|
Name |
Accession |
Description |
Interval |
E-value |
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
13-423 |
3.63e-146 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 426.40 E-value: 3.63e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 13 WALEPDLPALLSRYWKGWGAhrGELERFGALAGGAAYRLADHVDKEaRPVLVMHDLNGNRIDRVRLSPAQEVLNREL--- 89
Cdd:cd01154 1 YLDDPVLQQTLRYFGDPEEE--PDLSRLGELAGGELYELARLADRN-PPVLEMWDRWGRRVDRVWVHPAWHALMRRLiee 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 90 --AAINRAPYQGGSWHLHFAMGYLLADP--GLYCIQTITNATVYAIHKYAPQFANWKEELLAGQA-----FGATWMTEVQ 160
Cdd:cd01154 78 gvINIEDGPAGEGRRHVHFAAGYLLSDAaaGLLCPLTMTDAAVYALRKYGPEELKQYLPGLLSDRyktglLGGTWMTEKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 161 GGSDLGANRVRA-VPEGPVWRLYGDKYFSSGAgLTDYALVSARPEGAPAGPKGVALFLVPRLDSKGGLN-YRVRRLKDKL 238
Cdd:cd01154 158 GGSDLGANETTAeRSGGGVYRLNGHKWFASAP-LADAALVLARPEGAPAGARGLSLFLVPRLLEDGTRNgYRIRRLKDKL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 239 ATRAVPSGEVDFEGSEAHLVGRAEEGIYYILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPLIRRDL 318
Cdd:cd01154 237 GTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 319 TDLAVRIAGGLALTFRAVAAWDEAWLLTPpytPRYHYARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAIARLAR 398
Cdd:cd01154 317 AEMEVDVEAATALTFRAARAFDRAAADKP---VEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHR 393
|
410 420
....*....|....*....|....*
gi 2315639808 399 EALITPIWEGPANVQALDTLEVLFR 423
Cdd:cd01154 394 EAQVTPIWEGTGNIQALDVLRVLVK 418
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
81-415 |
2.24e-66 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 217.92 E-value: 2.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 81 AQEVLNRELAAINRAPYQGG--SWHLHFAMGYLLAdpglyciqtitnatVYAIHKYAP--QFANWKEELLAGQAFGATWM 156
Cdd:cd00567 10 AREFAAEELEPYARERRETPeePWELLAELGLLLG--------------AALLLAYGTeeQKERYLPPLASGEAIAAFAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 157 TEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYALVSARPEGAPAGPKGVALFLVPRlDSKGglnYRVRRLKD 236
Cdd:cd00567 76 TEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEGPGHRGISAFLVPA-DTPG---VTVGRIWD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 237 KLATRAVPSGEVDFEG---SEAHLVGRAEEGIYYILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPL 313
Cdd:cd00567 152 KMGMRGSGTGELVFDDvrvPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 314 IRRDLTDLAVRIAGGLALTFRAVAAWDEAWlltppytpryHYARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAI 393
Cdd:cd00567 232 VQFKLADMAAELEAARLLLYRAAWLLDQGP----------DEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPV 301
|
330 340
....*....|....*....|..
gi 2315639808 394 ARLAREALITPIWEGPANVQAL 415
Cdd:cd00567 302 ERYLRDARAARIAEGTAEIQRL 323
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
98-426 |
1.60e-64 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 214.70 E-value: 1.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 98 QGGSWHLHFAMGYLL--ADPGLYCIQTITNATVYAIHKYA--PQFANWKEELLAGQAFGATWMTEVQGGSDLGANRVRAV 173
Cdd:COG1960 62 LGLSLVELALVLEELarADASLALPVGVHNGAAEALLRFGteEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 174 PEGPVWRLYGDKYFSSGAGLTDYALVSARPEGAPaGPKGVALFLVPRlDSKGglnYRVRRLKDKLATRAVPSGEVDFEG- 252
Cdd:COG1960 142 RDGDGYVLNGQKTFITNAPVADVILVLARTDPAA-GHRGISLFLVPK-DTPG---VTVGRIEDKMGLRGSDTGELFFDDv 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 253 --SEAHLVGRAEEGIYYILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLA 330
Cdd:COG1960 217 rvPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 331 LTFRAVAAWDEAwlltppytpryHYARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAIARLAREALITPIWEGPA 410
Cdd:COG1960 297 LVYRAAWLLDAG-----------EDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTN 365
|
330
....*....|....*.
gi 2315639808 411 NVQALDTLEVLFRKGA 426
Cdd:COG1960 366 EIQRLIIARRLLGRPG 381
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
61-435 |
1.94e-48 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 175.71 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 61 PVLVMHDLNGNRIDRVRLSPAQEVLNRELAAiNRA---PYQ----GGSWHLHFAMGYLLA--DPGLYCIQTITNATVYAI 131
Cdd:PRK11561 67 PELLRYDAQGQRLDDVRFHPAWHLLMQGLCA-NRVhnlAWEedarSGAFVARAARFMLHAqvEAGTLCPITMTFAATPLL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 132 HKYAPQ-FANWKEELL----------AGQAFG---ATWMTEVQGGSDLGANRVRAVP-EGPVWRLYGDKYFSSgAGLTDY 196
Cdd:PRK11561 146 LQMLPApFQDWLTPLLsdrydshllpGGQKRGlliGMGMTEKQGGSDVLSNTTRAERlADGSYRLVGHKWFFS-VPQSDA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 197 ALVSARPEGapagpkGVALFLVPRLDSKGGLN-YRVRRLKDKLATRAVPSGEVDFEGSEAHLVGRAEEGIYYILETLTLS 275
Cdd:PRK11561 225 HLVLAQAKG------GLSCFFVPRFLPDGQRNaIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMT 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 276 RLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEawlltpPYTPRYH- 354
Cdd:PRK11561 299 RFDCALGSHGLMRRAFSVAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDR------RADAKEAl 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 355 YARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAIARLAREALITPIWEGPANVQALDTLEVLFRK-GAAEPFEAE 433
Cdd:PRK11561 373 WARLFTPAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQpGVYDLLSEA 452
|
..
gi 2315639808 434 FG 435
Cdd:PRK11561 453 FV 454
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
137-424 |
3.64e-41 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 152.93 E-value: 3.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 137 QFANWKEELLAGQAFGATWMTEVQGGSDLGANRVRAVPEG-PVWRLYGDKYF-SSGAGLTD---YALVSARPEGAPAGPK 211
Cdd:cd01153 104 QREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQAdGSWRINGVKRFiSAGEHDMSeniVHLVLARSEGAPPGVK 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 212 GVALFLVPRLDSKGGLN-YRVRRLKDKLATRAVPSGEVDFEGSEAHLVGRAEEGIYYILETLTLSRLANAAGAMGLARKA 290
Cdd:cd01153 184 GLSLFLVPKFLDDGERNgVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 291 QLEALFRSEARVAFGKRLQE--------HPLIRRDLTDLAVRIAGGLALTFRAVAAWDEAWLLTPPYTPRYH---YARLL 359
Cdd:cd01153 264 YLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAERKATEGEDRKAlsaLADLL 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2315639808 360 AHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAIARLAREALITPIWEGPANVQALDtleVLFRK 424
Cdd:cd01153 344 TPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALD---LIGRK 405
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
132-415 |
5.42e-36 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 137.78 E-value: 5.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 132 HKYAPQFAnwkeellAGQAFGATWMTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYALVSARpEGAPAGPK 211
Cdd:cd01158 102 KKYLPPLA-------TGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAV-TDPSKGYR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 212 GVALFLVPRlDSKGglnYRVRRLKDKLATRAVPSGEVDFEG---SEAHLVGRAEEGIYYILETLTLSRLANAAGAMGLAR 288
Cdd:cd01158 174 GITAFIVER-DTPG---LSVGKKEDKLGIRGSSTTELIFEDvrvPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 289 KAQLEALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEAwlltPPYTPRYHYARLLAhlakartA 368
Cdd:cd01158 250 AALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNG----EPFIKEAAMAKLFA-------S 318
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2315639808 369 EHGTYCTQLAMELFGGVGFVEDFAIARLAREALITPIWEGPANVQAL 415
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRL 365
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
137-408 |
2.20e-29 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 119.14 E-value: 2.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 137 QFANWKEELLAGQAFGATWMTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYALVSARPEGAPAGPKGVALF 216
Cdd:cd01160 99 QKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEARGAGGISLF 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 217 LVPRlDSKGglnYRVRRLKDKLATRAVPSGEVDFEGSE---AHLVGRAEEGIYYILETLTLSRLANAAGAMGLARKAQLE 293
Cdd:cd01160 179 LVER-GTPG---FSRGRKLKKMGWKAQDTAELFFDDCRvpaENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 294 ALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAvaawdeAWLLTPPYTPRYHyarllAHLAKARTAEHGTY 373
Cdd:cd01160 255 TRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNC------AWRHEQGRLDVAE-----ASMAKYWATELQNR 323
|
250 260 270
....*....|....*....|....*....|....*
gi 2315639808 374 CTQLAMELFGGVGFVEDFAIARLAREALITPIWEG 408
Cdd:cd01160 324 VAYECVQLHGGWGYMREYPIARAYRDARVQPIYGG 358
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
263-413 |
2.77e-28 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 110.04 E-value: 2.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 263 EGIYYILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEA 342
Cdd:pfam00441 2 RGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2315639808 343 wlltppytpryHYARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAIARLAREALITPIWEGPANVQ 413
Cdd:pfam00441 82 -----------GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQ 141
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
119-408 |
1.24e-24 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 105.57 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 119 CIQTIT-NATVYAIHKYAPQfanwkeeLLAGQAFGATWMTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYA 197
Cdd:cd01156 91 CINQIYrNGSAAQKEKYLPK-------LISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 198 LVSARpEGAPAGPKGVALFLVPRldSKGGLNyRVRRLkDKLATRAVPSGEVDFEG---SEAHLVGRAEEGIYYILETLTL 274
Cdd:cd01156 164 VVYAK-TDPSAGAHGITAFIVEK--GMPGFS-RAQKL-DKLGMRGSNTCELVFEDcevPEENILGGENKGVYVLMSGLDY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 275 SRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEAwlltppytpryH 354
Cdd:cd01156 239 ERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRG-----------N 307
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2315639808 355 YARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAIARLAREALITPIWEG 408
Cdd:cd01156 308 MDPKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAG 361
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
113-408 |
2.45e-23 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 101.75 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 113 ADPGLYCIQTITNATVYAIHKYAP--QFANWKEELLAGQAFGATWMTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSG 190
Cdd:cd01162 75 GCVSTAAYISIHNMCAWMIDSFGNdeQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISG 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 191 AGLTDYALVSARPEGapAGPKGVALFLVPrldsKGGLNYRVRRLKDKLATRAVPSGEVDFEG---SEAHLVGRAEEGIYY 267
Cdd:cd01162 155 AGDSDVYVVMARTGG--EGPKGISCFVVE----KGTPGLSFGANEKKMGWNAQPTRAVIFEDcrvPVENRLGGEGQGFGI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 268 ILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEAwlltp 347
Cdd:cd01162 229 AMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRG----- 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2315639808 348 pyTPRyhyARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAIARLAREALITPIWEG 408
Cdd:cd01162 304 --DPD---AVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEG 359
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
153-251 |
4.62e-20 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 85.02 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 153 ATWMTEVQGGSDLGANRVRAVP-EGPVWRLYGDKYFSSGAGLTDYALVSARPEGaPAGPKGVALFLVPRldSKGGLnyRV 231
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADgDGGGWVLNGTKWWITNAGIADLFLVLARTGG-DDRHGGISLFLVPK--DAPGV--SV 75
|
90 100
....*....|....*....|
gi 2315639808 232 RRLKDKLATRAVPSGEVDFE 251
Cdd:pfam02770 76 RRIETKLGVRGLPTGELVFD 95
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
157-400 |
2.77e-18 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 86.71 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 157 TEVQGGSDLGANRVRAV-PEGPVWrLYGDKYFSSGAGLTDYALVSARPEGAPAGPKGVALFLVPrLDSKGglnYRVRRLK 235
Cdd:PRK12341 125 TEPGAGSDNNSATTTYTrKNGKVY-LNGQKTFITGAKEYPYMLVLARDPQPKDPKKAFTLWWVD-SSKPG---IKINPLH 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 236 dKLATRAVPSGEV---DFEGSEAHLVGRAEEGIYYILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHP 312
Cdd:PRK12341 200 -KIGWHMLSTCEVyldNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQ 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 313 LIRRDLTDLAVRIAGGLALTFRavAAWDEAWLLTppytpryhyARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFA 392
Cdd:PRK12341 279 LIQEKLTLMAIKIENMRNMVYK--VAWQADNGQS---------LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEAR 347
|
....*...
gi 2315639808 393 IARLAREA 400
Cdd:PRK12341 348 VSRFWRDV 355
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
156-415 |
4.24e-18 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 86.10 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 156 MTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYALVSARPEGAPAGPKGVAL--FLVPRlDSKGglnYRVRR 233
Cdd:cd01157 120 VTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKCPASKAFtgFIVEA-DTPG---IQPGR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 234 LKDKLATRAVPSGEVDFEG----SEAHLVGRAEeGIYYILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQ 309
Cdd:cd01157 196 KELNMGQRCSDTRGITFEDvrvpKENVLIGEGA-GFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 310 EHPLIRRDLTDLAVRIAGGLALTFRAvaawdeAWLLTPPYTPRYHyarllAHLAKARTAEHGTYCTQLAMELFGGVGFVE 389
Cdd:cd01157 275 EHQAVSFMLADMAMKVELARLAYQRA------AWEVDSGRRNTYY-----ASIAKAFAADIANQLATDAVQIFGGNGFNS 343
|
250 260
....*....|....*....|....*.
gi 2315639808 390 DFAIARLAREALITPIWEGPANVQAL 415
Cdd:cd01157 344 EYPVEKLMRDAKIYQIYEGTSQIQRL 369
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
116-470 |
4.43e-17 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 84.53 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 116 GLYCIQTITNATVYAIHKYAPQFANWKEELLAGQAFGATWMTEVQGGSDLGANRVRAVPEGP-VWRLYGDKYFSSgAGLT 194
Cdd:PTZ00456 147 SMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDH 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 195 DYA-----LVSARPEGAPAGPKGVALFLVPR--LDSKGGL----NYRVRRLKDKLATRAVPSGEVDFEGSEAHLVGRAEE 263
Cdd:PTZ00456 226 DLTenivhIVLARLPNSLPTTKGLSLFLVPRhvVKPDGSLetakNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 264 GIYYILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAF------------GKRLQEHPLIRRDLtdlavriagglaL 331
Cdd:PTZ00456 306 GMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNI------------L 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 332 TFRAVAAWDEAWLLTPPYTPRYHYARLLAHLAKARTAEHGTYCTQL--------------AMELFGGVGFVEDFAIARLA 397
Cdd:PTZ00456 374 FAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAkgcltewgveaasrCLQVWGGHGYIKGNGMEQIL 453
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2315639808 398 REALITPIWEGPANVQALDTL--EVLFRKGAAEpfEAEFGRMLEAagteearLARSRL--QRTLA-HLRTLSQEEAQW 470
Cdd:PTZ00456 454 RDARIGTLYEGTTGIQALDFIgrKVLSLKGGNE--VARFGKRVSK-------LVRAHLfsRGALGqYARRLWLLQKQW 522
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
124-415 |
1.42e-16 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 81.64 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 124 TNATVYAIHKY--APQFANWKEELLAGQAFGATWMTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYALVSA 201
Cdd:cd01151 98 SSLVMLPIYDFgsEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 202 RPEGApAGPKGvalFLVPRldSKGGLnyRVRRLKDKLATRAVPSGEVDFEG----SEAHLVGraEEGIYYILETLTLSRL 277
Cdd:cd01151 178 RNDET-GKIRG---FILER--GMKGL--SAPKIQGKFSLRASITGEIVMDNvfvpEENLLPG--AEGLRGPFKCLNNARY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 278 ANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEAwLLTPPytpryhyar 357
Cdd:cd01151 248 GIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQG-KATPE--------- 317
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 358 lLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDFAIAR--LAREALITpiWEGPANVQAL 415
Cdd:cd01151 318 -QISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRhmVNLESVNT--YEGTHDIHAL 374
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
119-425 |
3.53e-16 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 80.69 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 119 CI-QTITNATVYAIHKYAPQfanwkeeLLAGQAFGATWMTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYA 197
Cdd:PLN02519 117 CInQLVRNGTPAQKEKYLPK-------LISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 198 LVSARPEGApAGPKGVALFLVprldSKGGLNYRVRRLKDKLATRAVPSGEVDFEG---SEAHLVGRAEEGIYYILETLTL 274
Cdd:PLN02519 190 VVYAKTDVA-AGSKGITAFII----EKGMPGFSTAQKLDKLGMRGSDTCELVFENcfvPEENVLGQEGKGVYVMMSGLDL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 275 SRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEAWLltppyTPRYH 354
Cdd:PLN02519 265 ERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKV-----DRKDC 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2315639808 355 YARLLAhlakarTAEHGTYCTQLAMELFGGVGFVEDFAIARLAREALITPIWEGPANVQALDTLEVLFRKG 425
Cdd:PLN02519 340 AGVILC------AAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKEE 404
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
137-413 |
9.16e-13 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 69.68 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 137 QFANWKEELLAGQAFGATWMTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYALVSARPEGAPAGPKGVALF 216
Cdd:cd01152 104 QKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVRTDPEAPKHRGISIL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 217 LVPrLDSKGglnYRVRRLKDklATRAVPSGEV---DFEGSEAHLVGRAEEGIYYILETLTLSRLANAAGAmglarKAQLE 293
Cdd:cd01152 184 LVD-MDSPG---VTVRPIRS--INGGEFFNEVfldDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSA-----ATFFE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 294 ALFRSEARV-AFGKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEAWLLTPPytpryhyarllAHLAKARTAEHGT 372
Cdd:cd01152 253 LLLARLLLLtRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAE-----------ASIAKLFGSELAQ 321
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2315639808 373 YCTQLAMELFGGVG-FVEDFAIARLARE-------ALITPIWEGPANVQ 413
Cdd:cd01152 322 ELAELALELLGTAAlLRDPAPGAELAGRweadylrSRATTIYGGTSEIQ 370
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
114-408 |
1.37e-10 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 63.42 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 114 DPGlYCIQTITNATVYAIHKY----APQFANWKEELLAGQAFGATWMTEVQGGSDLGANRVRAVPEG-PVWRLYGDKYFS 188
Cdd:PTZ00461 112 DPG-FCLAYLAHSMLFVNNFYysasPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSnGNYVLNGSKIWI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 189 SGAGLTDYALVSARPEGApagpkgVALFLVprldSKGGLNYRVRRLKDKLATRAVPSGEVDFEG---SEAHLVGRAEEGI 265
Cdd:PTZ00461 191 TNGTVADVFLIYAKVDGK------ITAFVV----ERGTKGFTQGPKIDKCGMRASHMCQLFFEDvvvPAENLLGEEGKGM 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 266 YYILETLTLSRLANAAGAMGLA-RKAQLEALFRSEaRVAFGKRLQEHPLIRRDLTDLAVRIAGGLALTF---RAVAAWDE 341
Cdd:PTZ00461 261 VGMMRNLELERVTLAAMAVGIAeRSVELMTSYASE-RKAFGKPISNFGQIQRYIAEGYADTEAAKALVYsvsHNVHPGNK 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2315639808 342 AWLLTPPytpryhyARLLAHLAKARTAEHgtyctqlAMELFGGVGFVEDFAIARLAREALITPIWEG 408
Cdd:PTZ00461 340 NRLGSDA-------AKLFATPIAKKVADS-------AIQVMGGMGYSRDMPVERLWRDAKLLEIGGG 392
|
|
| AidB_N |
pfam18158 |
Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive ... |
9-149 |
1.31e-09 |
|
Adaptive response protein AidB N-terminal domain; This is the N-terminal domain of Adaptive response protein AidB present in E. coli. AidB is upregulated in response to small doses of DNA-methylating agents initiates a response that mitigates the mutagenic and cytotoxic effects of DNA methylation. Tetramer formation is thought to be carried out by the N-terminal domain.
Pssm-ID: 436317 [Multi-domain] Cd Length: 156 Bit Score: 56.87 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 9 GKNHWALEPDLPALLSRYWKGWgaHRGELERFGALAGGA-AYRLADHVDkEARPVLVMHDLNGNRIDRVRLSPA-----Q 82
Cdd:pfam18158 8 DYNLFASDPALQEAVAREGAAW--ATEALAALGALAGSAeALELARLAN-RNPPQLHTHDRFGRRIDEVEFHPAyhalmA 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2315639808 83 EVLNRELAAINRAPYQGGSWHLHFAMGYLLA--DPGLYCIQTITNATVYAIHKYAPQFANWKEELLAGQ 149
Cdd:pfam18158 85 LAIEAGLHASPWTDARPGAHVARAALFYLHAqvEAGHLCPLTMTYAAVPALRAEPALAEEWLPKLLSRD 153
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
156-399 |
3.41e-06 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 49.44 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 156 MTEVQGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYALVSARPEGAPAGPKGVALFLvprlD-SKGGLnyRVRRL 234
Cdd:PRK03354 124 ITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFV----DmSKPGI--KVTKL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 235 kDKLATRAVPSGEVDF---EGSEAHLVGRAEEGIYYILETLTLSRLANAAGAMGLARKAQLEALFRSEARVAFGKRLQEH 311
Cdd:PRK03354 198 -EKLGLRMDSCCEITFddvELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRF 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 312 PLIRRDLTDLAVRIAGGLALTFRAvaAWDeawlltppyTPRYHYARLLAHLAKARTAEHGTYCTQLAMELFGGVGFVEDF 391
Cdd:PRK03354 277 QLIQEKFAHMAIKLNSMKNMLYEA--AWK---------ADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNH 345
|
....*...
gi 2315639808 392 AIARLARE 399
Cdd:PRK03354 346 RISRFWRD 353
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
141-384 |
5.57e-06 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 48.86 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 141 WKEELLAGQAFGATWmTEVqGGSDLGANRVRAVPEGPVWRLYGDKYFSSGAGLTDYALVSA-RPEGAPAGpkgvalFLVP 219
Cdd:cd01163 95 WFGRVLNGWIFGNAV-SER-GSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSAlDEEGKLVF------AAVP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 220 RlDSKGglnyrVRRLKD--KLATRAVPSGEVDFEG---SEAHLVGRAEEGIYYILETlTLSRLANAAGAMGLARKAQLEA 294
Cdd:cd01163 167 T-DRPG-----ITVVDDwdGFGQRLTASGTVTFDNvrvEPDEVLPRPNAPDRGTLLT-AIYQLVLAAVLAGIARAALDDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315639808 295 L--FRSEARVAF---GKRLQEHPLIRRDLTDLAVRIAGGLALTFRAVAAWDEAWLLTPPYTP-RYHYARLLAHLAKARTA 368
Cdd:cd01163 240 VayVRSRTRPWIhsgAESARDDPYVQQVVGDLAARLHAAEALVLQAARALDAAAAAGTALTAeARGEAALAVAAAKVVVT 319
|
250
....*....|....*.
gi 2315639808 369 EHGTYCTQLAMELFGG 384
Cdd:cd01163 320 RLALDATSRLFEVGGA 335
|
|
| |
