|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
4-590 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 580.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 4 YDAPLRDMRFVLNE-LHADD-----GFGDIpalaefTPDLTDAILEEAARFCRDVLLPINRSGDEEGCH-LENGVVRTPA 76
Cdd:PTZ00456 26 YQPRIRDVQFLVEEvFNMYDhyeklGKTDV------TKELMDSLLEEASKLATQTLLPLYESSDSEGCVlLKDGNVTTPK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 77 GFAQAYKQFAEGGWTALASDPEWGGQGLPEAVNKLVEEMICSSNLSFGLYPGLTHGATTAIEGHGSDALKQAYLPKMVSG 156
Cdd:PTZ00456 100 GFKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 157 QWSGTMCLTEPHCGTDLGLLRSRAVPQGDGSYKVTGSKIFISAGEHDLTENIIHLVLARLPDAPKGVKGISLFLVPKYLP 236
Cdd:PTZ00456 180 EWSGTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 237 KEDGTPGQSNGVACAAIEHKMGLKASATCQMNFDDSTGWLVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWY 316
Cdd:PTZ00456 260 KPDGSLETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRY 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 317 AKDRIQGRALSGPKYPEQAADPIIVHPDVRRMLMTMRAYNEGCRALSAWVSRALDAEKHSPEPEVRQRASDFIALMTPVV 396
Cdd:PTZ00456 340 ARERRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIA 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 397 KALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGTNGVQALDLVGRK-LGAHMGRYLRSFFHPVSAFIE 475
Cdd:PTZ00456 420 KGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKvLSLKGGNEVARFGKRVSKLVR 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 476 ENNVD-GPMKPMVEALAKAFGALQLSTATVAQRALKDPEEAGAASADYLRLMGLVAMGYCFAKATKIAGLQLFFGSEDKR 554
Cdd:PTZ00456 500 AHLFSrGALGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWLRMAEVAQKKVAAGQDADG 579
|
570 580 590
....*....|....*....|....*....|....*.
gi 644223274 555 FYDAKIKTATFFFERILPQATASFLAIKAGkKSLMA 590
Cdd:PTZ00456 580 FYQCKVDTCQYVFQRILPRADAHFQIMQAG-PSIMA 614
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
41-456 |
4.61e-174 |
|
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: 499.22 E-value: 4.61e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 41 ILEEAARFCRDVLLPINRSGDEEGCHLENGVVRTPAGFAQAYKQFAEGGWTALASDPEWGGQGLPEAVNKLVEEMIcSSN 120
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIF-SRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 121 LSFGLYPGLTHGATTAIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDGSYKVTGSKIFISAG 200
Cdd:cd01153 80 DAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 201 EHDLTENIIHLVLARLPDAPKGVKGISLFLVPKYLpkedgTPGQSNGVACAAIEHKMGLKASATCQMNFDDSTGWLVGEP 280
Cdd:cd01153 160 EHDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFL-----DDGERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 281 GKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRIQGRALSgpkyPEQAADPIIVHPDVRRMLMTMRAYNEGCR 360
Cdd:cd01153 235 GMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQKAYAEGSR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 361 ALSAWVSRALDAEKHSP-EPEVRQRASDFIALMTPVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIY 439
Cdd:cd01153 311 ALDLYTATVQDLAERKAtEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIY 390
|
410
....*....|....*..
gi 644223274 440 EGTNGVQALDLVGRKLG 456
Cdd:cd01153 391 EGTTGIQALDLIGRKIV 407
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
32-460 |
6.30e-118 |
|
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: 354.92 E-value: 6.30e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 32 EFTPDLtDAILEEAARFCRDVLLPINRSGDEEGchlengvvRTPAgfaQAYKQFAEGGWTALASDPEWGGQGLPEAVNKL 111
Cdd:COG1960 4 ELTEEQ-RALRDEVREFAEEEIAPEAREWDREG--------EFPR---ELWRKLAELGLLGLTIPEEYGGLGLSLVELAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 112 VEEMICSSNLSFGLYPGLTHGATTAIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDGsYKVT 191
Cdd:COG1960 72 VLEELARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 192 GSKIFIS-AGEHDlteniIHLVLARLPDAPkGVKGISLFLVPKYLPkedgtpgqsnGVACAAIEHKMGLKASATCQMNFD 270
Cdd:COG1960 151 GQKTFITnAPVAD-----VILVLARTDPAA-GHRGISLFLVPKDTP----------GVTVGRIEDKMGLRGSDTGELFFD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 271 D---STGWLVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRIQ-GRalsgpkypeqaadPIIVHPDVR 346
Cdd:COG1960 215 DvrvPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQfGR-------------PIADFQAVQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 347 RMLMTMRAYNEGCRALSAWVSRALDAEKHspepevrqrasdfIALMTPVVKALFTDLAFDSANLAVQCYGGHGYIRESGV 426
Cdd:COG1960 282 HRLADMAAELEAARALVYRAAWLLDAGED-------------AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPL 348
|
410 420 430
....*....|....*....|....*....|....
gi 644223274 427 EQYARDARITMIYEGTNGVQALDLvGRKLGAHMG 460
Cdd:COG1960 349 ERLYRDARILTIYEGTNEIQRLII-ARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
132-450 |
9.01e-60 |
|
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: 202.13 E-value: 9.01e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 132 GATTAIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDGsYKVTGSKIFISAGEH-DLteniiH 210
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNGGDaDL-----F 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 211 LVLARLPDAPKGVKGISLFLVPKYLPkedgtpgqsnGVACAAIEHKMGLKASATCQMNFDD---STGWLVGEPGKGMAAM 287
Cdd:cd00567 117 IVLARTDEEGPGHRGISAFLVPADTP----------GVTVGRIWDKMGMRGSGTGELVFDDvrvPEDNLLGEEGGGFELA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 288 FTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRiqgralsgpkypEQAADPIIVHPDVRRMLMTMRAYNEGCRALSAWVS 367
Cdd:cd00567 187 MKGLNVGRLLLAAVALGAARAALDEAVEYAKQR------------KQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 368 RALDAEkhspEPEVRQRASdfialmtpVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGTNGVQA 447
Cdd:cd00567 255 WLLDQG----PDEARLEAA--------MAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQR 322
|
...
gi 644223274 448 LDL 450
Cdd:cd00567 323 LII 325
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
39-448 |
7.26e-57 |
|
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: 195.56 E-value: 7.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 39 DAILEEAARFCRDVLLPINRSGDEEGchlengvvRTPAgfaQAYKQFAEGGWTALASDPEWGGQGLPEAVNKLVEEMICS 118
Cdd:cd01158 4 QMIRKTVRDFAEKEIAPLAAEMDEKG--------EFPR---EVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 119 SNLSFGLYPGLTHG-ATTAIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDgSYKVTGSKIFI 197
Cdd:cd01158 73 VDASVAVIVSVHNSlGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSKMWI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 198 S-AGEHDlteniIHLVLARLpDAPKGVKGISLFLVPKylpkedGTPGQSNGVAcaaiEHKMGLKASATCQMNFDD---ST 273
Cdd:cd01158 152 TnGGEAD-----FYIVFAVT-DPSKGYRGITAFIVER------DTPGLSVGKK----EDKLGIRGSSTTELIFEDvrvPK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 274 GWLVGEPGKGMA-AMFTMmNTERVSVGIQGLGVGEAAYQAAAWYAKDRiqgralsgpkypEQAADPIIVHPDVRRMLMTM 352
Cdd:cd01158 216 ENILGEEGEGFKiAMQTL-DGGRIGIAAQALGIAQAALDAAVDYAKER------------KQFGKPIADFQGIQFKLADM 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 353 RAYNEGCRALsawVSRAldAEKhspepevRQRASDFI--ALMTpvvKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYA 430
Cdd:cd01158 283 ATEIEAARLL---TYKA--ARL-------KDNGEPFIkeAAMA---KLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYY 347
|
410
....*....|....*...
gi 644223274 431 RDARITMIYEGTNGVQAL 448
Cdd:cd01158 348 RDAKITEIYEGTSEIQRL 365
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
67-451 |
1.53e-50 |
|
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: 179.87 E-value: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 67 LENGVV---RTPAGFAQAYKQFAEGGwtaLASDPEWGgqglpeavnklveeMICSSNLsfglypglTHGATTAIEGHGSD 143
Cdd:cd01154 75 IEEGVInieDGPAGEGRRHVHFAAGY---LLSDAAAG--------------LLCPLTM--------TDAAVYALRKYGPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 144 ALKQAYLPKMVSGQ---WSGTMCLTEPHCGTDLGLLRSRAVPQGDGSYKVTGSKIFISAGEHDlteniIHLVLARLPDAP 220
Cdd:cd01154 130 ELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLAD-----AALVLARPEGAP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 221 KGVKGISLFLVPKYLPKedgtpGQSNGVACAAIEHKMGLKASATCQMNFDDSTGWLVGEPGKGMAAMFTMMNTERVSVGI 300
Cdd:cd01154 205 AGARGLSLFLVPRLLED-----GTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYILEMLNISRLDNAV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 301 QGLGVGEAAYQAAAWYAKDRiqgRALSGPkypeqaadpIIVHPDVRRMLMTMRAYNEGCRALSAWVSRALD-AEKHSPEP 379
Cdd:cd01154 280 AALGIMRRALSEAYHYARHR---RAFGKP---------LIDHPLMRRDLAEMEVDVEAATALTFRAARAFDrAAADKPVE 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644223274 380 EVRQRasdfiaLMTPVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGTNGVQALDLV 451
Cdd:cd01154 348 AHMAR------LATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVL 413
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
40-455 |
1.46e-40 |
|
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: 151.44 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 40 AILEEAARFCRDVLLPINRSGDEEGcHLENGVVRtpagfaqaykQFAEGGWTALASDPEWGGQGLPEAVNKLVEEMICSS 119
Cdd:cd01162 7 AIQEVARAFAAKEMAPHAADWDQKK-HFPVDVLR----------KAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 120 NLSFGLYPGLTHGATTAIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDgSYKVTGSKIFIS- 198
Cdd:cd01162 76 CVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFISg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 199 AGEHDlteniIHLVLARlpDAPKGVKGISLFLVPKylpkedGTPGQSNGvacaAIEHKMGLKASATCQMNFDD---STGW 275
Cdd:cd01162 155 AGDSD-----VYVVMAR--TGGEGPKGISCFVVEK------GTPGLSFG----ANEKKMGWNAQPTRAVIFEDcrvPVEN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 276 LVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRiqgralsgpkypEQAADPIIVHPDVRRMLMTMRAY 355
Cdd:cd01162 218 RLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEER------------KQFGKPLADFQALQFKLADMATE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 356 NEGCRALSAWVSRALDAEkhspEPEVrqrasdfiALMTPVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARI 435
Cdd:cd01162 286 LVASRLMVRRAASALDRG----DPDA--------VKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRV 353
|
410 420
....*....|....*....|
gi 644223274 436 TMIYEGTNGVQALdLVGRKL 455
Cdd:cd01162 354 HQILEGTNEIMRL-IIARAL 372
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
467-591 |
1.42e-36 |
|
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal region of many bacterial acetyl-CoA dehydrogenases.
Pssm-ID: 463716 Cd Length: 126 Bit Score: 132.67 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 467 FHPVSAFIEENNVDGPMKPMVEALAKAFGALQLSTATVAQRALK-DPEEAGAASADYLRLMGLVAMGYCFAKATKIAGLQ 545
Cdd:pfam12806 1 LAEIRAFIAAAAGDPALAAEAAALAAALAALQEATAWLLARAAKgDPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 644223274 546 LFFGSEDKRFYDAKIKTATFFFERILPQATASFLAIKAGKKSLMAL 591
Cdd:pfam12806 81 LAAGAKDAAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
82-456 |
1.54e-34 |
|
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: 134.55 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 82 YKQFAEGGWTALASDPEWGGQG---LPEAVnkLVEEMICS--SNLSFGLYPGLthgATTAIEGHGSDALKQAYLPKMVSG 156
Cdd:cd01160 36 WRKAGEQGLLGVGFPEEYGGIGgdlLSAAV--LWEELARAggSGPGLSLHTDI---VSPYITRAGSPEQKERVLPQMVAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 157 QWSGTMCLTEPHCGTDLGLLRSRAVPQGDgSYKVTGSKIFISAGEHdlteNIIHLVLARLPDAPKGVKGISLFLVpkylp 236
Cdd:cd01160 111 KKIGAIAMTEPGAGSDLQGIRTTARKDGD-HYVLNGSKTFITNGML----ADVVIVVARTGGEARGAGGISLFLV----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 237 kEDGTPGQSNGVACaaieHKMGLKASATCQMNFDD---STGWLVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAA 313
Cdd:cd01160 181 -ERGTPGFSRGRKL----KKMGWKAQDTAELFFDDcrvPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEET 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 314 AWYAKDRiqgralsgpkypEQAADPIIVHPDVRRMLMTMRAYNEGCRAL---SAWvsraLDAEKHSPEPEVrqrasdfia 390
Cdd:cd01160 256 RNYVKQR------------KAFGKTLAQLQVVRHKIAELATKVAVTRAFldnCAW----RHEQGRLDVAEA--------- 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 644223274 391 lmtPVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGTNGVQaLDLVGRKLG 456
Cdd:cd01160 311 ---SMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIM-KELISRQMV 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
83-448 |
1.36e-33 |
|
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: 132.59 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 83 KQFAEGGWTALASDPEWGGQGLPEAVNKLVEEmICSSNLSFGLYPGLTHG-ATTAIEGHGSDALKQAYLPKMVSGQWSGT 161
Cdd:cd01161 63 TQLKELGLFGLQVPEEYGGLGLNNTQYARLAE-IVGMDLGFSVTLGAHQSiGFKGILLFGTEAQKEKYLPKLASGEWIAA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 162 MCLTEPHCGTDLGLLRSRAVPQGDGS-YKVTGSKIFISAGehDLTEniIHLVLARLP--DAPKGVK-GISLFLVPKYLpk 237
Cdd:cd01161 142 FALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNG--GIAD--IFTVFAKTEvkDATGSVKdKITAFIVERSF-- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 238 edgtpgqsNGVACAAIEHKMGLKASATCQMNFDDS---TGWLVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAA 314
Cdd:cd01161 216 --------GGVTNGPPEKKMGIKGSNTAEVYFEDVkipVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 315 WYAKDRIQ-GRALSgpKY---PEQAAdpiivhpdvrrmLMTMRAYNEGCRALsaWVSRALDaekhspepevRQRASDFiA 390
Cdd:cd01161 288 DYANNRKQfGKKIH--EFgliQEKLA------------NMAILQYATESMAY--MTSGNMD----------RGLKAEY-Q 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 644223274 391 LMTPVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGTNGVQAL 448
Cdd:cd01161 341 IEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
36-455 |
7.96e-31 |
|
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: 124.06 E-value: 7.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 36 DLTDAILEEAARFCRDVLLPINRSGDEEgchleNGVVRtpagfaQAYKQFAEGGWTALASDPEWGGQGLPEAVNKLVEEM 115
Cdd:cd01156 4 DEIEMLRQSVREFAQKEIAPLAAKIDRD-----NEFPR------DLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 116 ICSSNLSFGLypglTHGATT-----AIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDGsYKV 190
Cdd:cd01156 73 ISRASGSVAL----SYGAHSnlcinQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDR-YVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 191 TGSKIFISAGEHDLTeniiHLVLARlPDAPKGVKGISLFLVpkylpkEDGTPGQSNGVACaaieHKMGLKASATCQMNFD 270
Cdd:cd01156 148 NGSKMWITNGPDADT----LVVYAK-TDPSAGAHGITAFIV------EKGMPGFSRAQKL----DKLGMRGSNTCELVFE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 271 D---STGWLVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRiqgralsgpkypEQAADPI----IVHP 343
Cdd:cd01156 213 DcevPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQR------------KQFGQPIgefqLVQG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 344 DVRRMLMTMRAynegCRALSAWVSRALDAEKHSPepevRQRASdfiALMTPVVKAlfTDLAFDsanlAVQCYGGHGYIRE 423
Cdd:cd01156 281 KLADMYTRLNA----SRSYLYTVAKACDRGNMDP----KDAAG---VILYAAEKA--TQVALD----AIQILGGNGYIND 343
|
410 420 430
....*....|....*....|....*....|..
gi 644223274 424 SGVEQYARDARITMIYEGTNGVQALdLVGRKL 455
Cdd:cd01156 344 YPTGRLLRDAKLYEIGAGTSEIRRM-VIGREL 374
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
83-455 |
1.01e-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: 109.36 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 83 KQFAEGGWTALASDPEWGGQGLPEAVNKLVEEMICSSNlsfGLYPGLTHGATTA---IEGHGSDALKQAYLPKMVSGQ-- 157
Cdd:cd01152 42 RALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAG---APVPFNQIGIDLAgptILAYGTDEQKRRFLPPILSGEei 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 158 WsgtmCL--TEPHCGTDLGLLRSRAVPQGDGsYKVTGSKIFISAGEhdltENIIHLVLARL-PDAPKGvKGISLFLVPKY 234
Cdd:cd01152 119 W----CQgfSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAH----YADWAWLLVRTdPEAPKH-RGISILLVDMD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 235 LPkedgtpgqsnGVACAAIEHKMGlkASATCQMNFDD---STGWLVGEPGKGMAAMFTMMNTERVSVGiqglgvgeaayq 311
Cdd:cd01152 189 SP----------GVTVRPIRSING--GEFFNEVFLDDvrvPDANRVGEVNDGWKVAMTTLNFERVSIG------------ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 312 AAAWYAKDRIQGRALSGPKYPEQAADpiivHPDVRRMLMTMRAYNEGCRALSAWVSRALDAEKHSPepevrqrasdfiaL 391
Cdd:cd01152 245 GSAATFFELLLARLLLLTRDGRPLID----DPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG-------------A 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644223274 392 MTPVVKALFTDLAFDSANLAVQCYGGHGYIRESG--------VEQYARDARITMIYEGTNGVQaLDLVGRKL 455
Cdd:cd01152 308 EASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQ-RNIIAERL 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
142-442 |
2.30e-24 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 105.79 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 142 SDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDGSYKVTGSKIFISAGehdlTENIIHLVLARlpdapk 221
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNG----TVADVFLIYAK------ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 222 gVKG-ISLFLVpkylpkEDGTPGQSNGvacAAIEhKMGLKASATCQMNFDD---STGWLVGEPGKGMAAMFTMMNTERVS 297
Cdd:PTZ00461 205 -VDGkITAFVV------ERGTKGFTQG---PKID-KCGMRASHMCQLFFEDvvvPAENLLGEEGKGMVGMMRNLELERVT 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 298 VGIQGLGVGEAAYQAAAWYAKDRiqgralsgpkypEQAADPIIVHPDVRRMLMTMRAYNEGCRALSAWVSraldaekHSP 377
Cdd:PTZ00461 274 LAAMAVGIAERSVELMTSYASER------------KAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVS-------HNV 334
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644223274 378 EPEVRQRasdfiaLMTPVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGT 442
Cdd:PTZ00461 335 HPGNKNR------LGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
40-453 |
5.02e-24 |
|
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: 104.36 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 40 AILEEAARFCRDVLLPINRSGDEEGchlengvvrtpAGFAQAYKQFAEGGWTAlASDPEWGGQGLPEAVNKLVEEMI--- 116
Cdd:cd01151 19 AIRDTAREFCQEELAPRVLEAYREE-----------KFDRKIIEEMGELGLLG-ATIKGYGCAGLSSVAYGLIAREVerv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 117 ---CSS----NLSFGLYPglthgattaIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDGsYK 189
Cdd:cd01151 87 dsgYRSfmsvQSSLVMLP---------IYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG-YK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 190 VTGSKIFISAGehDLTENIIhlVLARLPDAPKgVKGislFLVPKylpkedGTPGQSngvaCAAIEHKMGLKASATCQMNF 269
Cdd:cd01151 157 LNGSKTWITNS--PIADVFV--VWARNDETGK-IRG---FILER------GMKGLS----APKIQGKFSLRASITGEIVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 270 DDStgwLVGE----PG-KGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRIQ-GRALSGPK-YPEQAADPIIvh 342
Cdd:cd01151 219 DNV---FVPEenllPGaEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQfGRPLAAFQlVQKKLADMLT-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 343 pDVRRMLmtmraynegcraLSAW-VSRALDAEKHSPEpevrqrasdfialMTPVVKALFTDLAFDSANLAVQCYGGHGYI 421
Cdd:cd01151 294 -EIALGL------------LACLrVGRLKDQGKATPE-------------QISLLKRNNCGKALEIARTAREMLGGNGIS 347
|
410 420 430
....*....|....*....|....*....|..
gi 644223274 422 RESGVEQYARDARITMIYEGTNGVQALdLVGR 453
Cdd:cd01151 348 DEYHIIRHMVNLESVNTYEGTHDIHAL-ILGR 378
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
162-470 |
8.94e-22 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 99.06 E-value: 8.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 162 MCLTEPHCGTDLGLLRSRAVPQGDGSYKVTGSKIFISAGEHDlteniIHLVLARlpdaPKGvkGISLFLVPKYLPKedgt 241
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSD-----AHLVLAQ----AKG--GLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 242 pGQSNGVACAAIEHKMGLKASATCQMNFDDSTGWLVGEPGKGMAAMFTMMNTERV--SVGIQGLgvgeaayqaaawyakd 319
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFdcALGSHGL---------------- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 320 riQGRALSGPKY---PEQA-ADPIIVHPDVRRMLMTMRAYNEGCRALSAWVSRALDAEKhspepEVRQRAsdFIALMTPV 395
Cdd:PRK11561 310 --MRRAFSVAIYhahQRQVfGKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRA-----DAKEAL--WARLFTPA 380
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 644223274 396 VKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGTNGVQALDlVGRKLGAHMGRY--LRSFFHPV 470
Cdd:PRK11561 381 AKFVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLD-VLRVLNKQPGVYdlLSEAFVEV 456
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
98-455 |
6.76e-21 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 95.33 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 98 EWGGQGLPEAVNKLVEEMICSSNLSFGL-YPGLTHGATTAIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLL 176
Cdd:PLN02519 81 EYGGLGLGYLYHCIAMEEISRASGSVGLsYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 177 RSRAvPQGDGSYKVTGSKIFISAGEHDLTeniihLVLARLPDAPKGVKGISLFLVPKYLPkedgtpgqsnGVACAAIEHK 256
Cdd:PLN02519 161 KCKA-ERVDGGYVLNGNKMWCTNGPVAQT-----LVVYAKTDVAAGSKGITAFIIEKGMP----------GFSTAQKLDK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 257 MGLKASATCQMNFDD---STGWLVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRiqgralsgpkypE 333
Cdd:PLN02519 225 LGMRGSDTCELVFENcfvPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQR------------E 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 334 QAADPIIVHPDVRRMLMTMRAYNEGCRALSAWVSRALDAEKHSPEpevrqrasDFIALMtpvvkaLFT-DLAFDSANLAV 412
Cdd:PLN02519 293 QFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK--------DCAGVI------LCAaERATQVALQAI 358
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 644223274 413 QCYGGHGYIRESGVEQYARDARITMIYEGTNGVQALdLVGRKL 455
Cdd:PLN02519 359 QCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGREL 400
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
281-455 |
1.38e-20 |
|
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: 88.47 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 281 GKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRIQ-GRalsgpkypeqaadPIIVHPDVRRMLMTMRAYNEGC 359
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAfGR-------------PLIDFQLVRHKLAEMAAEIEAA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 360 RALSAWVSRALDAEKHSPEPevrqrasdfialmTPVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIY 439
Cdd:pfam00441 68 RLLVYRAAEALDAGGPDGAE-------------ASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIG 134
|
170
....*....|....*.
gi 644223274 440 EGTNGVQaLDLVGRKL 455
Cdd:pfam00441 135 EGTSEIQ-RNIIARRL 149
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
42-448 |
1.75e-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: 87.64 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 42 LEEAAR-FCRDVLLPINRSGDEEGchlengvvRTPAgfaQAYKQFAEGGWTALASDPEWGGQGLpeavnKLVEEMICSSN 120
Cdd:cd01157 8 FQETARkFAREEIIPVAAEYDKSG--------EYPW---PLIKRAWELGLMNTHIPEDCGGLGL-----GTFDTCLITEE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 121 LSFGlypglTHGATTAIEGH----------GSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVPQGDgSYKV 190
Cdd:cd01157 72 LAYG-----CTGVQTAIEANslgqmpviisGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYII 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 191 TGSKIFISAGEHdlteNIIHLVLARL---PDAPKGvKGISLFLVpkylpkEDGTPGQSNGVAcaaiEHKMGLKASATCQM 267
Cdd:cd01157 146 NGQKMWITNGGK----ANWYFLLARSdpdPKCPAS-KAFTGFIV------EADTPGIQPGRK----ELNMGQRCSDTRGI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 268 NFDD----STGWLVGEpGKGMAAMFTMMNTERVSVGIQGLGVGEaayqaaawyakdriqgRAL-SGPKYP-EQAA--DPI 339
Cdd:cd01157 211 TFEDvrvpKENVLIGE-GAGFKIAMGAFDKTRPPVAAGAVGLAQ----------------RALdEATKYAlERKTfgKLI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 340 IVHPDVRRMLMTMRAYNEGCR---ALSAWvsraldaekhspEPEVRQRASDFIAlmtpVVKALFTDLAFDSANLAVQCYG 416
Cdd:cd01157 274 AEHQAVSFMLADMAMKVELARlayQRAAW------------EVDSGRRNTYYAS----IAKAFAADIANQLATDAVQIFG 337
|
410 420 430
....*....|....*....|....*....|..
gi 644223274 417 GHGYIRESGVEQYARDARITMIYEGTNGVQAL 448
Cdd:cd01157 338 GNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL 369
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
161-270 |
4.17e-15 |
|
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: 71.16 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 161 TMCLTEPHCGTDLGLLRSRAVPQGDGSYKVTGSKIFIS-AGEHDlteniIHLVLARlPDAPKGVKGISLFLVPKYLPked 239
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIAD-----LFLVLAR-TGGDDRHGGISLFLVPKDAP--- 71
|
90 100 110
....*....|....*....|....*....|.
gi 644223274 240 gtpgqsnGVACAAIEHKMGLKASATCQMNFD 270
Cdd:pfam02770 72 -------GVSVRRIETKLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
40-156 |
2.29e-13 |
|
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: 66.72 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 40 AILEEAARFCRDVLLPINRSGDEEGchlengvvRTPAgfaQAYKQFAEGGWTALASDPEWGGQGLPEAVNKLVEEMICSS 119
Cdd:pfam02771 6 ALRDTVREFAEEEIAPHAAEWDEEG--------EFPR---ELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARA 74
|
90 100 110
....*....|....*....|....*....|....*...
gi 644223274 120 NLSFGLYPGLTHG-ATTAIEGHGSDALKQAYLPKMVSG 156
Cdd:pfam02771 75 DASVALALSVHSSlGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
68-443 |
8.68e-13 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 70.14 E-value: 8.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 68 ENGVVrtPAGFAQAykqFAEGGWTALASDPEWGGQGLPEAVNKLVEEMICSSNLSFGLYPG--LTHGATTaiegHGSD-A 144
Cdd:PRK12341 34 ENGTY--PREFMRA---LADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLITNgqCIHSMRR----FGSAeQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 145 LKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVpQGDGSYKVTGSKIFIS-AGEHDLTeniihLVLARLPDAPKGV 223
Cdd:PRK12341 105 LRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVYLNGQKTFITgAKEYPYM-----LVLARDPQPKDPK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 224 KGISLFLVPKYLPkedgtpgqsnGVACAAIeHKMGLKASATCQMNFDD---STGWLVGEPGKGMAAMFTMMNTERVSVGI 300
Cdd:PRK12341 179 KAFTLWWVDSSKP----------GIKINPL-HKIGWHMLSTCEVYLDNvevEESDLVGEEGMGFLNVMYNFEMERLINAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 301 QGLGVGEAAYQAAAWYAKDRIQ-GRAL-SGPKYPEQAADPIIVHPDVRRMLMTmraynegcralSAWvsralDAEKHSPe 378
Cdd:PRK12341 248 RSLGFAECAFEDAARYANQRIQfGKPIgHNQLIQEKLTLMAIKIENMRNMVYK-----------VAW-----QADNGQS- 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644223274 379 pevrqrasdfIALMTPVVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGTN 443
Cdd:PRK12341 311 ----------LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTD 365
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
4-34 |
2.70e-06 |
|
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam02770, pfam00441, pfam02771. This family is one of the enzymes involved in AcylCoA interaction in beta-oxidation.
Pssm-ID: 463571 Cd Length: 32 Bit Score: 43.87 E-value: 2.70e-06
10 20 30
....*....|....*....|....*....|.
gi 644223274 4 YDAPLRDMRFVLNELHADDGFGDIPALAEFT 34
Cdd:pfam12418 2 YKAPLRDMRFVLYEVLGAEALAALPGFADAD 32
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
141-271 |
3.16e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 43.30 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 141 GSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAVpQGDGSYKVTGSKIFISAGehdlTENIIHLVLARLPDAp 220
Cdd:PLN02526 125 GSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT-KVEGGWILNGQKRWIGNS----TFADVLVIFARNTTT- 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 644223274 221 kgvKGISLFLVPKylpkedGTPgqsnGVACAAIEHKMGLKASATCQMNFDD 271
Cdd:PLN02526 199 ---NQINGFIVKK------GAP----GLKATKIENKIGLRMVQNGDIVLKD 236
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
136-466 |
4.66e-04 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 43.09 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 136 AIEGHGSDALKQAYLPKMVSGQWSGTMCLTEPHCGTDLGLLRSRAV--PQGD----GSYKVTGSKIFISAGEHDLTENIi 209
Cdd:cd01150 112 AIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATydPLTQefviNTPDFTATKWWPGNLGKTATHAV- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 210 hlVLARL--PDAPKGVKGislFLVPKYLPKedgTPGQSNGVACAAIEHKMGLKA-------------------SATCQMN 268
Cdd:cd01150 191 --VFAQLitPGKNHGLHA---FIVPIRDPK---THQPLPGVTVGDIGPKMGLNGvdngflqfrnvriprenllNRFGDVS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 269 FDDSTGWLVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYAKDRIQgralSGPKyPEQAADPIIVHPDVRRM 348
Cdd:cd01150 263 PDGTYVSPFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQ----FGPK-PSDPEVQILDYQLQQYR 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 349 LMTMRA---------------YNEGCRALSAWVSRALdAEKHspepevrqrasdfiALMTPVvKALFTDLAFDSANLAVQ 413
Cdd:cd01150 338 LFPQLAaayafhfaakslvemYHEIIKELLQGNSELL-AELH--------------ALSAGL-KAVATWTAAQGIQECRE 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 644223274 414 CYGGHGYIRESGVEQYARDARITMIYEGTNGVqALDLVGRKLgahMGRYLRSF 466
Cdd:cd01150 402 ACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTV-LLQQTANYL---LKKYAQAF 450
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
98-233 |
1.94e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 41.02 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 98 EWGGQGLPEAVNKLVEEMICSSNLSfGLYPGLTHG--ATTAIEGHGSDALKQAYLPKMVSGQ----WSgtmclTEPHCGT 171
Cdd:PTZ00457 73 EYGGLGLGHTAHALIYEEVGTNCDS-KLLSTIQHSgfCTYLLSTVGSKELKGKYLTAMSDGTimmgWA-----TEEGCGS 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 172 DLGLLRSRAVPQGDGSYKVTGSK--IFISAGEHdlteniiHLVLARL------PDAPKGVKGISLFLVPK 233
Cdd:PTZ00457 147 DISMNTTKASLTDDGSYVLTGQKrcEFAASATH-------FLVLAKTltqtaaEEGATEVSRNSFFICAK 209
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
83-453 |
3.53e-03 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 40.20 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 83 KQFAEGGWTALASDPEWGGQGLP-EAVNKLVEEMICSSNLSFGLYPgLTHGATTAIEgHGSDALKQAYLPKMVSGQWSGT 161
Cdd:PRK03354 44 KALADMGIDSLLIPEEHGGLDAGfVTLAAVWMELGRLGAPTYVLYQ-LPGGFNTFLR-EGTQEQIDKIMAFRGTGKQMWN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 162 MCLTEPHCGTDLGLLRSrAVPQGDGSYKVTGSKIFISAGEHdlTENIIhlVLARLPDAPKgvKGI-SLFLVPKYLPkedg 240
Cdd:PRK03354 122 SAITEPGAGSDVGSLKT-TYTRRNGKVYLNGSKCFITSSAY--TPYIV--VMARDGASPD--KPVyTEWFVDMSKP---- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 241 tpgqsnGVACAAIeHKMGLKASATCQMNFDD---STGWLVGEPGKGMAAMFTMMNTERVSVGIQGLGVGEAAYQAAAWYA 317
Cdd:PRK03354 191 ------GIKVTKL-EKLGLRMDSCCEITFDDvelDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644223274 318 KDRIQ-GRALSGPKY-PEQAADPIIVHPDVRRMLMTmraynegcralSAWVSRAldaekhspepevrqrasdfiALMTP- 394
Cdd:PRK03354 264 NQRVQfGEAIGRFQLiQEKFAHMAIKLNSMKNMLYE-----------AAWKADN--------------------GTITSg 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 644223274 395 ---VVKALFTDLAFDSANLAVQCYGGHGYIRESGVEQYARDARITMIYEGTNGVQALDLvGR 453
Cdd:PRK03354 313 daaMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTL-GR 373
|
|
| |
