|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
124-529 |
0e+00 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). 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 ACAD 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. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 643.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 124 RAKKTLDLVEEFVEKDCLPAEALFAAQLGHGEQRWNTTPAIMESLTAKARKLGLWNMFLPKNHFaqGAGFSNLEYGLMAE 203
Cdd:cd01155 2 KAQELRARVKAFMEEHVYPAEQEFLEYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSG--LSGLTNLEYAYLAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 204 YLGKSKLAAEGFlslspfsatNNAAPDTGNMEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEIASSDATNIQLDIRR 283
Cdd:cd01155 80 ETGRSFFAPEVF---------NCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 284 EGDEYVLNGSKWWSSGAGDPRCKIYLVMGKTDAQNPNPYRQQSVVLVPAGLPGITIHRMLQVYGYDDAPHGHGHISFTNV 363
Cdd:cd01155 151 DGDDYVINGRKWWSSGAGDPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAPHGHAEITFDNV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 364 RVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARINDerKTPFGQPLAAHGVIVEWLAKSRIEVDAA 443
Cdd:cd01155 231 RVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVS--REAFGKKLAQHGVVAHWIAKSRIEIEQA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 444 RLIVLNAAIKIDRGDAKAALTEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEVHLQQL 523
Cdd:cd01155 309 RLLVLKAAHMIDTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSI 388
|
....*.
gi 816333706 524 GKRENR 529
Cdd:cd01155 389 ARMELK 394
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
135-532 |
9.43e-156 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 465.81 E-value: 9.43e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 135 FVEKDCLPAEALFAaQLGHGEQRWNTTPAiMESLTAKARKLGLWNMFLPKNHFAQ----------------------GAG 192
Cdd:PLN02876 416 FMEDHIYPMENEFY-KLAQSSSRWTVHPE-EERLKELAKKEGLWNLWIPLDSAARarkllfednkhmvsgdsadqllGAG 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 193 FSNLEYGLMAEYLGKSKLAAEGFlslspfsatNNAAPDTGNMEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEIASS 272
Cdd:PLN02876 494 LSNLEYGYLCEIMGRSVWAPQVF---------NCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQVASS 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 273 DATNIQLDIRREGDEYVLNGSKWWSSGAGDPRCKIYLVMGKTDAQNPNpYRQQSVVLVPAGLPGITIHRMLQVYGYDDAP 352
Cdd:PLN02876 565 DATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKTDFNAPK-HKQQSMILVDIQTPGVQIKRPLLVFGFDDAP 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 353 HGHGHISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARINdERKTpFGQPLAAHGVIVEW 432
Cdd:PLN02876 644 HGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRAL-SRKA-FGKLIAQHGSFLSD 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 433 LAKSRIEVDAARLIVLNAAIKIDRGDAKAALTEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIA 512
Cdd:PLN02876 722 LAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIA 801
|
410 420
....*....|....*....|
gi 816333706 513 DGPDEVHLQQLGKRENRRRR 532
Cdd:PLN02876 802 DGPDEVHLGTIAKLELQRAK 821
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
122-532 |
2.04e-102 |
|
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: 314.09 E-value: 2.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 122 SDRAKKTLDLVEEFVEKDCLPAEAlfaaqlghgeqRWNTTPAIMESLTAKARKLGLWNMFLPKNHfaQGAGFSNLEYGLM 201
Cdd:COG1960 6 TEEQRALRDEVREFAEEEIAPEAR-----------EWDREGEFPRELWRKLAELGLLGLTIPEEY--GGLGLSLVELALV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 202 AEYLGKSkLAAEGFlslsPFSATNnaapdtGNMEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDI 281
Cdd:COG1960 73 LEELARA-DASLAL----PVGVHN------GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPG-AGSDAAALRTTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 282 RREGDEYVLNGSKWWSSGAgdPRCKIYLVMGKTDAQNPnpYRQQSVVLVPAGLPGITIHRMLQVYGYDdaPHGHGHISFT 361
Cdd:COG1960 141 VRDGDGYVLNGQKTFITNA--PVADVILVLARTDPAAG--HRGISLFLVPKDTPGVTVGRIEDKMGLR--GSDTGELFFD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 362 NVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARINdERKTpFGQPLAAHGVIVEWLAKSRIEVD 441
Cdd:COG1960 215 DVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAR-EREQ-FGRPIADFQAVQHRLADMAAELE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 442 AARLIVLNAAIKIDRGDAKAAltEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEVHLQ 521
Cdd:COG1960 293 AARALVYRAAWLLDAGEDAAL--EAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRL 370
|
410
....*....|.
gi 816333706 522 QLGKRENRRRR 532
Cdd:COG1960 371 IIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
230-525 |
7.64e-81 |
|
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: 256.44 E-value: 7.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 230 DTGNMEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGDEYVLNGSKWWSSGAGDprCKIYL 309
Cdd:cd00567 41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKDGDGYVLNGRKIFISNGGD--ADLFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 310 VMGKTDaQNPNPYRQQSVVLVPAGLPGITIHRMLQVYGYDdaPHGHGHISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGR 389
Cdd:cd00567 118 VLARTD-EEGPGHRGISAFLVPADTPGVTVGRIWDKMGMR--GSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 390 IHHAMRTIGAAEQAIEWMIARINdERKtPFGQPLAAHGVIVEWLAKSRIEVDAARLIVLNAAIKIDRGDAKAALtEIAQA 469
Cdd:cd00567 195 LLLAAVALGAARAALDEAVEYAK-QRK-QFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARL-EAAMA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 816333706 470 KVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEVHLQQLGK 525
Cdd:cd00567 272 KLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
129-520 |
6.95e-44 |
|
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: 160.13 E-value: 6.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 129 LDLVEEFVEKDCLPaealFAAQLGHGEQrwnttpaIMESLTAKARKLGLWNMFLPKNHfaQGAGFSNLEYGLMAEYLgks 208
Cdd:cd01158 7 RKTVRDFAEKEIAP----LAAEMDEKGE-------FPREVIKEMAELGLMGIPIPEEY--GGAGLDFLAYAIAIEEL--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 209 klaAEGFLSLSPFSATNNAAPDTGnmevLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGDEY 288
Cdd:cd01158 71 ---AKVDASVAVIVSVHNSLGANP----IIKFGTEEQKKKYLPPLATGEKIGAFALSEPG-AGSDAAALKTTAKKDGDDY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 289 VLNGSKWWSSGAGDprCKIYLVMGKTDAqnPNPYRQQSVVLVPAGLPGITI----HRMLQvygyddapHGHG--HISFTN 362
Cdd:cd01158 143 VLNGSKMWITNGGE--ADFYIVFAVTDP--SKGYRGITAFIVERDTPGLSVgkkeDKLGI--------RGSSttELIFED 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 363 VRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARINdERKTpFGQPLAAHGVIVEWLAKSRIEVDA 442
Cdd:cd01158 211 VRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAK-ERKQ-FGKPIADFQGIQFKLADMATEIEA 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 816333706 443 ARLIVLNAAIKIDRGdaKAALTEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEVHL 520
Cdd:cd01158 289 ARLLTYKAARLKDNG--EPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQR 364
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
171-518 |
2.22e-43 |
|
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: 158.76 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 171 KARKLGLWNMFLPKNHfaQGAGFSNLEYGLMAEYLGKSKLAAEGFLSLSpfsatnnaapdtgNMEV--LAKYGNDAQKQQ 248
Cdd:cd01162 40 KAAELGFGGIYIRDDV--GGSGLSRLDASIIFEALSTGCVSTAAYISIH-------------NMCAwmIDSFGNDEQRER 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 249 WLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGDEYVLNGSKWWSSGAGDprCKIYLVMGKTDAQNPnpyRQQSVV 328
Cdd:cd01162 105 FLPDLCTMEKLASYCLTEPG-SGSDAAALRTRAVREGDHYVLNGSKAFISGAGD--SDVYVVMARTGGEGP---KGISCF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 329 LVPAGLPGITIHRMLQVYGYDDAPhgHGHISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMI 408
Cdd:cd01162 179 VVEKGTPGLSFGANEKKMGWNAQP--TRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 409 ARINdERKTpFGQPLAAHGVIVEWLAKSRIEVDAARLIVLNAAIKIDRGDAKAALTeIAQAKVLVPQTALTIIDRAVQSY 488
Cdd:cd01162 257 AYLE-ERKQ-FGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDAVKL-CAMAKRFATDECFDVANQALQLH 333
|
330 340 350
....*....|....*....|....*....|...
gi 816333706 489 GAAGVCQDTPLAylwALVRTLR---IADGPDEV 518
Cdd:cd01162 334 GGYGYLKDYPVE---QYVRDLRvhqILEGTNEI 363
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
130-526 |
9.72e-36 |
|
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: 137.63 E-value: 9.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 130 DLVEEFVEKDCLPaealFAAQlghgeqrWNTTPAIMESLTAKARKLGLWNMFLPKNHfaQGAGFSNLEYGLMAEYLGKSK 209
Cdd:cd01160 8 DVVRRFFAKEVAP----FHHE-------WEKAGEVPREVWRKAGEQGLLGVGFPEEY--GGIGGDLLSAAVLWEELARAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 210 LAAEGFLSLSPFSatnnaapdtgnMEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGDEYV 289
Cdd:cd01160 75 GSGPGLSLHTDIV-----------SPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 290 LNGSKWW-SSGAgdpRCKIYLVMGKTDAQnPNPYRQQSVVLVPAGLPGITIHRMLQVYGY---DDAphghgHISFTNVRV 365
Cdd:cd01160 143 LNGSKTFiTNGM---LADVVIVVARTGGE-ARGAGGISLFLVERGTPGFSRGRKLKKMGWkaqDTA-----ELFFDDCRV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 366 PHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARINdERKTpFGQPLAAHGVIVEWLAKSRIEVDAARL 445
Cdd:cd01160 214 PAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVK-QRKA-FGKTLAQLQVVRHKIAELATKVAVTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 446 IVLNAAIKIDRGDAKAAltEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEVHLQQLGK 525
Cdd:cd01160 292 FLDNCAWRHEQGRLDVA--EASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
.
gi 816333706 526 R 526
Cdd:cd01160 370 Q 370
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
121-519 |
1.52e-30 |
|
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: 123.08 E-value: 1.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 121 VSDRAKKTLDLVEEFVEKDCLPAEALFAAQlghGEQRWnttpaimeSLTAKARKLGLWNMFLPKNHfaQGAGFSNLEYGL 200
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKS---GEYPW--------PLIKRAWELGLMNTHIPEDC--GGLGLGTFDTCL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 201 MAEYLgksklaAEGFLSLSpfsaTNNAAPDTGNMEVLAKyGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLD 280
Cdd:cd01157 68 ITEEL------AYGCTGVQ----TAIEANSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 281 IRREGDEYVLNGSKWWSSGAGdpRCKIYLVMGKTDaqnPNPYRQQSVV----LVPAGLPGITIHRMLQVYGyDDAPHGHG 356
Cdd:cd01157 136 AEKKGDEYIINGQKMWITNGG--KANWYFLLARSD---PDPKCPASKAftgfIVEADTPGIQPGRKELNMG-QRCSDTRG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 357 hISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEwMIARINDERKTpFGQPLAAHGVIVEWLAKS 436
Cdd:cd01157 210 -ITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALD-EATKYALERKT-FGKLIAEHQAVSFMLADM 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 437 RIEVDAARLIVLNAAIKIDRGDAKAALTEIaqAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPD 516
Cdd:cd01157 287 AMKVELARLAYQRAAWEVDSGRRNTYYASI--AKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTS 364
|
...
gi 816333706 517 EVH 519
Cdd:cd01157 365 QIQ 367
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
132-518 |
3.76e-30 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes 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. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 122.58 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 132 VEEFVEKDCLPAealfaaqlghgeqRWNTTPAIMESLTAKARKLGLWNMFLPKNHfaQGAGFSNLEYGLMAEYLGksklA 211
Cdd:cd01161 38 VEKFFEEVNDPA-------------KNDQLEKIPRKTLTQLKELGLFGLQVPEEY--GGLGLNNTQYARLAEIVG----M 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 212 AEGFlslspfSATNNAAPDTGNMEVLAkYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRR--EGDEYV 289
Cdd:cd01161 99 DLGF------SVTLGAHQSIGFKGILL-FGTEAQKEKYLPKLASGEWIAAFALTEPS-SGSDAASIRTTAVLseDGKHYV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 290 LNGSKWWSSGAGdpRCKIYLVMGKTDAQNPNPYRQQ--SVVLVPAGLPGITI---HRMLQVYGYDDAphghgHISFTNVR 364
Cdd:cd01161 171 LNGSKIWITNGG--IADIFTVFAKTEVKDATGSVKDkiTAFIVERSFGGVTNgppEKKMGIKGSNTA-----EVYFEDVK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 365 VPHGNmVLG-AGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARINDerKTPFGQPLAAHGVIVEWLAKSRIEVDAA 443
Cdd:cd01161 244 IPVEN-VLGeVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANN--RKQFGKKIHEFGLIQEKLANMAILQYAT 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816333706 444 RLIVLNAAIKIDRGDAKAALTEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEV 518
Cdd:cd01161 321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEI 395
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
375-526 |
2.25e-29 |
|
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: 113.12 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 375 GRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARINDeRKTpFGQPLAAHGVIVEWLAKSRIEVDAARLIVLNAAIKI 454
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARR-RKA-FGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEAL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 816333706 455 DRGdaKAALTEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEVHLQQLGKR 526
Cdd:pfam00441 79 DAG--GPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARR 148
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
190-518 |
2.91e-27 |
|
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: 113.27 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 190 GAGFSNLEYGLMAEYLGKsklaAEGFLSLSpFSATNNAAPDTgnmevLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEi 269
Cdd:cd01156 58 GSGMGYLAHVIIMEEISR----ASGSVALS-YGAHSNLCINQ-----IYRNGSAAQKEKYLPKLISGEHIGALAMSEPN- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 270 ASSDATNIQLDIRREGDEYVLNGSKWWSSGAgdPRCKIYLVMGKTDAQNPNpyRQQSVVLVPAGLPGITIHRMLQVYGYD 349
Cdd:cd01156 127 AGSDVVSMKLRAEKKGDRYVLNGSKMWITNG--PDADTLVVYAKTDPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 350 DAPhgHGHISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARINDERKtpFGQPLAAHGVI 429
Cdd:cd01156 203 GSN--TCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQ--FGQPIGEFQLV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 430 VEWLAKSRIEVDAARLIVLNAAIKIDRG--DAKAALTEIAQAKVLVPQTALtiidRAVQSYGAAGVCQDTPLAYLWALVR 507
Cdd:cd01156 279 QGKLADMYTRLNASRSYLYTVAKACDRGnmDPKDAAGVILYAAEKATQVAL----DAIQILGGNGYINDYPTGRLLRDAK 354
|
330
....*....|.
gi 816333706 508 TLRIADGPDEV 518
Cdd:cd01156 355 LYEIGAGTSEI 365
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
236-526 |
7.29e-25 |
|
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: 106.66 E-value: 7.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 236 VLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGDEYVLNGSKWWSSGAGDPRCKIYLVmgKTD 315
Cdd:cd01152 95 TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPG-AGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLV--RTD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 316 AQNPNpYRQQSVVLVPAGLPGITIHRMLQVygydDAPHGHGHISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRihhaMR 395
Cdd:cd01152 172 PEAPK-HRGISILLVDMDSPGVTVRPIRSI----NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFER----VS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 396 TIGAAEQAIEWMIARINDERKTPFGQ---PLAAHGvivewLAKSRIEVDAARLIVLNAAIKIDRGDAKAAltEIAQAKVL 472
Cdd:cd01152 243 IGGSAATFFELLLARLLLLTRDGRPLiddPLVRQR-----LARLEAEAEALRLLVFRLASALAAGKPPGA--EASIAKLF 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 816333706 473 VPQTALTIIDRAVQSYGAAGVCQDTP----------LAYLWAlvRTLRIADGPDEVHLQQLGKR 526
Cdd:cd01152 316 GSELAQELAELALELLGTAALLRDPApgaelagrweADYLRS--RATTIYGGTSEIQRNIIAER 377
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
261-355 |
1.78e-23 |
|
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: 94.65 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 261 AFLMTEPEiASSDATNIQLD-IRREGDEYVLNGSKWWSSGAGDprCKIYLVMGKTDAqnPNPYRQQSVVLVPAGLPGITI 339
Cdd:pfam02770 1 AFALTEPG-AGSDVASLKTTaADGDGGGWVLNGTKWWITNAGI--ADLFLVLARTGG--DDRHGGISLFLVPKDAPGVSV 75
|
90
....*....|....*.
gi 816333706 340 HRMLQVYGYDDAPHGH 355
Cdd:pfam02770 76 RRIETKLGVRGLPTGE 91
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
240-518 |
6.88e-23 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 100.57 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 240 YGNDAQKQQWLTPLLE-GKIRSAFLMTEPEiASSDATNIQLD-IRREGDEYvLNGSKWWSSGAGD-PRCkiyLVMGKtDA 316
Cdd:PRK12341 99 FGSAEQLRKTAESTLEtGDPAYALALTEPG-AGSDNNSATTTyTRKNGKVY-LNGQKTFITGAKEyPYM---LVLAR-DP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 317 QNPNPYRQQSVVLVPAGLPGITIHRMLQVyGYDDAPHGHghISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRT 396
Cdd:PRK12341 173 QPKDPKKAFTLWWVDSSKPGIKINPLHKI-GWHMLSTCE--VYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 397 IGAAEQAIEWMIARINdeRKTPFGQPLAAHGVIVEWLAKSRIEVDAARLIVLNAAIKIDRGdaKAALTEIAQAKVLVPQT 476
Cdd:PRK12341 250 LGFAECAFEDAARYAN--QRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNG--QSLRTSAALAKLYCART 325
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 816333706 477 ALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEV 518
Cdd:PRK12341 326 AMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
190-525 |
4.19e-22 |
|
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: 98.58 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 190 GAGFSNLEYGLMAEYLGKSKLAAEGFLSLspfsaTNNAApdtgnMEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEi 269
Cdd:cd01151 68 CAGLSSVAYGLIAREVERVDSGYRSFMSV-----QSSLV-----MLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPN- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 270 ASSDATNIQLDIRREGDEYVLNGSKWWSSGAgdPRCKIYLVMGKTDAQNpnpyrQQSVVLVPAGLPGITIHRMLQVYGYD 349
Cdd:cd01151 137 HGSDPGGMETRARKDGGGYKLNGSKTWITNS--PIADVFVVWARNDETG-----KIRGFILERGMKGLSAPKIQGKFSLR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 350 DAPhgHGHISFTNVRVPHGNMVLGAgRGFEIIQGRLGPGRIHHAMRTIGAAEQAieWMIARINDERKTPFGQPLAAHGVI 429
Cdd:cd01151 210 ASI--TGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWGALGAAEDC--YHTARQYVLDRKQFGRPLAAFQLV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 430 VEWLAKSRIEVDAARLIVLNAAIKIDRGdaKAALTEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTL 509
Cdd:cd01151 285 QKKLADMLTEIALGLLACLRVGRLKDQG--KATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESV 362
|
330
....*....|....*.
gi 816333706 510 RIADGPDEVHLQQLGK 525
Cdd:cd01151 363 NTYEGTHDIHALILGR 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
244-525 |
1.07e-21 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 97.70 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 244 AQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGDE-YVLNGSKWWSSGAgdPRCKIYLVMGKTDAQnpnpy 322
Cdd:PTZ00461 137 AQRARWLPKVLTGEHVGAMGMSEPG-AGTDVLGMRTTAKKDSNGnYVLNGSKIWITNG--TVADVFLIYAKVDGK----- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 323 rqQSVVLVPAGLPGITIHRMLQVYGYDdAPHgHGHISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQ 402
Cdd:PTZ00461 209 --ITAFVVERGTKGFTQGPKIDKCGMR-ASH-MCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAER 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 403 AIEWMiARINDERKTpFGQPLAAHGVIVEWLAKSRIEVDAARLIVLNAAIKIDRGDAKAALTEiaQAKVLVPQTALTIID 482
Cdd:PTZ00461 285 SVELM-TSYASERKA-FGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSD--AAKLFATPIAKKVAD 360
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 816333706 483 RAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEVHLQQLGK 525
Cdd:PTZ00461 361 SAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
175-532 |
3.77e-18 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 86.42 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 175 LGLWNMFLPKNHFAQGAGFSNLeyglMAEYLGKSKLAAEGF-LSLSPfsatnnaapdtGNMEVLAKYGNDAQKQQWLTPL 253
Cdd:PRK03354 49 MGIDSLLIPEEHGGLDAGFVTL----AAVWMELGRLGAPTYvLYQLP-----------GGFNTFLREGTQEQIDKIMAFR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 254 LEGKIRSAFLMTEPEiASSDATNIQLDIRREGDEYVLNGSKWW-SSGAGDPrckiYLVMGKTDAQNPNPyRQQSVVLVPA 332
Cdd:PRK03354 114 GTGKQMWNSAITEPG-AGSDVGSLKTTYTRRNGKVYLNGSKCFiTSSAYTP----YIVVMARDGASPDK-PVYTEWFVDM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 333 GLPGITIHRMLQVYGYDDAPhghGHISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIEWMIARIN 412
Cdd:PRK03354 188 SKPGIKVTKLEKLGLRMDSC---CEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYAN 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 413 deRKTPFGQPLAAHGVIVEWLAKSRIEVDAARLIVLNAAIKIDRGDAKAAltEIAQAKVLVPQTALTIIDRAVQSYGAAG 492
Cdd:PRK03354 265 --QRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSG--DAAMCKYFCANAAFEVVDSAMQVLGGVG 340
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 816333706 493 VCQDTPLAYLWALVRTLRIADGPDEVHLQQLGKRENRRRR 532
Cdd:PRK03354 341 IAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
191-518 |
3.35e-15 |
|
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: 77.80 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 191 AGFSNLEYGLMAEYLgkskLAAEGFLSLSPFSATNNAAPdtgnmeVLAKYGnDAQKQQWLTPLLEGKIR----SAFLMTE 266
Cdd:cd01154 87 AGEGRRHVHFAAGYL----LSDAAAGLLCPLTMTDAAVY------ALRKYG-PEELKQYLPGLLSDRYKtgllGGTWMTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 267 PEIASSDATNIQLDIRREGDEYVLNGSKWWSSGagdPRCKIYLVMGKTdAQNPNPYRQQSVVLVPAGLP-----GITIHR 341
Cdd:cd01154 156 KQGGSDLGANETTAERSGGGVYRLNGHKWFASA---PLADAALVLARP-EGAPAGARGLSLFLVPRLLEdgtrnGYRIRR 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 342 MLQVYGYDDAPhgHGHISFTNVRvphGNMVLGAGRGFEIIQGRLGPGRIHHAMRTIGAAEQAIewMIARINDERKTPFGQ 421
Cdd:cd01154 232 LKDKLGTRSVA--TGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRAL--SEAYHYARHRRAFGK 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 422 PLAAHGVIVEWLAKSRIEVDAARLIVLNAAIKIDR------GDAKAALTEIAQAKVLVPQTALTIIDRAVQSYGAAGVCQ 495
Cdd:cd01154 305 PLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRaaadkpVEAHMARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLE 384
|
330 340
....*....|....*....|...
gi 816333706 496 DTPLAYLWALVRTLRIADGPDEV 518
Cdd:cd01154 385 EWPVARLHREAQVTPIWEGTGNI 407
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
237-525 |
1.58e-13 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 72.60 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 237 LAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGDEYVLNGSKWWSSGAgdPRCKIYLVMGKTDA 316
Cdd:PLN02519 121 LVRNGTPAQKEKYLPKLISGEHVGALAMSEPN-SGSDVVSMKCKAERVDGGYVLNGNKMWCTNG--PVAQTLVVYAKTDV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 317 QNPNpyRQQSVVLVPAGLPGITIHRMLQVYGYDDAphGHGHISFTNVRVPHGNMVLGAGRGFEIIQGRLGPGRIHHAMRT 396
Cdd:PLN02519 198 AAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGS--DTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 397 IGAAEQAIEWMIARINDERKtpFGQPLAAHGVIVEWLAKSRIEVDAARLIVLNAAIKIDRG--DAKAALTEIAQAKVLVP 474
Cdd:PLN02519 274 LGLMQACLDVVLPYVRQREQ--FGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGkvDRKDCAGVILCAAERAT 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 816333706 475 QTALtiidRAVQSYGAAGVCQDTPLAYLWALVRTLRIADGPDEVHLQQLGK 525
Cdd:PLN02519 352 QVAL----QAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| Spo12 |
pfam05032 |
Spo12 family; This family of proteins includes Spo12 from S. cerevisiae. The Spo12 protein ... |
47-78 |
1.08e-12 |
|
Spo12 family; This family of proteins includes Spo12 from S. cerevisiae. The Spo12 protein plays a regulatory role in two of the most fundamental processes of biology, mitosis and meiosis, and yet its biochemical function remains elusive. Spo12 is a nuclear protein. Spo12 is a component of the FEAR (Cdc fourteen early anaphase release) regulatory network, that promotes Cdc14 release from the nucleolus during early anaphase. The FEAR network is comprised of the polo kinase Cdc5, the separase Esp1, the kinetochore-associated protein Slk19, and Spo12.
Pssm-ID: 398624 Cd Length: 33 Bit Score: 62.35 E-value: 1.08e-12
10 20 30
....*....|....*....|....*....|..
gi 816333706 47 VSPSDDIMSPCSKKLSDLKGKRFKNAGKPQSL 78
Cdd:pfam05032 1 VSPTDNLMSPCSQKLNAHKSKLFKKKSKPTKL 32
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
231-514 |
2.53e-12 |
|
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: 68.96 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 231 TGNMEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGD-EYVLNGSKWW-SSGAGDPRCKI- 307
Cdd:cd01153 90 QGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPD-AGSDLGALRTKAVYQADgSWRINGVKRFiSAGEHDMSENIv 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 308 YLVMGKTDAQNPNPyRQQSVVLVPAGLP-----GITIHRMLQVYGYDDAPhgHGHISFTNVRVPhgnmVLGA-GRG---- 377
Cdd:cd01153 169 HLVLARSEGAPPGV-KGLSLFLVPKFLDdgernGVTVARIEEKMGLHGSP--TCELVFDNAKGE----LIGEeGMGlaqm 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 378 FEIIQG-RLGPGrihhaMRTIGAAEQAIEWMIARINDerKTPFGQPLAA--------HGVIVEWLAKSRIEVDAARLIVL 448
Cdd:cd01153 242 FAMMNGaRLGVG-----TQGTGLAEAAYLNALAYAKE--RKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDL 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 816333706 449 NAAIKIDRGDAKAALTEIAQ-----AKVLVP-------QTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRIADG 514
Cdd:cd01153 315 YTATVQDLAERKATEGEDRKalsalADLLTPvvkgfgsEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
130-257 |
2.10e-11 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 60.94 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 130 DLVEEFVEKDCLPAEAlfaaqlghgeqRWNTTPAIMESLTAKARKLGLWNMFLPKNHfaQGAGFSNLEYGLMAEylgksK 209
Cdd:pfam02771 9 DTVREFAEEEIAPHAA-----------EWDEEGEFPRELWKKLGELGLLGITIPEEY--GGAGLDYLAYALVAE-----E 70
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 816333706 210 LAAEGFLSLSPFSATNNAApdtgnMEVLAKYGNDAQKQQWLTPLLEGK 257
Cdd:pfam02771 71 LARADASVALALSVHSSLG-----APPILRFGTEEQKERYLPKLASGE 113
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
235-493 |
4.31e-10 |
|
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: 61.57 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 235 EVLAKYGNDAQKQQWLTPLLEGKIRSAflmTEPEIASSDATNIQLDIRREGDEYVLNGSKWWSSGAgdprckIYLVMGKT 314
Cdd:cd01163 81 EALLLAGPEQFRKRWFGRVLNGWIFGN---AVSERGSVRPGTFLTATVRDGGGYVLNGKKFYSTGA------LFSDWVTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 315 DAQNPNpyRQQSVVLVPAGLPGITIHrmlqvygyDD-APHGH-----GHISFTNVRVPHGNMVLGAGRGFeiiQGRLGPG 388
Cdd:cd01163 152 SALDEE--GKLVFAAVPTDRPGITVV--------DDwDGFGQrltasGTVTFDNVRVEPDEVLPRPNAPD---RGTLLTA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 389 --RIHHAMRTIGAAEQAIEWMIARINdERKTPFGQPLAAHGV----IVEWLAKSRIEVDAARLIVLNAAIKIDRGDAK-A 461
Cdd:cd01163 219 iyQLVLAAVLAGIARAALDDAVAYVR-SRTRPWIHSGAESARddpyVQQVVGDLAARLHAAEALVLQAARALDAAAAAgT 297
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 816333706 462 ALTE---------IAQAKVLVPQTALTIIDRAVQSYGAAGV 493
Cdd:cd01163 298 ALTAeargeaalaVAAAKVVVTRLALDATSRLFEVGGASAT 338
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
392-511 |
4.83e-10 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 57.74 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 392 HAMRTIGAAEQAIEWMIARINDERKTPFGQPLAAHGVIVEWLAKSRIEVDAARLIVLNAAI----KIDRGDAKAALT--E 465
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAArieaAAAAGKPVTPALraE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 816333706 466 IAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLWALVRTLRI 511
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQ 127
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
234-425 |
1.93e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 53.32 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 234 MEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEIAsSDATNIQLDIRREGDEYVLNGSKWW--SSGAGDprckIYLVM 311
Cdd:PLN02526 118 MLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYG-SDASSLNTTATKVEGGWILNGQKRWigNSTFAD----VLVIF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 312 GKTDAQNpnpyrQQSVVLVPAGLPGITIH--------RMLQvygyddaphgHGHISFTNVRVPHGNMVLGAgRGFEIIQG 383
Cdd:PLN02526 193 ARNTTTN-----QINGFIVKKGAPGLKATkienkiglRMVQ----------NGDIVLKDVFVPDEDRLPGV-NSFQDTNK 256
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 816333706 384 RLGPGRIHHAMRTIGAAEQAIEwMIARINDERKTpFGQPLAA 425
Cdd:PLN02526 257 VLAVSRVMVAWQPIGISMGVYD-MCHRYLKERKQ-FGAPLAA 296
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
281-503 |
9.56e-04 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 41.57 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 281 IRREGDEYVLNGSkwWSSGAGDPRCKIYLVMGK-TDAQNPNPYRqqsVVLVPAGlpGITIHRMLQVYGYddAPHGHGHIS 359
Cdd:cd01159 113 AERVDGGYRVSGT--WPFASGCDHADWILVGAIvEDDDGGPLPR---AFVVPRA--EYEIVDTWHVVGL--RGTGSNTVV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 360 FTNVRVPH------GNMVLGAGRGFEIIQGRLGPGRIH---HAMRTIGAAEQAIEWMIARINDE-RKTPFGQPLAAHGVI 429
Cdd:cd01159 184 VDDVFVPEhrtltaGDMMAGDGPGGSTPVYRMPLRQVFplsFAAVSLGAAEGALAEFLELAGKRvRQYGAAVKMAEAPIT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 430 VEWLAKSRIEVDAARLIVLNAAIKIDR----GDAKAALT--EIAQAKVLVPQTALTIIDRAVQSYGAAGVCQDTPLAYLW 503
Cdd:cd01159 264 QLRLAEAAAELDAARAFLERATRDLWAhalaGGPIDVEEraRIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIW 343
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
235-277 |
9.93e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 42.11 E-value: 9.93e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 816333706 235 EVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNI 277
Cdd:PRK09463 170 ELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPE-AGSDAGSI 211
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
235-278 |
1.26e-03 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 41.87 E-value: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 816333706 235 EVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQ 278
Cdd:PRK13026 169 ELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPE-AGSDAGAIP 211
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
232-335 |
5.62e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 39.47 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816333706 232 GNMEVLAKYGNDAQKQQWLTPLLEGKIRSAFLMTEPEiASSDATNIQLDIRREGD-EYVLNGSKWWSSgAGDPRCK---I 307
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQ-CGTDLGQVKTKAEPSADgSYKITGTKIFIS-AGDHDLTeniV 232
|
90 100
....*....|....*....|....*...
gi 816333706 308 YLVMGKTDAQNPNPyRQQSVVLVPAGLP 335
Cdd:PTZ00456 233 HIVLARLPNSLPTT-KGLSLFLVPRHVV 259
|
|
| |
