLCASPR 217
Cdd:cd07148 115 GRIAFTTREpiGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAG-LPEGWCQaVPCENAV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 218 ALLDHLDGQDTVL-FTGSASTASKLRGHpnvVEGGVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKC 296
Cdd:cd07148 194 AEKLVTDPRVAFFsFIGSARVGWMLRSK---LAPGTRCALEHGGAAPVIVDRSA-----DLDAMIPPLVKGGFYHAGQVC 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 297 TAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASldqREEVLRSLKSLRDS----ATVVFGdpddfsveG 372
Cdd:cd07148 266 VSVQRVFVPAEIADDFAQRLAAAAEKLVVGDPTDPDTEVGPLIR---PREVDRVEEWVNEAvaagARLLCG--------G 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1816981345 373 ADASSGAFLPPLLLRAQDSAAAAIHEVeaFGPISTVIGYSDVDDAIQLA 421
Cdd:cd07148 335 KRLSDTTYAPTVLLDPPRDAKVSTQEI--FGPVVCVYSYDDLDEAIAQA 381
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
18-436 |
5.96e-25 |
|
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: 108.46 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 18 GESIPLINASTGEEVARFAS-GSLDVAAAIAYGREV--------GGPAlraltfhQRAGALKALGKLLMSRKEEF-YPSS 87
Cdd:cd07112 1 GETFATINPATGRVLAEVAAcDAADVDRAVAAARRAfesgvwsrLSPA-------ERKAVLLRLADLIEAHRDELaLLET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 88 TATGATAKDS-GIDIDGGIGTLLSYAskgtrELPnDTIYldGGLEPLGRGGTfvgqHIYTSRP-GVAVQINAFNFPVWGM 165
Cdd:cd07112 74 LDMGKPISDAlAVDVPSAANTFRWYA-----EAI-DKVY--GEVAPTGPDAL----ALITREPlGVVGAVVPWNFPLLMA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 166 LEKLAPAFLAGVPSIVKPAHQTAyLTEL-VVRAIVESGlLPEGSIQLLCA----SPRALLDHLDgQDTVLFTGSASTASK 240
Cdd:cd07112 142 AWKIAPALAAGNSVVLKPAEQSP-LTALrLAELALEAG-LPAGVLNVVPGfghtAGEALGLHMD-VDALAFTGSTEVGRR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 241 LrghpnvveggVRFNAEAD----SLNCSilGPDAA---KDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVV 313
Cdd:cd07112 219 F----------LEYSGQSNlkrvWLECG--GKSPNivfADAPDLDAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 314 EATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSL-KSLRDSATVVFGDPDDFSVEGadassGAFLPPLLLRaQDSA 392
Cdd:cd07112 287 EKVVAAAREWKPGDPLDPATRMGALVSEAHFDKVLGYIeSGKAEGARLVAGGKRVLTETG-----GFFVEPTVFD-GVTP 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1816981345 393 AAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07112 361 DMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSD 404
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
25-436 |
1.76e-24 |
|
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: 107.14 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 25 NASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYP-SSTATGATAKDS-GIDI 101
Cdd:cd07115 3 NPATGELIARVAQASAeDVDAAVAAARA-AFEAWSAMDPAERGRILWRLAELILANADELARlESLDTGKPIRAArRLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 102 DGGIGTLLSYASKGTRE----LPNDTIYLDggleplgrggtfvgqhiYTSRP--GVAVQINAFNFPVWGMLEKLAPAFLA 175
Cdd:cd07115 82 PRAADTFRYYAGWADKIegevIPVRGPFLN-----------------YTVREpvGVVGAIVPWNFPLMFAAWKVAPALAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 176 GVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCASPR----ALLDHLDgQDTVLFTGSASTASKLrghpnvVEGG 251
Cdd:cd07115 145 GNTVVLKPAELTP-LSALRIAELMAEAGFPAGVLNVVTGFGEvagaALVEHPD-VDKITFTGSTAVGRKI------MQGA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 252 V----RFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGH 327
Cdd:cd07115 217 AgnlkRVSLELGGKSANIVFADA-----DLDAAVRAAATGIFYNQGQMCTAGSRLLVHESIYDEFLERFTSLARSLRPGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 328 PNAEGVRMGPLASLDQREEVLRSLKSLR-DSATVVFGDPddfsvegADASSGAFLPPLLLRAQdSAAAAIHEVEAFGPIS 406
Cdd:cd07115 292 PLDPKTQMGPLVSQAQFDRVLDYVDVGReEGARLLTGGK-------RPGARGFFVEPTIFAAV-PPEMRIAQEEIFGPVV 363
|
410 420 430
....*....|....*....|....*....|
gi 1816981345 407 TVIGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07115 364 SVMRFRDEEEALRIANGTEYGLAAGVWTRD 393
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
8-444 |
1.04e-23 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 105.20 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAP-EGESIPLINASTGEEVARFASG-SLDVAAAI-----AYGREVGGPALRAlTFHQRAGALKALGKLLMSRK 80
Cdd:PLN02467 11 FIGGEWREPvLGKRIPVVNPATEETIGDIPAAtAEDVDAAVeaarkAFKRNKGKDWART-TGAVRAKYLRAIAAKITERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 81 EEFYPSSTA-TGATAKDSGIDIDGGIGTLLSYAS-----KGTRELPndtiyLDGGLEplgrggTFVGqHIYTSRPGVAVQ 154
Cdd:PLN02467 90 SELAKLETLdCGKPLDEAAWDMDDVAGCFEYYADlaealDAKQKAP-----VSLPME------TFKG-YVLKEPLGVVGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 155 INAFNFPVWGMLEKLAPAFLAGVPSIVKPAhQTAYLTELVVRAIVESGLLPEGSIQL-----------LCASPralldhl 223
Cdd:PLN02467 158 ITPWNYPLLMATWKVAPALAAGCTAVLKPS-ELASVTCLELADICREVGLPPGVLNVvtglgteagapLASHP------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 224 dGQDTVLFTGSASTASKlrghpnvveggVRFNAEADSLNCSI-LGPDAAKDTpeFELYIKQLVAEMTT-----KAGQKCT 297
Cdd:PLN02467 230 -GVDKIAFTGSTATGRK-----------IMTAAAQMVKPVSLeLGGKSPIIV--FDDVDLDKAVEWAMfgcfwTNGQICS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 298 AIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGdpddfSVEGADAS 376
Cdd:PLN02467 296 ATSRLLVHERIASEFLEKLVKWAKNIKISDPLEEGCRLGPVVSEGQYEKVLKFIStAKSEGATILCG-----GKRPEHLK 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816981345 377 SGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:PLN02467 371 KGFFIEPTII-TDVTTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVS 437
|
|
| MaoC_like |
cd03446 |
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ... |
535-673 |
7.30e-23 |
|
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.
Pssm-ID: 239530 [Multi-domain] Cd Length: 140 Bit Score: 94.68 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 535 HLEELQIGDTVVGGPRVVSLEDIDHFAEFTGDTFYAHTDPKAAAENPlFGGIVAHGYLVVSLAAGL--FVEPNPGPVLAN 612
Cdd:cd03446 1 YFEDFEIGQVFESVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTR-FGERIAHGLLTLSIATGLlqRLGVFERTVVAF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816981345 613 FGVDGLRFLTPVKAGDALTVTLTAKQVTPRLSADYGEVRWDAVVANQNDDPVATYDVLTLV 673
Cdd:cd03446 80 YGIDNLRFLNPVFIGDTIRAEAEVVEKEEKDGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
8-448 |
8.01e-23 |
|
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: 102.47 E-value: 8.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPEG-ESIPLINASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYP 85
Cdd:cd07111 25 FINGKWVKPENrKSFPTINPATGEVLASVLQAEEeDVDAAVAAART-AFESWSALPGHVRARHLYRIARHIQKHQRLFAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 -SSTATGATAKDS-GIDIDGGIGTLLSYA---SKGTRELPndtiyldgGLEPlgrggtfvgqhiytsrPGVAVQINAFNF 160
Cdd:cd07111 104 lESLDNGKPIRESrDCDIPLVARHFYHHAgwaQLLDTELA--------GWKP----------------VGVVGQIVPWNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 161 PVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCASPR---ALLDHlDGQDTVLFTGSAST 237
Cdd:cd07111 160 PLLMLAWKICPALAMGNTVVLKPAEYTP-LTALLFAEICAEAGLPPGVLNIVTGNGSfgsALANH-PGVDKVAFTGSTEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 238 ASKLRghpnvveggvRFNAEAD---SLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVE 314
Cdd:cd07111 238 GRALR----------RATAGTGkklSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLLVQESVAEELIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 315 ATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPDDFSvegadaSSGAFLPPLLLrAQDSAAA 394
Cdd:cd07111 308 KLKERMSHLRVGDPLDKAIDMGAIVDPAQLKRIRELVEEGRAEGADVFQPGADLP------SKGPFYPPTLF-TNVPPAS 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1816981345 395 AIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGVA 448
Cdd:cd07111 381 RIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLK 434
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
8-444 |
1.33e-22 |
|
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: 101.52 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWI-APEGESIPLINASTGEEVARFASGSL-DVAAAIAYGREV--GGPAlRALTFHQRAGALKALGKLLMSRKEEF 83
Cdd:cd07091 7 FINNEFVdSVSGKTFPTINPATEEVICQVAEADEeDVDAAVKAARAAfeTGWW-RKMDPRERGRLLNKLADLIERDRDEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 YP-SSTATGATAKDS-GIDIDGGIGTLLSYASKGtrelpnDTIylDGGLEPLGRGGTFvgqhiYTSR-P-GVAVQINAFN 159
Cdd:cd07091 86 AAlESLDNGKPLEESaKGDVALSIKCLRYYAGWA------DKI--QGKTIPIDGNFLA-----YTRRePiGVCGQIIPWN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 160 FPVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCASPR----ALLDHLDgQDTVLFTGSA 235
Cdd:cd07091 153 FPLLMLAWKLAPALAAGNTVVLKPAEQTP-LSALYLAELIKEAGFPPGVVNIVPGFGPtagaAISSHMD-VDKIAFTGST 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 236 STASKlrghpnVVEGGVRFNAEADSLNC-----SILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVD 310
Cdd:cd07091 231 AVGRT------IMEAAAKSNLKKVTLELggkspNIVFDDA-----DLDKAVEWAAFGIFFNQGQCCCAGSRIFVQESIYD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 311 DVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKS-LRDSATVVFGDpddfsveGADASSGAFLPP-LLLRA 388
Cdd:cd07091 300 EFVEKFKARAEKRVVGDPFDPDTFQGPQVSKAQFDKILSYIESgKKEGATLLTGG-------ERHGSKGYFIQPtVFTDV 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1816981345 389 QDSAAAAIHEVeaFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07091 373 KDDMKIAKEEI--FGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVS 426
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
24-443 |
1.61e-22 |
|
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: 101.23 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARF-ASGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEF-YPSSTATGATAKDSGIDI 101
Cdd:cd07090 2 IEPATGEVLATVhCAGAEDVDLAVKSAKA-AQKEWSATSGMERGRILRKAADLLRERNDEIaRLETIDNGKPIEEARVDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 102 DGGIGTLLSYASKGTRelpndtiyLDGGLEPLgRGGTFVgqhiYTSR-P-GVAVQINAFNFPVWGMLEKLAPAFLAGVPS 179
Cdd:cd07090 81 DSSADCLEYYAGLAPT--------LSGEHVPL-PGGSFA----YTRRePlGVCAGIGAWNYPIQIASWKSAPALACGNAM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 180 IVKPAHQTAyLTELVVRAIVESGLLPEGSIQLL--CASPRALLDHLDGQDTVLFTGSASTASKLRGhpnvveggvrfnAE 257
Cdd:cd07090 148 VYKPSPFTP-LTALLLAEILTEAGLPDGVFNVVqgGGETGQLLCEHPDVAKVSFTGSVPTGKKVMS------------AA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 258 ADSLNCS----------ILGPDAAkdtpefelyIKQLV--AEMTT--KAGQKCTAIRRALVPNELVDDVVEATRTRLSKV 323
Cdd:cd07090 215 AKGIKHVtlelggksplIIFDDAD---------LENAVngAMMANflSQGQVCSNGTRVFVQRSIKDEFTERLVERTKKI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 324 VVGHPNAEGVRMGPLASLDQREEVLRSLKSLR-DSATVVFGDpdDFSVEGADASSGAFLPPLLLRAQDSAAAAIHEvEAF 402
Cdd:cd07090 286 RIGDPLDEDTQMGALISEEHLEKVLGYIESAKqEGAKVLCGG--ERVVPEDGLENGFYVSPCVLTDCTDDMTIVRE-EIF 362
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1816981345 403 GPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07090 363 GPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRV 403
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
8-420 |
1.26e-21 |
|
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: 98.43 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPeGESIPLINASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEfyps 86
Cdd:cd07130 2 VYDGEWGGG-GGVVTSISPANGEPIARVRQATPeDYESTIKAAQE-AFKEWRDVPAPKRGEIVRQIGDALRKKKEA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 87 statgatakdsgididggIGTLLSY-ASKgtrelpndtIYLDGGLE----------PLGRGGTFVGQHIYTSRPG----- 150
Cdd:cd07130 76 ------------------LGKLVSLeMGK---------ILPEGLGEvqemidicdfAVGLSRQLYGLTIPSERPGhrmme 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 151 -------VAVqINAFNFP--VWGMleKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGL----LPEGSIQLLCASPR 217
Cdd:cd07130 129 qwnplgvVGV-ITAFNFPvaVWGW--NAAIALVCGNVVVWKPSPTTP-LTAIAVTKIVARVLekngLPGAIASLVCGGAD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 218 ---ALLDHLDgQDTVLFTGSASTASKLrgHPNVVEggvRFnaeADSL------NCSILGPDAakdtpEFELYIKQ-LVAE 287
Cdd:cd07130 205 vgeALVKDPR-VPLVSFTGSTAVGRQV--GQAVAA---RF---GRSLlelggnNAIIVMEDA-----DLDLAVRAvLFAA 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 288 MTTkAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPL---ASLDQREEVLRSLKSlrDSATVVFGD 364
Cdd:cd07130 271 VGT-AGQRCTTTRRLIVHESIYDEVLERLKKAYKQVRIGDPLDDGTLVGPLhtkAAVDNYLAAIEEAKS--QGGTVLFGG 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1816981345 365 PddfSVEGadasSGAFLPPLLLRAqDSAAAAIHEvEAFGPISTVIGYSDVDDAIQL 420
Cdd:cd07130 348 K---VIDG----PGNYVEPTIVEG-LSDAPIVKE-ETFAPILYVLKFDTLEEAIAW 394
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
8-444 |
4.36e-21 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 97.20 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWI-APEGESIPLINASTGEEVARFASG-SLDVAAAIAYGREV--GGPALRaLTFHQRAGALKALGKLLMSRKEEF 83
Cdd:PLN02766 24 FINGEFVdAASGKTFETRDPRTGEVIARIAEGdKEDVDLAVKAAREAfdHGPWPR-MSGFERGRIMMKFADLIEEHIEEL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 YPSSTATGATAKDSG--IDIDGGIGTLLSYASKGtrelpnDTIYldgGlEPLGRGGTFVGqhiYTSRP--GVAVQINAFN 159
Cdd:PLN02766 103 AALDTIDAGKLFALGkaVDIPAAAGLLRYYAGAA------DKIH---G-ETLKMSRQLQG---YTLKEpiGVVGHIIPWN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 160 FPVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCA----SPRALLDHLDgQDTVLFTGSA 235
Cdd:PLN02766 170 FPSTMFFMKVAPALAAGCTMVVKPAEQTP-LSALFYAHLAKLAGVPDGVINVVTGfgptAGAAIASHMD-VDKVSFTGST 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 236 STASKlrghpnVVEGGVRFNAEADSLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEA 315
Cdd:PLN02766 248 EVGRK------IMQAAATSNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSRVYVQEGIYDEFVKK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 316 TRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGDPddfsvegADASSGAFLPPLLLrAQDSAAA 394
Cdd:PLN02766 322 LVEKAKDWVVGDPFDPRARQGPQVDKQQFEKILSYIEhGKREGATLLTGGK-------PCGDKGYYIEPTIF-TDVTEDM 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1816981345 395 AIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:PLN02766 394 KIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTVS 443
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
11-446 |
5.48e-21 |
|
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: 96.60 E-value: 5.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 11 GKWIAPEGE-SIPLINASTGEEVARFASGSL-DVAAAIAYGREVGGPALRALTFHQRAGALKALGkLLMSRKEEF-YPSS 87
Cdd:cd07151 1 GEWRDGTSErTIDVLNPYTGETLAEIPAASKeDVDEAYRAAAAAQKEWAATLPQERAEILEKAAQ-ILEERRDEIvEWLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 88 TATGATAKDSGIDIDGGIGTLLSYAS----KGTRELPNDTiyldGGLEplgrggtfvgQHIYTSRPGVAVQINAFNFPVW 163
Cdd:cd07151 80 RESGSTRIKANIEWGAAMAITREAATfplrMEGRILPSDV----PGKE----------NRVYREPLGVVGVISPWNFPLH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 164 GMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLLPEGSIQLLCASPRALLDHLDGQ---DTVLFTGS------ 234
Cdd:cd07151 146 LSMRSVAPALALGNAVVLKPASDTPITGGLLLAKIFEEAGLPKGVLNVVVGAGSEIGDAFVEHpvpRLISFTGStpvgrh 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 235 -ASTASKLRGHPNVVEGGvrfN------AEADSlncsilgpDAAKDTPEFELYIKQlvaemttkaGQKCTAIRRALVPNE 307
Cdd:cd07151 226 iGELAGRHLKKVALELGG---NnpfvvlEDADI--------DAAVNAAVFGKFLHQ---------GQICMAINRIIVHED 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 308 LVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSL-KSLRDSATVVFGDPDDfsvegadassGAFLPPLLL 386
Cdd:cd07151 286 VYDEFVEKFVERVKALPYGDPSDPDTVVGPLINESQVDGLLDKIeQAVEEGATLLVGGEAE----------GNVLEPTVL 355
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816981345 387 RAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDP----AVARQVTLG 446
Cdd:cd07151 356 SDVTNDMEIARE-EIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLergvQFARRIDAG 418
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
27-421 |
8.71e-21 |
|
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: 95.87 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 27 STGEEVARFASGSL-DVAAAIAYGREV--GGPALRaLTFHQRAGALKALGKLLMSRKEEF-YPSSTATGATAKDSGIDID 102
Cdd:cd07118 5 AHGVVVARYAEGTVeDVDAAVAAARKAfdKGPWPR-MSGAERAAVLLKVADLIRARRERLaLIETLESGKPISQARGEIE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 103 GGIGtLLSYASKGTRELPNDTiyldggLEPLGRG--GTFVGQHIytsrpGVAVQINAFNFPVWGMLEKLAPAFLAGVPSI 180
Cdd:cd07118 84 GAAD-LWRYAASLARTLHGDS------YNNLGDDmlGLVLREPI-----GVVGIITPWNFPFLILSQKLPFALAAGCTVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 181 VKPAHQTAYLTELVVRAIVESGlLPEGSIQLLCASPR----ALLDHLDgQDTVLFTGSASTASKLRGhpnvveggvrfnA 256
Cdd:cd07118 152 VKPSEFTSGTTLMLAELLIEAG-LPAGVVNIVTGYGAtvgqAMTEHPD-VDMVSFTGSTRVGKAIAA------------A 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 257 EADSL----------NCSILGPD----AAKDTPEFELYIkqlvaemttKAGQKCTAIRRALVPNELVDDVVEATRTRLSK 322
Cdd:cd07118 218 AARNLkkvslelggkNPQIVFADadldAAADAVVFGVYF---------NAGECCNSGSRLLVHESIADAFVAAVVARSRK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 323 VVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDpddfsvEGADASSGAFLPPLLLRAQdSAAAAIHEVEA 401
Cdd:cd07118 289 VRVGDPLDPETKVGAIINEAQLAKITDYVDAGRAEgATLLLGG------ERLASAAGLFYQPTIFTDV-TPDMAIAREEI 361
|
410 420
....*....|....*....|
gi 1816981345 402 FGPISTVIGYSDVDDAIQLA 421
Cdd:cd07118 362 FGPVLSVLTFDTVDEAIALA 381
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
41-447 |
9.33e-21 |
|
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: 95.29 E-value: 9.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 41 DVAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEFYPS-STATGATAKDSGIDIDGGIGTLLSYASKGTRel 119
Cdd:cd07104 1 DVDRAYAAAAAAQ-KAWAATPPQERAAILRKAAEILEERRDEIADWlIRESGSTRPKAAFEVGAAIAILREAAGLPRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 120 pndtiyLDGGLEPLGRGGTFvgQHIYTSRPGVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIV 199
Cdd:cd07104 78 ------PEGEILPSDVPGKE--SMVRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLIAEIF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 200 ESGLLPEGSIQLLCASPR----ALLDHLDgQDTVLFTGS-------ASTASKLRGHPNVVEGGvrfN------AEADsln 262
Cdd:cd07104 150 EEAGLPKGVLNVVPGGGSeigdALVEHPR-VRMISFTGStavgrhiGELAGRHLKKVALELGG---NnplivlDDAD--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 263 csilgPDAAKDTPEFELYIKQlvaemttkaGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLD 342
Cdd:cd07104 223 -----LDLAVSAAAFGAFLHQ---------GQICMAAGRILVHESVYDEFVEKLVAKAKALPVGDPRDPDTVIGPLINER 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 343 QREEVLRSL-KSLRDSATVVFGDPDDfsvegadassGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLA 421
Cdd:cd07104 289 QVDRVHAIVeDAVAAGARLLTGGTYE----------GLFYQPTVLSDVTPDMPIFRE-EIFGPVAPVIPFDDDEEAVELA 357
|
410 420 430
....*....|....*....|....*....|
gi 1816981345 422 ARGKGSLVGSLVTHDP----AVARQVTLGV 447
Cdd:cd07104 358 NDTEYGLSAAVFTRDLeramAFAERLETGM 387
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
41-446 |
1.23e-20 |
|
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: 95.05 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 41 DVAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKEEFYP-SSTATGATAKDSGIDIDGGIGTLLSYASKGTREL 119
Cdd:cd07152 14 DVDRAAARAAAAQ-RAWAATPPRERAAVLRRAADLLEEHADEIADwIVRESGSIRPKAGFEVGAAIGELHEAAGLPTQPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 120 pndtiyldGGLEPLGRGGTFVGQHiytsRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAI 198
Cdd:cd07152 93 --------GEILPSAPGRLSLARR----VPlGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGGVVIARL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 199 VESGLLPEGSIQLLCASP---RALLDHLDgQDTVLFTGSASTASKLrghpNVVEGGV--RFNAEADSLNCSILGPDA--- 270
Cdd:cd07152 161 FEEAGLPAGVLHVLPGGAdagEALVEDPN-VAMISFTGSTAVGRKV----GEAAGRHlkKVSLELGGKNALIVLDDAdld 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 271 -AKDTPEFELYIKQlvaemttkaGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLR 349
Cdd:cd07152 236 lAASNGAWGAFLHQ---------GQICMAAGRHLVHESVADAYTAKLAAKAKHLPVGDPATGQVALGPLINARQLDRVHA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 350 SLK-SLRDSATVVFGDPDDfsvegadassGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSL 428
Cdd:cd07152 307 IVDdSVAAGARLEAGGTYD----------GLFYRPTVLSGVKPGMPAFDE-EIFGPVAPVTVFDSDEEAVALANDTEYGL 375
|
410
....*....|....*...
gi 1816981345 429 VGSLVTHDpaVARQVTLG 446
Cdd:cd07152 376 SAGIISRD--VGRAMALA 391
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
9-444 |
4.66e-20 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 94.10 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 9 VSGKWI-APEGESIPLINASTGEEVARFASGSL-DVAAAIAYGREV--GGPALRaLTFHQRAGALKALGKLLMSRKEEFY 84
Cdd:PLN02466 62 INGQFVdAASGKTFPTLDPRTGEVIAHVAEGDAeDVNRAVAAARKAfdEGPWPK-MTAYERSRILLRFADLLEKHNDELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 85 PSSTAtgatakDSGididggigtlLSYASKGTRELP------------NDTIYldgGLEPLGRGGTFVgqHIYTSRPGVA 152
Cdd:PLN02466 141 ALETW------DNG----------KPYEQSAKAELPmfarlfryyagwADKIH---GLTVPADGPHHV--QTLHEPIGVA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 153 VQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCA----SPRALLDHLDgQDT 228
Cdd:PLN02466 200 GQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAGL-PPGVLNVVSGfgptAGAALASHMD-VDK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 229 VLFTGSASTAsKLrghpnVVEGGVRFNAEADSLN---------CSILGPDAAKDTPEFELYIKQlvaemttkaGQKCTAI 299
Cdd:PLN02466 278 LAFTGSTDTG-KI-----VLELAAKSNLKPVTLElggkspfivCEDADVDKAVELAHFALFFNQ---------GQCCCAG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 300 RRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGDpDDFSvegadaSSG 378
Cdd:PLN02466 343 SRTFVHERVYDEFVEKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVESgATLECGG-DRFG------SKG 415
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816981345 379 AFLPPLLLR-AQDSAAAAIHEVeaFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:PLN02466 416 YYIQPTVFSnVQDDMLIAQDEI--FGPVQSILKFKDLDEVIRRANNTRYGLAAGVFTQNLDTANTLS 480
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
8-438 |
6.22e-20 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 93.46 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPEgESIPLIN-ASTGEEVARFASGSLDVA-AAIAygrevggPALRALTF------HQRAGALKALGKLLMSR 79
Cdd:PRK03137 40 IIGGERITTE-DKIVSINpANKSEVVGRVSKATKELAeKAMQ-------AALEAFETwkkwspEDRARILLRAAAIIRRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 80 KEEFypSSTAT---GATAKDSGIDIDGGIGTLLSYAskgtRElpndTIYLDGGLEPLGRGGTFVGqhiYTSRP-GVAVQI 155
Cdd:PRK03137 112 KHEF--SAWLVkeaGKPWAEADADTAEAIDFLEYYA----RQ----MLKLADGKPVESRPGEHNR---YFYIPlGVGVVI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 156 NAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHL-DGQDT--VLFT 232
Cdd:PRK03137 179 SPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAGL-PAGVVNFVPGSGSEVGDYLvDHPKTrfITFT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 233 GSASTasklrghpnvvegGVRFNAEAdslncsilgpdaAKDTPEfELYIKQLVAEMTTK--------------------- 291
Cdd:PRK03137 258 GSREV-------------GLRIYERA------------AKVQPG-QIWLKRVIAEMGGKdaivvdedadldlaaesivas 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 292 ----AGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPnAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGdpdd 367
Cdd:PRK03137 312 afgfSGQKCSACSRAIVHEDVYDEVLEKVVELTKELTVGNP-EDNAYMGPVINQASFDKIMSYIEIGKEEGRLVLG---- 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816981345 368 fsvEGADASSGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPA 438
Cdd:PRK03137 387 ---GEGDDSKGYFIQPTIFADVDPKARIMQE-EIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNNRE 453
|
|
| YdeM |
cd03454 |
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ... |
536-674 |
6.54e-20 |
|
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.
Pssm-ID: 239538 [Multi-domain] Cd Length: 140 Bit Score: 86.47 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 536 LEELQIGDTVVGGPRVVSLEDIDHFA-EFtgDTFYAHTDPkAAAENPLFGGIVAHGYLVVSLAAGLFVEPN-------PG 607
Cdd:cd03454 1 FEDLVIGQRFTSGSYTVTEEEIIAFArEF--DPQPFHLDE-EAAKESLFGGLAASGWHTAAITMRLLVDAGlsgsasgGS 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816981345 608 PvlanfGVDGLRFLTPVKAGDALTVTLTAKQVTPRLS-ADYGEVRWDAVVANQNDDPVATYDVLTLVA 674
Cdd:cd03454 78 P-----GIDELRWPRPVRPGDTLSVEVEVLDKRPSRSrPDRGIVTLRSETLNQRGEVVLTFEATVLVR 140
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
141-447 |
9.16e-20 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 92.11 E-value: 9.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 141 GQHIYT-SRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGlLPEGSIQLLcaspra 218
Cdd:PRK10090 62 GENILLfKRAlGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIG-LPKGVFNLV------ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 219 lldhldgqdtvlfTGSAST-ASKLRGHPNV--------VEGGVRFnAEADSLN----CSILG---PDAAKDTPEFELYIK 282
Cdd:PRK10090 135 -------------LGRGETvGQELAGNPKVamvsmtgsVSAGEKI-MAAAAKNitkvCLELGgkaPAIVMDDADLDLAVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 283 QLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHP-NAEGVRMGPLASLDQREEVLRSL-KSLRDSATV 360
Cdd:PRK10090 201 AIVDSRVINSGQVCNCAERVYVQKGIYDQFVNRLGEAMQAVQFGNPaERNDIAMGPLINAAALERVEQKVaRAVEEGARV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 361 VFGDPddfsvegADASSGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVA 440
Cdd:PRK10090 281 ALGGK-------AVEGKGYYYPPTLLLDVRQEMSIMHE-ETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQNLNVA 352
|
....*..
gi 1816981345 441 RQVTLGV 447
Cdd:PRK10090 353 MKAIKGL 359
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
11-447 |
9.18e-20 |
|
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: 93.03 E-value: 9.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 11 GKWIAPEGESIPLIN---------------ASTGEEVARFA-SGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGK 74
Cdd:cd07125 24 KAFDEKEWEAIPIINgeetetgegapvidpADHERTIGEVSlADAEDVDAALAIAAA-AFAGWSATPVEERAEILEKAAD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 75 LLMSRKEEFYPSSTA-TGATAKDsGID-----IDggigtLLSYASKGTRELPNDTIyLDGGLEPLgRGGTFVGQhiytsr 148
Cdd:cd07125 103 LLEANRGELIALAAAeAGKTLAD-ADAevreaID-----FCRYYAAQARELFSDPE-LPGPTGEL-NGLELHGR------ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 149 pGVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHL---DG 225
Cdd:cd07125 169 -GVFVCISPWNFPLAIFTGQIAAALAAGNTVIAKPAEQTPLIAARAVELLHEAGV-PRDVLQLVPGDGEEIGEALvahPR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 226 QDTVLFTGSASTASK-LRGHPNVVEGGVRFNAEADSLNCSILGPDAAKdtpefELYIKQLVAEMTTKAGQKCTAIRRALV 304
Cdd:cd07125 247 IDGVIFTGSTETAKLiNRALAERDGPILPLIAETGGKNAMIVDSTALP-----EQAVKDVVQSAFGSAGQRCSALRLLYL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 305 PNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLAsldqREEVLRSLKSL----RDSATVVFGDPddfsvegADASSGAF 380
Cdd:cd07125 322 QEEIAERFIEMLKGAMASLKVGDPWDLSTDVGPLI----DKPAGKLLRAHtelmRGEAWLIAPAP-------LDDGNGYF 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 381 LPPLLLRAQDSAAaaiHEVEAFGPISTVIGY--SDVDDAI-QLAARGKGsLVGSLVTHDPAVARQVTLGV 447
Cdd:cd07125 391 VAPGIIEIVGIFD---LTTEVFGPILHVIRFkaEDLDEAIeDINATGYG-LTLGIHSRDEREIEYWRERV 456
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
8-443 |
1.11e-19 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 92.64 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWIAPE-GESIPLINASTGEEVARF-ASGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYP 85
Cdd:PRK13252 10 YIDGAYVEATsGETFEVINPATGEVLATVqAATPADVEAAVASAKQ-GQKIWAAMTAMERSRILRRAVDILRERNDELAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 SSTA-TG-ATAKDSGIDIDGGIGTLLSYASKGTRelpndtiyLDGGLEPLgRGGTFVgqhiYTSR-P-GVAVQINAFNFP 161
Cdd:PRK13252 89 LETLdTGkPIQETSVVDIVTGADVLEYYAGLAPA--------LEGEQIPL-RGGSFV----YTRRePlGVCAGIGAWNYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 162 VWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAI-VESGLlPEGSIQLLCASPR--ALLDHLDGQDTVLFTGS---- 234
Cdd:PRK13252 156 IQIACWKSAPALAAGNAMIFKPSEVTP-LTALKLAEIyTEAGL-PDGVFNVVQGDGRvgAWLTEHPDIAKVSFTGGvptg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 235 ----ASTASKLRgHPNVVEGG----VRFNaEADsLNCSIlgpDAAkdtpefelyikqLVAEMTTkAGQKCTAIRRALVPN 306
Cdd:PRK13252 234 kkvmAAAAASLK-EVTMELGGksplIVFD-DAD-LDRAA---DIA------------MLANFYS-SGQVCTNGTRVFVQK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 307 ELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKS-LRDSATVVFGdpdDFSVEGADASSGAFLPPLL 385
Cdd:PRK13252 295 SIKAAFEARLLERVERIRIGDPMDPATNFGPLVSFAHRDKVLGYIEKgKAEGARLLCG---GERLTEGGFANGAFVAPTV 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816981345 386 LrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:PRK13252 372 F-TDCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADLSRAHRV 428
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
8-444 |
1.26e-19 |
|
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: 92.59 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWI-APEGESIPLINASTGE---EVARFASGSLDVAAAIAYgREVGGPALRALTFHQRAGALKALGKLlMSRKEEF 83
Cdd:cd07143 10 FINGEFVdSVHGGTVKVYNPSTGKlitKIAEATEADVDIAVEVAH-AAFETDWGLKVSGSKRGRCLSKLADL-MERNLDY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 YPSSTA-----TGATAKdsGIDIDGGIGTLLSYASKGtrelpnDTIYldggleplgrggtfvGQHIYTS---------RP 149
Cdd:cd07143 88 LASIEAldngkTFGTAK--RVDVQASADTFRYYGGWA------DKIH---------------GQVIETDikkltytrhEP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 -GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCASPR----ALLDHLD 224
Cdd:cd07143 145 iGVCGQIIPWNFPLLMCAWKIAPALAAGNTIVLKPSELTP-LSALYMTKLIPEAGFPPGVINVVSGYGRtcgnAISSHMD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 225 gQDTVLFTGSASTASKlrghpnVVEGGVRFNAEADSLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALV 304
Cdd:cd07143 224 -IDKVAFTGSTLVGRK------VMEAAAKSNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 305 PNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLR-DSATVVFGDPddfsvegADASSGAFLPP 383
Cdd:cd07143 297 QEGIYDKFVKRFKEKAKKLKVGDPFAEDTFQGPQVSQIQYERIMSYIESGKaEGATVETGGK-------RHGNEGYFIEP 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816981345 384 LLLrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07143 370 TIF-TDVTEDMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNINNAIRVA 429
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
150-444 |
3.58e-19 |
|
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: 91.10 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHLDGQDT- 228
Cdd:cd07083 156 GAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEDAVVVGYKVFEIFHEAGF-PPGVVQFLPGVGEEVGAYLTEHERi 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 229 --VLFTGSASTASKLRGHPNVVEGG----VRFNAEADSLNCSILgpdaaKDTPEFELYIKQLVAEMTTKAGQKCTAIRRA 302
Cdd:cd07083 235 rgINFTGSLETGKKIYEAAARLAPGqtwfKRLYVETGGKNAIIV-----DETADFELVVEGVVVSAFGFQGQKCSAASRL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 303 LVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPddfsvegADASSGAFLP 382
Cdd:cd07083 310 ILTQGAYEPVLERLLKRAERLSVGPPEENGTDLGPVIDAEQEAKVLSYIEHGKNEGQLVLGGK-------RLEGEGYFVA 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816981345 383 PLLLRaQDSAAAAIHEVEAFGPISTVIGYSDVD--DAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07083 383 PTVVE-EVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEAR 445
|
|
| NodN |
cd03450 |
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ... |
535-642 |
8.10e-19 |
|
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.
Pssm-ID: 239534 [Multi-domain] Cd Length: 149 Bit Score: 83.38 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 535 HLEELQ--IGDTV-VGGPRVVSLEDIDHFAEFTGDTFYAHTDPKAAAENPlFGGIVAHGYLVVSLAAGLFVE--PNPGPV 609
Cdd:cd03450 4 SLADLAalVGQELgVSDWVTVDQERIDQFADATGDHQWIHVDPERAAAEP-FGGTIAHGFLTLSLLPALTPQlfRVEGVK 82
|
90 100 110
....*....|....*....|....*....|....
gi 1816981345 610 LA-NFGVDGLRFLTPVKAGDALTVTLTAKQVTPR 642
Cdd:cd03450 83 MGvNYGLDKVRFPAPVPVGSRVRGRFTLLSVEEL 116
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
5-447 |
1.70e-18 |
|
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: 88.73 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 5 LESYVSGKWIAPEG-ESIPLINASTGEEVARFA-SGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEE 82
Cdd:cd07085 1 LKLFINGEWVESKTtEWLDVYNPATGEVIARVPlATAEEVDAAVAAAKA-AFPAWSATPVLKRQQVMFKFRQLLEENLDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 83 FYPSSTA-TGATAKDSGIDIDGGI-----GTLLSYASKGTrelpndtiYLDGgleplgrggtfVGQHI--YTSR-P-GVA 152
Cdd:cd07085 80 LARLITLeHGKTLADARGDVLRGLevvefACSIPHLLKGE--------YLEN-----------VARGIdtYSYRqPlGVV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 153 VQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPR---ALLDHLDgQDTV 229
Cdd:cd07085 141 AGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGAAMRLAELLQEAGL-PDGVLNVVHGGKEavnALLDHPD-IKAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 230 LFTGSA-------STASKLrghpnvvegGVRFNAEADSLNCSILGPDAAKdtpefELYIKQLVAEMTTKAGQKCTAIRRA 302
Cdd:cd07085 219 SFVGSTpvgeyiyERAAAN---------GKRVQALGGAKNHAVVMPDADL-----EQTANALVGAAFGAAGQRCMALSVA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 303 LVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSL-KSLRDSATVVFgDPDDFSVEGADAssGAFL 381
Cdd:cd07085 285 VAVGDEADEWIPKLVERAKKLKVGAGDDPGADMGPVISPAAKERIEGLIeSGVEEGAKLVL-DGRGVKVPGYEN--GNFV 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816981345 382 PPLLLrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAAR---GKGSlvgSLVTHDPAVARQVTLGV 447
Cdd:cd07085 362 GPTIL-DNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINAnpyGNGA---AIFTRSGAAARKFQREV 426
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
6-421 |
2.93e-18 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 88.43 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 6 ESYVSGKWI-APEGESIPLINASTGEEVARFAS-GSLDVAAAI-AYGREVggPALRALTFHQRAGALKALGKLLMSRKEE 82
Cdd:PRK11241 12 QALINGEWLdANNGEVIDVTNPANGDKLGSVPKmGADETRAAIdAANRAL--PAWRALTAKERANILRRWFNLMMEHQDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 83 FYPSST-ATGATAKDSGIDIDGGIGTLLSYASKGTReLPNDTIyldGGLEPLGRggtfvgqHIYTSRP-GVAVQINAFNF 160
Cdd:PRK11241 90 LARLMTlEQGKPLAEAKGEISYAASFIEWFAEEGKR-IYGDTI---PGHQADKR-------LIVIKQPiGVTAAITPWNF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 161 PVWGMLEKLAPAFLAGVPSIVKPAHQTAY----LTELVVRAIVesgllPEGSIQLLCASPRALLDHLDGQDTVL---FTG 233
Cdd:PRK11241 159 PAAMITRKAGPALAAGCTMVLKPASQTPFsalaLAELAIRAGI-----PAGVFNVVTGSAGAVGGELTSNPLVRklsFTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 234 SASTASKLRGHpnvveggVRFNAEADSLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVV 313
Cdd:PRK11241 234 STEIGRQLMEQ-------CAKDIKKVSLELGGNAPFIVFDDADLDKAVEGALASKFRNAGQTCVCANRLYVQDGVYDRFA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 314 EATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGDPddfsvegADASSGAFLPPLLLrAQDSA 392
Cdd:PRK11241 307 EKLQQAVSKLHIGDGLEKGVTIGPLIDEKAVAKVEEHIAdALEKGARVVCGGK-------AHELGGNFFQPTIL-VDVPA 378
|
410 420
....*....|....*....|....*....
gi 1816981345 393 AAAIHEVEAFGPISTVIGYSDVDDAIQLA 421
Cdd:PRK11241 379 NAKVAKEETFGPLAPLFRFKDEADVIAQA 407
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
20-438 |
4.30e-18 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 87.49 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 20 SIPLINASTGEEVARFASGSLD-VAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYPS-STATGATAKDS 97
Cdd:PRK09406 2 PIATINPATGETVKTFTALTDDeVDAAIARAHA-RFRDYRTTTFAQRARWANAAADLLEAEADQVAALmTLEMGKTLASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 98 GIDIDGGIGTLLSYASKGTRELPNdtiyldgglEPLGRGGTFVGQHIYTSRP-GVAVQINAFNFPVWGMLEKLAPAFLAG 176
Cdd:PRK09406 81 KAEALKCAKGFRYYAEHAEALLAD---------EPADAAAVGASRAYVRYQPlGVVLAVMPWNFPLWQVVRFAAPALMAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 177 VPSIVKPAH---QTA-YLTELVVRAIVESG-----LLPEGSIQLLCASPRALLDHLDGQDTVLFTGSASTASKLRghPNV 247
Cdd:PRK09406 152 NVGLLKHASnvpQTAlYLADLFRRAGFPDGcfqtlLVGSGAVEAILRDPRVAAATLTGSEPAGRAVAAIAGDEIK--KTV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 248 VE-GGvrfnaeADSLncsILGPDAAKDTPefelyIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVG 326
Cdd:PRK09406 230 LElGG------SDPF---IVMPSADLDRA-----AETAVTARVQNNGQSCIAAKRFIVHADVYDAFAEKFVARMAALRVG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 327 HPNAEGVRMGPLASLDQREEVLRSLK-SLRDSATVVFGD--PDdfsvegadaSSGAFLPPLLLrAQDSAAAAIHEVEAFG 403
Cdd:PRK09406 296 DPTDPDTDVGPLATEQGRDEVEKQVDdAVAAGATILCGGkrPD---------GPGWFYPPTVI-TDITPDMRLYTEEVFG 365
|
410 420 430
....*....|....*....|....*....|....*
gi 1816981345 404 PISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPA 438
Cdd:PRK09406 366 PVASLYRVADIDEAIEIANATTFGLGSNAWTRDEA 400
|
|
| R_hydratase |
cd03449 |
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ... |
539-664 |
5.82e-18 |
|
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.
Pssm-ID: 239533 [Multi-domain] Cd Length: 128 Bit Score: 80.28 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 539 LQIGDT--VVggpRVVSLEDIDHFAEFTGDTFYAHTDPKAAAENpLFGGIVAHGYLVVSLAAGLFVEPNPGPvlanfgvd 616
Cdd:cd03449 1 LKVGDSasLT---RTITEEDVELFAELSGDFNPIHLDEEYAKKT-RFGGRIAHGMLTASLISAVLGTLLPGP-------- 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1816981345 617 G-------LRFLTPVKAGDALTVTLTAKQVTPrlsaDYGEVRWDAVVANQNDDPV 664
Cdd:cd03449 69 GtiylsqsLRFLRPVFIGDTVTATVTVTEKRE----DKKRVTLETVCTNQNGEVV 119
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
25-436 |
6.42e-18 |
|
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: 87.00 E-value: 6.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 25 NASTGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDSGIDID 102
Cdd:cd07150 5 NPADGSVYARVAVGSRqDAERAIAAAYD-AFPAWAATTPSERERILLKAAEIMERRADDLIDLLIDeGGSTYGKAWFETT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 103 GGIgTLLSYASKGTRELPNDTIyldgglePLGRGGTFvgQHIYTSRPGVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVK 182
Cdd:cd07150 84 FTP-ELLRAAAGECRRVRGETL-------PSDSPGTV--SMSVRRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 183 PAHQTaYLTELVVRAIVESGLLPEGSIQLLCASPRALLDHLDGQ---DTVLFTGSAST----ASKLRGH--PNVVE-GG- 251
Cdd:cd07150 154 PSEET-PVIGLKIAEIMEEAGLPKGVFNVVTGGGAEVGDELVDDprvRMVTFTGSTAVgreiAEKAGRHlkKITLElGGk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 252 --VRFNAEADslncsilgPDAAKDTPEFELYIKQlvaemttkaGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPN 329
Cdd:cd07150 233 npLIVLADAD--------LDYAVRAAAFGAFMHQ---------GQICMSASRIIVEEPVYDEFVKKFVARASKLKVGDPR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 330 AEGVRMGPLASLDQREEVLRSLkslrdsatvvfgdpDDFSVEGADA-----SSGAFLPPLLLRAQDSAAAAIHEvEAFGP 404
Cdd:cd07150 296 DPDTVIGPLISPRQVERIKRQV--------------EDAVAKGAKLltggkYDGNFYQPTVLTDVTPDMRIFRE-ETFGP 360
|
410 420 430
....*....|....*....|....*....|..
gi 1816981345 405 ISTVIGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07150 361 VTSVIPAKDAEEALELANDTEYGLSAAILTND 392
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
43-443 |
2.21e-17 |
|
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: 84.94 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 43 AAAIAYgrevggPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TGATAKDSGIDIDGGIGTLLSYASKGTRelpn 121
Cdd:cd07105 8 AAAAAF------PAWSKTPPSERRDILLKAADLLESRRDEFIEAMMEeTGATAAWAGFNVDLAAGMLREAASLITQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 122 dtiyLDGGLEPLGRGGT--FVGQHIYtsrpGVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIV 199
Cdd:cd07105 78 ----IIGGSIPSDKPGTlaMVVKEPV----GVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVFH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 200 ESGLlPEGSIQLLCASP-------RALLDHlDGQDTVLFTGS-------ASTASKlrgH--PNVVE-GGVrfnaeadslN 262
Cdd:cd07105 150 EAGL-PKGVLNVVTHSPedapevvEALIAH-PAVRKVNFTGStrvgriiAETAAK---HlkPVLLElGGK---------A 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 263 CSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHpnaegVRMGPLASLD 342
Cdd:cd07105 216 PAIVLEDA-----DLDAAANAALFGAFLNSGQICMSTERIIVHESIADEFVEKLKAAAEKLFAGP-----VVLGSLVSAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 343 QREEVLRSLKS-LRDSATVVFGDPDDFSvegadaSSGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLA 421
Cdd:cd07105 286 AADRVKELVDDaLSKGAKLVVGGLADES------PSGTSMPPTIL-DNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIA 358
|
410 420
....*....|....*....|..
gi 1816981345 422 ARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07105 359 NDSEYGLSAAVFTRDLARALAV 380
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
9-447 |
2.45e-17 |
|
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: 85.48 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 9 VSGKwiapegeSIPLINASTGEEVARFASG-SLDVAAAIAYGREV--GGPALRALTFHQRaGALkaLGKL--LMSRkEEF 83
Cdd:cd07141 19 VSGK-------TFPTINPATGEKICEVQEGdKADVDKAVKAARAAfkLGSPWRTMDASER-GRL--LNKLadLIER-DRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 YPSSTATGATAK----DSGIDIDGGIGTLLSYASKGTRELPNdTIYLDGGLeplgrggtfvgqHIYT-SRP-GVAVQINA 157
Cdd:cd07141 88 YLASLETLDNGKpfskSYLVDLPGAIKVLRYYAGWADKIHGK-TIPMDGDF------------FTYTrHEPvGVCGQIIP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 158 FNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLL----CASPRALLDHLDgQDTVLFTG 233
Cdd:cd07141 155 WNFPLLMAAWKLAPALACGNTVVLKPAEQTP-LTALYLASLIKEAGFPPGVVNVVpgygPTAGAAISSHPD-IDKVAFTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 234 S---------ASTASKLRghpnvveggvRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALV 304
Cdd:cd07141 233 StevgkliqqAAGKSNLK----------RVTLELGGKSPNIVFADA-----DLDYAVEQAHEALFFNMGQCCCAGSRTFV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 305 PNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDsatvvfgdpddfsvEGAD--------AS 376
Cdd:cd07141 298 QESIYDEFVKRSVERAKKRVVGNPFDPKTEQGPQIDEEQFKKILELIESGKK--------------EGAKlecggkrhGD 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816981345 377 SGAFLPPLLLR-AQDSAAAAIHEVeaFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGV 447
Cdd:cd07141 364 KGYFIQPTVFSdVTDDMRIAKEEI--FGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNAL 433
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
7-411 |
3.22e-17 |
|
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: 84.96 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 7 SYVSGKWIApEGESIPLIN-ASTGEEVARFASGSLDVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRKEEFYP 85
Cdd:TIGR01238 40 PIIGHSYKA-DGEAQPVTNpADRRDIVGQVFHANLAHVQAAIDSAQQAFPTWNATPAKERAAKLDRLADLLELHMPELMA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 -SSTATGATAKDSGIDIDGGIGTLLSYASKGTRELPNDTIyldgglEPLGrggtfvgqhiytsrpgVAVQINAFNFPVWG 164
Cdd:TIGR01238 119 lCVREAGKTIHNAIAEVREAVDFCRYYAKQVRDVLGEFSV------ESRG----------------VFVCISPWNFPLAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 165 MLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLC---ASPRALLDHLDGQDTVLFTGSASTASKL 241
Cdd:TIGR01238 177 FTGQISAALAAGNTVIAKPAEQTSLIAYRAVELMQEAGF-PAGTIQLLPgrgADVGAALTSDPRIAGVAFTGSTEVAQLI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 242 -RGHPNVVEGGVRFNAEADSLNCSILGPDAAKdtpefELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRL 320
Cdd:TIGR01238 256 nQTLAQREDAPVPLIAETGGQNAMIVDSTALP-----EQVVRDVLRSAFDSAGQRCSALRVLCVQEDVADRVLTMIQGAM 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 321 SKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPDDFSVegaDASSGAFLPPLLLRAQDSAAAaihEVE 400
Cdd:TIGR01238 331 QELKVGVPHLLTTDVGPVIDAEAKQNLLAHIEHMSQTQKKIAQLTLDDSR---ACQHGTFVAPTLFELDDIAEL---SEE 404
|
410
....*....|.
gi 1816981345 401 AFGPISTVIGY 411
Cdd:TIGR01238 405 VFGPVLHVVRY 415
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
18-444 |
5.69e-17 |
|
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: 84.27 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 18 GESIPLINASTGEEVARfasgslDVAAAIAYGREVGGPalralTFHQRAGALKALGKLLMSRKEEFypsstaTGATAKDS 97
Cdd:cd07098 6 GQHLGSVPADTPEDVDE------AIAAARAAQREWAKT-----SFAERRKVLRSLLKYILENQEEI------CRVACRDT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 98 G-IDIDGGIGTLLSYASKGTRELPNDtiylDGGLEPLGRGGTFVGQHiYTSR----P-GVAVQINAFNFPVWGMLEKLAP 171
Cdd:cd07098 69 GkTMVDASLGEILVTCEKIRWTLKHG----EKALRPESRPGGLLMFY-KRARveyePlGVVGAIVSWNYPFHNLLGPIIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 172 AFLAGVPSIVKPAHQTAYLTEL---VVRAIVESGLLPEGSIQLLCASPR---ALLDHlDGQDTVLFTGSASTASKLrghp 245
Cdd:cd07098 144 ALFAGNAIVVKVSEQVAWSSGFflsIIRECLAACGHDPDLVQLVTCLPEtaeALTSH-PVIDHITFIGSPPVGKKV---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 246 nvveggvrFNAEADSLNCSIL---GPDAAKDTPEFEL-YIKQLVAEMT-TKAGQKCTAIRRALVPNELVDDVVEATRTRL 320
Cdd:cd07098 219 --------MAAAAESLTPVVLelgGKDPAIVLDDADLdQIASIIMRGTfQSSGQNCIGIERVIVHEKIYDKLLEILTDRV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 321 SKVVVGHPNAEGVRMGPL---ASLDQREEVLRSlkSLRDSATVVFGDPddfSVEGADASSGAFLPPLLLrAQDSAAAAIH 397
Cdd:cd07098 291 QALRQGPPLDGDVDVGAMispARFDRLEELVAD--AVEKGARLLAGGK---RYPHPEYPQGHYFPPTLL-VDVTPDMKIA 364
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1816981345 398 EVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07098 365 QEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIA 411
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
6-421 |
1.16e-16 |
|
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: 83.27 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 6 ESYVSGKWIAP-EGESIPLINASTGE---EVARfaSGSLDVAAAIAYGREVGgPALRALTFHQRAGALKALGKLLMSRKE 81
Cdd:cd07116 2 DNFIGGEWVAPvKGEYFDNITPVTGKvfcEVPR--STAEDIELALDAAHAAK-EAWGKTSVAERANILNKIADRMEANLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 82 EFypsstatgATAKDsgidIDGGigtllsyasKGTRELPNDTIYL---------------DGGLEPLGrgGTFVGQHIYt 146
Cdd:cd07116 79 ML--------AVAET----WDNG---------KPVRETLAADIPLaidhfryfagciraqEGSISEID--ENTVAYHFH- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 147 sRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESgLLPEGSIQL-----------LCA 214
Cdd:cd07116 135 -EPlGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTP-ASILVLMELIGD-LLPPGVVNVvngfgleagkpLAS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 215 SPRAlldhldgqDTVLFTGSASTASKLRGH------PNVVE-GGVRFNAEADSLncsilgpdAAKDTPEFELYIKQLVAe 287
Cdd:cd07116 212 SKRI--------AKVAFTGETTTGRLIMQYaseniiPVTLElGGKSPNIFFADV--------MDADDAFFDKALEGFVM- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 288 MTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPDD 367
Cdd:cd07116 275 FALNQGEVCTCPSRALIQESIYDRFMERALERVKAIKQGNPLDTETMIGAQASLEQLEKILSYIDIGKEEGAEVLTGGER 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1816981345 368 FSVEGaDASSGAFLPPLLLRAQDsaaAAIHEVEAFGPISTVIGYSDVDDAIQLA 421
Cdd:cd07116 355 NELGG-LLGGGYYVPTTFKGGNK---MRIFQEEIFGPVLAVTTFKDEEEALEIA 404
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
28-443 |
1.36e-16 |
|
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: 82.74 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 28 TGEEVARFASGSL-DVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYP-SSTATGATAKDSGIDIDGGI 105
Cdd:cd07101 5 TGEPLGELPQSTPaDVEAAFARARA-AQRAWAARPFAERAAVFLRFHDLVLERRDELLDlIQLETGKARRHAFEEVLDVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 106 GTLLSYASKGTRELpndtiyldgglEPLGRGGT--FVGQHIYTSRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVK 182
Cdd:cd07101 84 IVARYYARRAERLL-----------KPRRRRGAipVLTRTTVNRRPkGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 183 PAHQTAYLTELVVRAIVESGlLPEGSIQLLCASPR----ALLDHLDGqdtVLFTGSAST--------ASKLRGhpnvveg 250
Cdd:cd07101 153 PDSQTALTALWAVELLIEAG-LPRDLWQVVTGPGSevggAIVDNADY---VMFTGSTATgrvvaeraGRRLIG------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 251 gvrFNAEADSLNCSILGPDAAKDTPEfelyiKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNA 330
Cdd:cd07101 222 ---CSLELGGKNPMIVLEDADLDKAA-----AGAVRACFSNAGQLCVSIERIYVHESVYDEFVRRFVARTRALRLGAALD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 331 EGVRMGPLASLDQREEVLRSLKSLRDS-ATVVFGD---PDdfsvegadaSSGAFLPPLLLRAQDsAAAAIHEVEAFGPIS 406
Cdd:cd07101 294 YGPDMGSLISQAQLDRVTAHVDDAVAKgATVLAGGrarPD---------LGPYFYEPTVLTGVT-EDMELFAEETFGPVV 363
|
410 420 430
....*....|....*....|....*....|....*..
gi 1816981345 407 TVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07101 364 SIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRI 400
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
150-443 |
1.97e-16 |
|
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: 82.29 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLcaspraLLDHLDGQ--- 226
Cdd:cd07102 118 GVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAGL-PEGVFQVL------HLSHETSAali 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 227 -----DTVLFTGSastasklrghpnvVEGGVR-FNAEAD---SLNCSILGPDAA--KDTPEFELYIKQLVAEMTTKAGQK 295
Cdd:cd07102 191 adpriDHVSFTGS-------------VAGGRAiQRAAAGrfiKVGLELGGKDPAyvRPDADLDAAAESLVDGAFFNSGQS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 296 CTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPDDFSVegaDA 375
Cdd:cd07102 258 CCSIERIYVHESIYDAFVEAFVAVVKGYKLGDPLDPSTTLGPVVSARAADFVRAQIADAIAKGARALIDGALFPE---DK 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1816981345 376 SSGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07102 335 AGGAYLAPTVLTNVDHSMRVMRE-ETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEAL 401
|
|
| MaoC_dehydratas |
pfam01575 |
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ... |
549-634 |
3.60e-16 |
|
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.
Pssm-ID: 396243 [Multi-domain] Cd Length: 123 Bit Score: 75.07 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 549 PRVVSLEDIDHFAEFTGDTFYAHTDPKAAAEnPLFGGIVAHGYLVVSLAAGLFVEPNPGPVLANFGVDGLRFLTPVKAGD 628
Cdd:pfam01575 15 PRTVTEADIALFALVSGDHNPIHVDPEFAKK-AGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVRFTKPVFPGD 93
|
....*.
gi 1816981345 629 ALTVTL 634
Cdd:pfam01575 94 TLRTEA 99
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
18-443 |
4.19e-16 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 81.85 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 18 GESIPLINASTGEEVARF-ASGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFYPSSTA-TG---A 92
Cdd:PRK09407 31 GPTREVTAPFTGEPLATVpVSTAADVEAAFARARA-AQRAWAATPVRERAAVLLRFHDLVLENREELLDLVQLeTGkarR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 93 TAKDSGIDIdggIGTLLSYASKGTRELpndtiyldgglEPLGRGGTF--VGQHIYTSRP-GVAVQINAFNFPVWGMLEKL 169
Cdd:PRK09407 110 HAFEEVLDV---ALTARYYARRAPKLL-----------APRRRAGALpvLTKTTELRQPkGVVGVISPWNYPLTLAVSDA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 170 APAFLAGVPSIVKPAHQTAYLTELVVRAIVESGlLPEGSIQLLCASPR----ALLDHLDGqdtVLFTGSASTASKLRGHp 245
Cdd:PRK09407 176 IPALLAGNAVVLKPDSQTPLTALAAVELLYEAG-LPRDLWQVVTGPGPvvgtALVDNADY---LMFTGSTATGRVLAEQ- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 246 nvveGGVR---FNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSK 322
Cdd:PRK09407 251 ----AGRRligFSLELGGKNPMIVLDDA-----DLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEFVRAFVAAVRA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 323 VVVGHPNAEGVRMGPLASLDQREEVlrslkslrdSATVvfgdpDDFSVEGADASSG---------AFLPPLLLR-AQDSA 392
Cdd:PRK09407 322 MRLGAGYDYSADMGSLISEAQLETV---------SAHV-----DDAVAKGATVLAGgkarpdlgpLFYEPTVLTgVTPDM 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1816981345 393 AAAIHEVeaFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:PRK09407 388 ELAREET--FGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAI 436
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
24-442 |
1.57e-15 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 79.52 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 24 INASTGEEVARFA-SGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMSRKEEFY---------PSSTATGAT 93
Cdd:PRK13968 12 VNPATGEQLSVLPwAGADDIENALQLAAA-GFRDWRETNIDYRAQKLRDIGKALRARSEEMAqmitremgkPINQARAEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 94 AKDSGIdIDGgigtllsYASKGTRELPNdtiyldgglEPlgrggTFV--GQHIYTSRP-GVAVQINAFNFPVWGMLEKLA 170
Cdd:PRK13968 91 AKSANL-CDW-------YAEHGPAMLKA---------EP-----TLVenQQAVIEYRPlGTILAIMPWNFPLWQVMRGAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 171 PAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHLDGQD--TVLFTGSastasklrghpnvV 248
Cdd:PRK13968 149 PILLAGNGYLLKHAPNVMGCAQLIAQVFKDAGI-PQGVYGWLNADNDGVSQMINDSRiaAVTVTGS-------------V 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 249 EGGVRFNAEADSL--NCSI-LG---PDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSK 322
Cdd:PRK13968 215 RAGAAIGAQAGAAlkKCVLeLGgsdPFIVLNDADLELAVKAAVAGRYQNTGQVCAAAKRFIIEEGIASAFTERFVAAAAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 323 VVVGHPNAEGVRMGPLASLDQREEVLRSL-KSLRDSATVVFGDPddfSVEGAdassGAFLPPLLLRAQDSAAAAIHEvEA 401
Cdd:PRK13968 295 LKMGDPRDEENALGPMARFDLRDELHHQVeATLAEGARLLLGGE---KIAGA----GNYYAPTVLANVTPEMTAFRE-EL 366
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1816981345 402 FGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQ 442
Cdd:PRK13968 367 FGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQ 407
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
15-436 |
3.71e-14 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 75.32 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 15 APEGESIPLINASTGEEVARFASG-SLDVAAAIAYGREV--------GGPAlraltfhQRAGALKALGKLLMSRKEEFYP 85
Cdd:PRK09847 31 AAENETFETVDPVTQAPLAKIARGkSVDIDRAVSAARGVfergdwslSSPA-------KRKAVLNKLADLMEAHAEELAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 86 SSTA-TGATAKDS-GIDIDGGIGTLLSYASKGtrelpnDTIYldGGLEPLGRGGTFVgqhIYTSRPGVAVQINAFNFPVW 163
Cdd:PRK09847 104 LETLdTGKPIRHSlRDDIPGAARAIRWYAEAI------DKVY--GEVATTSSHELAM---IVREPVGVIAAIVPWNFPLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 164 GMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLPEGSIQLLCA----SPRALLDHLDgQDTVLFTGSASTAS 239
Cdd:PRK09847 173 LTCWKLGPALAAGNSVILKPSEKSP-LSAIRLAGLAKEAGLPDGVLNVVTGfgheAGQALSRHND-IDAIAFTGSTRTGK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 240 KL---RGHPNVveggVRFNAEADSLNCSILgpdaAKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELVDDVVEAT 316
Cdd:PRK09847 251 QLlkdAGDSNM----KRVWLEAGGKSANIV----FADCPDLQQAASATAAGIFYNQGQVCIAGTRLLLEESIADEFLALL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 317 RTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVfgdpddfsVEGADASSGAFLPPLLLRAQDSAAAAI 396
Cdd:PRK09847 323 KQQAQNWQPGHPLDPATTMGTLIDCAHADSVHSFIREGESKGQLL--------LDGRNAGLAAAIGPTIFVDVDPNASLS 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1816981345 397 HEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:PRK09847 395 RE-EIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRD 433
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
1-447 |
8.37e-14 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 74.78 E-value: 8.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 1 MTAVLESYVSGKWIAPEGES-IPLINASTGEEVARFA-SGSLDVAAAIAYGREvGGPALRALTFHQRAGALKALGKLLMS 78
Cdd:PLN02419 110 MPPRVPNLIGGSFVESQSSSfIDVINPATQEVVSKVPlTTNEEFKAAVSAAKQ-AFPLWRNTPITTRQRVMLKFQELIRK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 79 RKEEFYPS-STATGATAKDSGIDIDGGIGTLLSYASKGTRE----LPNDTIYLD--GGLEPLGrggtfvgqhiytsrpgV 151
Cdd:PLN02419 189 NMDKLAMNiTTEQGKTLKDSHGDIFRGLEVVEHACGMATLQmgeyLPNVSNGVDtySIREPLG----------------V 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 152 AVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGlLPEGSIQLLCASPRALLDHLDGQDTVLF 231
Cdd:PLN02419 253 CAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAG-LPDGVLNIVHGTNDTVNAICDDEDIRAV 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 232 TGSASTASKLRGHPNVVEGGVRFNAEADSLNCSILGPDAAKDTPefelyIKQLVAEMTTKAGQKCTAIRRALVPNELV-- 309
Cdd:PLN02419 332 SFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDAT-----LNALLAAGFGAAGQRCMALSTVVFVGDAKsw 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 310 -DDVVEatRTRLSKVVVG-HPNAEgvrMGPLASLDQREEVLRSLKSLRDSATVVFGDPDDFSVEGADasSGAFLPPLLLR 387
Cdd:PLN02419 407 eDKLVE--RAKALKVTCGsEPDAD---LGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYE--KGNFIGPTILS 479
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 388 AQDSAAAAIHEvEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQVTLGV 447
Cdd:PLN02419 480 GVTPDMECYKE-EIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDI 538
|
|
| PRK08190 |
PRK08190 |
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated |
537-666 |
1.09e-13 |
|
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
Pssm-ID: 236180 [Multi-domain] Cd Length: 466 Bit Score: 73.76 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 537 EELQIGDT--VVggpRVVSLEDIDHFAEFTGDTFYAHTDPkAAAENPLFGGIVAHGYLVVSLAAGLF--VEPNPGPVLAN 612
Cdd:PRK08190 12 DEIAIGDSasLV---RTLTPDDIELFAAMSGDVNPAHLDA-AYAASDGFHHVVAHGMWGGALISAVLgtRLPGPGTIYLG 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1816981345 613 fgvDGLRFLTPVKAGDALTVTLTAKQvtprLSADYGEVRWDAVVANQNDDPVAT 666
Cdd:PRK08190 88 ---QSLRFRRPVRIGDTLTVTVTVRE----KDPEKRIVVLDCRCTNQDGEVVIT 134
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
146-454 |
2.80e-13 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 73.47 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 146 TSRP-GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQL-----------LC 213
Cdd:PRK11809 765 THRPlGPVVCISPWNFPLAIFTGQVAAALAAGNSVLAKPAEQTPLIAAQAVRILLEAGV-PAGVVQLlpgrgetvgaaLV 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 214 ASPRAlldhldgqDTVLFTGSASTASKL----------RGHPnvveggVRFNAEADSLNCSILGPDAAKDtpefelyikQ 283
Cdd:PRK11809 844 ADARV--------RGVMFTGSTEVARLLqrnlagrldpQGRP------IPLIAETGGQNAMIVDSSALTE---------Q 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 284 LVAEMTTK----AGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSAT 359
Cdd:PRK11809 901 VVADVLASafdsAGQRCSALRVLCLQDDVADRTLKMLRGAMAECRMGNPDRLSTDIGPVIDAEAKANIERHIQAMRAKGR 980
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 360 VVFGDPDDfsvEGADASSGAFLPPLLLRAqDSAAAAIHEVeaFGPISTVIGY--SDVDDAI-QLAARGKGslvgslvthd 436
Cdd:PRK11809 981 PVFQAARE---NSEDWQSGTFVPPTLIEL-DSFDELKREV--FGPVLHVVRYnrNQLDELIeQINASGYG---------- 1044
|
330
....*....|....*...
gi 1816981345 437 pavarqVTLGVapfHGRI 454
Cdd:PRK11809 1045 ------LTLGV---HTRI 1053
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
170-455 |
3.26e-13 |
|
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: 72.19 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 170 APAFLAGVPSIVK--PAHqtAYLTELVVRAIV----ESGLlPEGSIQLLCASPRALldhldGQDTVL--------FTGS- 234
Cdd:cd07129 129 ASALAAGCPVVVKahPAH--PGTSELVARAIRaalrATGL-PAGVFSLLQGGGREV-----GVALVKhpaikavgFTGSr 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 235 ------ASTASKlRGHPnvveggVRFNAEADSLNCSILGPDAAKDTPEfELyIKQLVAEMTTKAGQKCTAIRRALVP-NE 307
Cdd:cd07129 201 rggralFDAAAA-RPEP------IPFYAELGSVNPVFILPGALAERGE-AI-AQGFVGSLTLGAGQFCTNPGLVLVPaGP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 308 LVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVlrslkslrDSATVVfgdpddfsVEGADASSGAFLPPLLLR 387
Cdd:cd07129 272 AGDAFIAALAEALAAAPAQTMLTPGIAEAYRQGVEALAAA--------PGVRVL--------AGGAAAEGGNQAAPTLFK 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816981345 388 AqDSAAAAIHEV---EAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTH--DPAVARQVTLGVAPFHGRIL 455
Cdd:cd07129 336 V-DAAAFLADPAlqeEVFGPASLVVRYDDAAELLAVAEALEGQLTATIHGEedDLALARELLPVLERKAGRLL 407
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-436 |
6.57e-13 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 71.33 E-value: 6.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 4 VLESYVSGKW-IAPEGESIPLINASTGEEVARFASGSLDVAAAIAYGREVGGPALRALTFHQRAGALKALGKLLMSRKEE 82
Cdd:PLN00412 15 VYKYYADGEWrTSSSGKSVAITNPSTRKTQYKVQACTQEEVNKAMESAKAAQKAWAKTPLWKRAELLHKAAAILKEHKAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 83 FYPSSTATGAT-AKDSGIDIDGGiGTLLSYASkgtrelpndtiylDGGLEPLGRGG-----TFVG----QHIYTSR-P-G 150
Cdd:PLN00412 95 IAECLVKEIAKpAKDAVTEVVRS-GDLISYTA-------------EEGVRILGEGKflvsdSFPGnernKYCLTSKiPlG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 151 VAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLDHLD---GQD 227
Cdd:PLN00412 161 VVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCFHLAGF-PKGLISCVTGKGSEIGDFLTmhpGVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 228 TVLFTGSASTASKLRGhpnvvEGGVRFNAEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRALVPNE 307
Cdd:PLN00412 240 CISFTGGDTGIAISKK-----AGMVPLQMELGGKDACIVLEDA-----DLDLAAANIIKGGFSYSGQRCTAVKVVLVMES 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 308 LVDDVVEATRTRLSKVVVGHPNAEgVRMGPLASldqreevlrslkslRDSATVVFGDPDDFSVEGADASS-----GAFLP 382
Cdd:PLN00412 310 VADALVEKVNAKVAKLTVGPPEDD-CDITPVVS--------------ESSANFIEGLVMDAKEKGATFCQewkreGNLIW 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1816981345 383 PLLLraqDSAAA--AIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:PLN00412 375 PLLL---DNVRPdmRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRD 427
|
|
| FkbR2 |
cd03451 |
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ... |
537-677 |
1.65e-11 |
|
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.
Pssm-ID: 239535 [Multi-domain] Cd Length: 146 Bit Score: 62.61 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 537 EELQIGDTVVGGP-RVVSLEDIDHFAEFTGDTFYAHTDPKAAAENPlFGGIVAHGYLVVSLAAGLFVEPNPGPVLANFGV 615
Cdd:cd03451 5 EDFTVGQVFEHAPgRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTE-FGRRLVNSLFTLSLALGLSVNDTSLTAVANLGY 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816981345 616 DGLRFLTPVKAGDALTVTLTAKQVTPRLS-ADYGEVRWDAVVANQNDDPVATYDVLTLVAKKN 677
Cdd:cd03451 84 DEVRFPAPVFHGDTLYAESEVLSKRESKSrPDAGIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
89-444 |
7.70e-11 |
|
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: 65.19 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 89 ATGATAKDSGIDIdggigtlLSYASKGTRELPNDTIYLdgglEPLGRGGTFVGQHIYTSRP-GVAVQINAFNFPVWGMLE 167
Cdd:cd07127 144 AGGPHAQDRGLEA-------VAYAWREMSRIPPTAEWE----KPQGKHDPLAMEKTFTVVPrGVALVIGCSTFPTWNGYP 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 168 KLAPAFLAGVPSIVKPaHQTAYL----TELVVRAIV-ESGLLPegSIQLLCASPRA------LLDHLDGQdTVLFTGSAS 236
Cdd:cd07127 213 GLFASLATGNPVIVKP-HPAAILplaiTVQVAREVLaEAGFDP--NLVTLAADTPEepiaqtLATRPEVR-IIDFTGSNA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 237 TASKLRGHPnvveGGVRFNAEADSLNCSILgpdaaKDTPEFELYIKQLVAEMTTKAGQKCTAIRRALVPNELV------- 309
Cdd:cd07127 289 FGDWLEANA----RQAQVYTEKAGVNTVVV-----DSTDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDGIqtddgrk 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 310 --DDVVEATRTRLSKVVVGHPNAEGVrMGPL---ASLDQREEVLRSLKSLRDSATVvfGDPDdfsVEGADASSgaflpPL 384
Cdd:cd07127 360 sfDEVAADLAAAIDGLLADPARAAAL-LGAIqspDTLARIAEARQLGEVLLASEAV--AHPE---FPDARVRT-----PL 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816981345 385 LLRAqDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLA---ARGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07127 429 LLKL-DASDEAAYAEERFGPIAFVVATDSTDHSIELAresVREHGAMTVGVYSTDPEVVERVQ 490
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
150-439 |
1.59e-10 |
|
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: 63.78 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYlTELVVRAIVESGlLPEGSIQLLCASP---RALLDHldGQ 226
Cdd:cd07135 110 GVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPH-TAALLAELVPKY-LDPDAFQVVQGGVpetTALLEQ--KF 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 227 DTVLFTGS-------ASTASKlrgH--PNVVE-GGvrfnaeadsLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKC 296
Cdd:cd07135 186 DKIFYTGSgrvgriiAEAAAK---HltPVTLElGG---------KSPVIVTKNA-----DLELAAKRILWGKFGNAGQIC 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 297 TAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGvRMGPLASLDQREEVLRSLKSLRdsATVVFGDPDDfsvegadaS 376
Cdd:cd07135 249 VAPDYVLVDPSVYDEFVEELKKVLDEFYPGGANASP-DYTRIVNPRHFNRLKSLLDTTK--GKVVIGGEMD--------E 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816981345 377 SGAFLPPlLLRAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAV 439
Cdd:cd07135 318 ATRFIPP-TIVSDVSWDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSE 379
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
158-415 |
4.18e-10 |
|
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: 62.60 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 158 FNFPVWGMLEKLAPAFLAGVpSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPRALLD------HLDGqdtVLF 231
Cdd:cd07123 180 FNFTAIGGNLAGAPALMGNV-VLWKPSDTAVLSNYLVYKILEEAGL-PPGVINFVPGDGPVVGDtvlaspHLAG---LHF 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 232 TGSASTASKL-----------RGHPNVV--EGGVRF-----NAEADSL-NCSILGPdaakdtpeFElYikqlvaemttkA 292
Cdd:cd07123 255 TGSTPTFKSLwkqigenldryRTYPRIVgeTGGKNFhlvhpSADVDSLvTATVRGA--------FE-Y-----------Q 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 293 GQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPL---ASLDQREEVLRSLKSlRDSATVVFGDpddfs 369
Cdd:cd07123 315 GQKCSAASRAYVPESLWPEVKERLLEELKEIKMGDPDDFSNFMGAVideKAFDRIKGYIDHAKS-DPEAEIIAGG----- 388
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1816981345 370 veGADASSGAFLPPLLLRAQDSAAAAIHEvEAFGPISTVIGYSDVD 415
Cdd:cd07123 389 --KCDDSVGYFVEPTVIETTDPKHKLMTE-EIFGPVLTVYVYPDSD 431
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
150-454 |
1.06e-09 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 61.75 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQL-----------LCASPRa 218
Cdd:PRK11904 686 GVFVCISPWNFPLAIFLGQVAAALAAGNTVIAKPAEQTPLIAAEAVKLLHEAGI-PKDVLQLlpgdgatvgaaLTADPR- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 219 lldhLDGqdtVLFTGSASTASKL------RGHPNVVeggvrFNAEADSLNCSILgpdaakDT---PEfelyikQLVAEMT 289
Cdd:PRK11904 764 ----IAG---VAFTGSTETARIInrtlaaRDGPIVP-----LIAETGGQNAMIV------DStalPE------QVVDDVV 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 290 TK----AGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDP 365
Cdd:PRK11904 820 TSafrsAGQRCSALRVLFVQEDIADRVIEMLKGAMAELKVGDPRLLSTDVGPVIDAEAKANLDAHIERMKREARLLAQLP 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 366 ddfsvEGADASSGAFLPPLLLRAQDsaAAAIHEvEAFGPISTVIGY--SDVDDAI-QLAARGKGslvgslvthdpavarq 442
Cdd:PRK11904 900 -----LPAGTENGHFVAPTAFEIDS--ISQLER-EVFGPILHVIRYkaSDLDKVIdAINATGYG---------------- 955
|
330
....*....|..
gi 1816981345 443 VTLGVapfHGRI 454
Cdd:PRK11904 956 LTLGI---HSRI 964
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
150-439 |
1.41e-09 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 61.00 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLT---ELVVRAIVESGLLPEGSIQLLCASprALLDHLDGQ 226
Cdd:PLN02315 156 GIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITiamTKLVAEVLEKNNLPGAIFTSFCGG--AEIGEAIAK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 227 DT----VLFTGSASTASKLRGHPNVVEGGVRFnaEADSLNCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKCTAIRRA 302
Cdd:PLN02315 234 DTriplVSFTGSSKVGLMVQQTVNARFGKCLL--ELSGNNAIIVMDDA-----DIQLAVRSVLFAAVGTAGQRCTTCRRL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 303 LVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSA-TVVFGDpddfsveGADASSGAFL 381
Cdd:PLN02315 307 LLHESIYDDVLEQLLTVYKQVKIGDPLEKGTLLGPLHTPESKKNFEKGIEIIKSQGgKILTGG-------SAIESEGNFV 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816981345 382 PPLLLraQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAV 439
Cdd:PLN02315 380 QPTIV--EISPDADVVKEELFGPVLYVMKFKTLEEAIEINNSVPQGLSSSIFTRNPET 435
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
150-418 |
2.47e-07 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 53.58 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIveSGLLPEGSIQLLCASPRA---LLDHldGQ 226
Cdd:PLN02203 110 GVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANI--PKYLDSKAVKVIEGGPAVgeqLLQH--KW 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 227 DTVLFTGSASTA----SKLRGH--PNVVEGGVRFNAEADSLncsilgpDAAKDTpefELYIKQLV-AEMTTKAGQKCTAI 299
Cdd:PLN02203 186 DKIFFTGSPRVGriimTAAAKHltPVALELGGKCPCIVDSL-------SSSRDT---KVAVNRIVgGKWGSCAGQACIAI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 300 RRALVPNELVDDVVEATRTRLSKVVVGHPNaegvRMGPLASLDQREEVLRSLKSLRDS---ATVVFG---DPDDFSVEga 373
Cdd:PLN02203 256 DYVLVEERFAPILIELLKSTIKKFFGENPR----ESKSMARILNKKHFQRLSNLLKDPrvaASIVHGgsiDEKKLFIE-- 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1816981345 374 dassgaflPPLLLraQDSAAAAIHEVEAFGPISTVIGYSDVDDAI 418
Cdd:PLN02203 330 --------PTILL--NPPLDSDIMTEEIFGPLLPIITVKKIEDSI 364
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
150-426 |
3.11e-07 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 54.10 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLC-----------ASPRA 218
Cdd:PRK11905 678 GPVVCISPWNFPLAIFTGQIAAALVAGNTVLAKPAEQTPLIAARAVRLLHEAGV-PKDALQLLPgdgrtvgaalvADPRI 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 219 lldhldgqDTVLFTGSASTASKL------RGHPNVVeggvrFNAEADSLNCSILGPDAakdTPEfelyikQLVAEMTT-- 290
Cdd:PRK11905 757 --------AGVMFTGSTEVARLIqrtlakRSGPPVP-----LIAETGGQNAMIVDSSA---LPE------QVVADVIAsa 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 291 --KAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSATVVFGDPddf 368
Cdd:PRK11905 815 fdSAGQRCSALRVLCLQEDVADRVLTMLKGAMDELRIGDPWRLSTDVGPVIDAEAQANIEAHIEAMRAAGRLVHQLP--- 891
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816981345 369 svEGADASSGAFLPPLLLRAqDSAAAAIHEVeaFGPISTVIGY--SDVDDAI-QLAARGKG 426
Cdd:PRK11905 892 --LPAETEKGTFVAPTLIEI-DSISDLEREV--FGPVLHVVRFkaDELDRVIdDINATGYG 947
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
138-454 |
3.88e-07 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 53.79 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 138 TFVGQHIYTSRpGVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLlPEGSIQLLCASPR 217
Cdd:COG4230 671 LFAAPTVLRGR-GVFVCISPWNFPLAIFTGQVAAALAAGNTVLAKPAEQTPLIAARAVRLLHEAGV-PADVLQLLPGDGE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 218 ----ALLDH--LDGqdtVLFTGSASTASKL------RGHPNVVeggvrFNAEADSLNCSILgpdaakDT---PEfelyik 282
Cdd:COG4230 749 tvgaALVADprIAG---VAFTGSTETARLInrtlaaRDGPIVP-----LIAETGGQNAMIV------DSsalPE------ 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 283 QLVAEMTT----KAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGPLASLDQREEVLRSLKSLRDSA 358
Cdd:COG4230 809 QVVDDVLAsafdSAGQRCSALRVLCVQEDIADRVLEMLKGAMAELRVGDPADLSTDVGPVIDAEARANLEAHIERMRAEG 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 359 TVVfgdpddFSVE-GADASSGAFLPPLLLRAqDSAAAAIHEVeaFGPISTVIGY--SDVDDAI-QLAARGKGslvgslvt 434
Cdd:COG4230 889 RLV------HQLPlPEECANGTFVAPTLIEI-DSISDLEREV--FGPVLHVVRYkaDELDKVIdAINATGYG-------- 951
|
330 340
....*....|....*....|
gi 1816981345 435 hdpavarqVTLGVapfHGRI 454
Cdd:COG4230 952 --------LTLGV---HSRI 960
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
151-444 |
1.19e-06 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 51.73 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 151 VAVqINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVESGLLPE------------GSIqLLCASPRa 218
Cdd:cd07126 146 VAI-ITPFNFPLEIPALQLMGALFMGNKPLLKVDSKVSVVMEQFLRLLHLCGMPATdvdlihsdgptmNKI-LLEANPR- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 219 lldhldgqdTVLFTGSASTASKLrghPNVVEGGVRFnaEADSLNCSILGPDAAkdtpEFELYIKQLVAEMTTKAGQKCTA 298
Cdd:cd07126 223 ---------MTLFTGSSKVAERL---ALELHGKVKL--EDAGFDWKILGPDVS----DVDYVAWQCDQDAYACSGQKCSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 299 -----IRRALVPNELVDDVVEATRTRlskvvvghpNAEGVRMGPLASLDQrEEVLRSLKSLRD--SATVVFG-----DPD 366
Cdd:cd07126 285 qsilfAHENWVQAGILDKLKALAEQR---------KLEDLTIGPVLTWTT-ERILDHVDKLLAipGAKVLFGgkpltNHS 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 367 DFSVEGADASSGAFLPplLLRAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAA--RGKGSLVGSLVTHDPAVARQVT 444
Cdd:cd07126 355 IPSIYGAYEPTAVFVP--LEEIAIEENFELVTTEVFGPFQVVTEYKDEQLPLVLEAleRMHAHLTAAVVSNDIRFLQEVL 432
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
8-436 |
1.39e-06 |
|
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: 51.34 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 8 YVSGKWI-APEGESIPLINASTGEEVARFASGSL-DVAAAIAYGREV--GGPaLRALTFHQRAGALKALGKLLMSRKEEF 83
Cdd:cd07140 9 FINGEFVdAEGGKTYNTINPTDGSVICKVSLATVeDVDRAVAAAKEAfeNGE-WGKMNARDRGRLMYRLADLMEEHQEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 84 ypsstatgatAKDSGIDiDGGIGTLlsyASKGTRELPNDTI-YLDGGLEPLgRGGTFvgqHIYTSRP------------G 150
Cdd:cd07140 88 ----------ATIESLD-SGAVYTL---ALKTHVGMSIQTFrYFAGWCDKI-QGKTI---PINQARPnrnltltkrepiG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 151 VAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAhQTAYLT-----ELVVRAivesGlLPEGSIQLLCASPR----ALLD 221
Cdd:cd07140 150 VCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPA-QVTPLTalkfaELTVKA----G-FPKGVINILPGSGSlvgqRLSD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 222 HLDGQdTVLFTGSASTASKlrghpnVVEGGVRFNAEADSLNCSILGPDAAKDTPEFELYIKQLVAEMTTKAGQKCTAIRR 301
Cdd:cd07140 224 HPDVR-KLGFTGSTPIGKH------IMKSCAVSNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 302 ALVPNELVDDVVEATRTRLSKVVVGHPNAEGVRMGP---LASLDQREEVLRslKSLRDSATVVFGDpddfsvEGADASSG 378
Cdd:cd07140 297 LFVEESIHDEFVRRVVEEVKKMKIGDPLDRSTDHGPqnhKAHLDKLVEYCE--RGVKEGATLVYGG------KQVDRPGF 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 379 AFLPPLLLRAQDSAAAAIHevEAFGPISTVIGY--SDVDDAIQLAARGKGSLVGSLVTHD 436
Cdd:cd07140 369 FFEPTVFTDVEDHMFIAKE--ESFGPIMIISKFddGDVDGVLQRANDTEYGLASGVFTKD 426
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
150-443 |
4.22e-06 |
|
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: 49.83 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 150 GVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAYLTELVVRAIVEsgLLPEGSIQLLCASPR---ALLDHldGQ 226
Cdd:cd07087 102 GVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPK--YFDPEAVAVVEGGVEvatALLAE--PF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 227 DTVLFTGSASTASKlrghpnVVEggvrfnAEADSL----------NCSILGPDAakdtpEFELYIKQLVAEMTTKAGQKC 296
Cdd:cd07087 178 DHIFFTGSPAVGKI------VME------AAAKHLtpvtlelggkSPCIVDKDA-----NLEVAARRIAWGKFLNAGQTC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 297 TAIRRALVPNELVDDVVEATRTRLSKVvvghpnaegvrMG--PLASLD----------QReevlrsLKSLRDSATVVFGD 364
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEF-----------YGedPKESPDygriinerhfDR------LASLLDDGKVVIGG 303
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816981345 365 pddfsveGADASSGAFLPPLLLraQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQLAARGKGSLVGSLVTHDPAVARQV 443
Cdd:cd07087 304 -------QVDKEERYIAPTILD--DVSPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERV 373
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
144-425 |
7.60e-06 |
|
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: 48.76 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 144 IYTSRpGVAVQINAFNFPVWGMLEKLAPAFLAGVPSIVKPAHQTAyLTELVVRAIVESGLLP------EGSIQLlcasPR 217
Cdd:cd07134 97 RYEPK-GVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTP-HTSAVIAKIIREAFDEdevavfEGDAEV----AQ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 218 ALL----DHldgqdtVLFTGSastasklrghPNVveGGVRFNAEADSLNcSI---LG---PDAAKDTPEFELYIKQLVAE 287
Cdd:cd07134 171 ALLelpfDH------IFFTGS----------PAV--GKIVMAAAAKHLA-SVtleLGgksPTIVDETADLKKAAKKIAWG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 288 MTTKAGQKCTAIRRALVPNELVDDVVEATRTRLSKVVvghpnaeGVRMGPLASLD----------QReevLRSL--KSLR 355
Cdd:cd07134 232 KFLNAGQTCIAPDYVFVHESVKDAFVEHLKAEIEKFY-------GKDAARKASPDlarivndrhfDR---LKGLldDAVA 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816981345 356 DSATVVFGdpddfsveGADASSGAFLPPLLLrAQDSAAAAIHEVEAFGPISTVIGYSDVDDAIQ-LAARGK 425
Cdd:cd07134 302 KGAKVEFG--------GQFDAAQRYIAPTVL-TNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEyINAKPK 363
|
|
| MaoC_dehydrat_N |
pfam13452 |
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ... |
540-666 |
8.64e-04 |
|
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of MaoC dehydratase, pfam01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerize to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together.
Pssm-ID: 433220 [Multi-domain] Cd Length: 132 Bit Score: 39.98 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 540 QIGDTVVGGPRVVSLEDIDHFAEFTGDTFYAHTDPKAAAEnplfggiVAHGYLVVSLAAGLFVEPNPGPVLANFGVDGLR 619
Cdd:pfam13452 2 LIGVEFGPVKYEVERGAIREFARAIGETNPAYWDEAAARA-------AGYGDLPAPPTFLFVLGWDAPGFMEQLGIDLSR 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1816981345 620 FL---------TPVKAGDALTVTLTAKQVTPRLSADYGE-VRWDAVVANQNDDPVAT 666
Cdd:pfam13452 75 LLhgeqrftyhRPLRAGDELTCRSQIADVYDKKGNGALCfVVVETEVTNQRGEPVAT 131
|
|
| hot_dog |
cd03440 |
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ... |
579-666 |
1.70e-03 |
|
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.
Pssm-ID: 239524 [Multi-domain] Cd Length: 100 Bit Score: 38.23 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816981345 579 ENPLFGGIVAHGYLVVSLAAGLFVE-------PNPGPVLANFGVdglRFLTPVKAGDALTVTLTAKQVTPRLsadygeVR 651
Cdd:cd03440 9 PEDIDGGGIVHGGLLLALADEAAGAaaarlggRGLGAVTLSLDV---RFLRPVRPGDTLTVEAEVVRVGRSS------VT 79
|
90
....*....|....*
gi 1816981345 652 WDAVVANQNDDPVAT 666
Cdd:cd03440 80 VEVEVRNEDGKLVAT 94
|
|
| |
