|
Name |
Accession |
Description |
Interval |
E-value |
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
41-451 |
0e+00 |
|
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: 771.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 41 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCdysvcplleactlyldaffllltgs 120
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDC------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 121 nlnlhlnlGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGS 200
Cdd:cd01157 56 --------GGLGLGTFDTCLITEELAYGCTGVQTAIEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 201 DVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDT 280
Cdd:cd01157 128 DVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 281 RGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMA 360
Cdd:cd01157 208 RGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 361 MKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQ 440
Cdd:cd01157 288 MKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQ 367
|
410
....*....|.
gi 554506556 441 RLIVAREHIDK 451
Cdd:cd01157 368 RLIISREHLGK 378
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
39-447 |
8.17e-149 |
|
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: 428.49 E-value: 8.17e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 39 FEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPEncdysvcpllEACTLYLDAFflllt 118
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPE----------EYGGLGLSLV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 119 gsnlnlhlnlgglglgtfDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGA 198
Cdd:COG1960 68 ------------------ELALVLEELARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 199 GSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELNMGQRCS 278
Cdd:COG1960 130 GSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPAAGH---RGISLFLVPKDTPGVTVGRIEDKMGLRGS 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 279 DTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAE 358
Cdd:COG1960 207 DTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 359 MAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 438
Cdd:COG1960 287 MAAELEAARALVYRAAWLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNE 366
|
....*....
gi 554506556 439 IQRLIVARE 447
Cdd:COG1960 367 IQRLIIARR 375
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
43-451 |
4.27e-143 |
|
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: 413.97 E-value: 4.27e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 43 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCDYSVCPLLeactlyldaffllltgsnl 122
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFL------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 123 nlhlnlgglglgtfDACLISEELAYGCTGVQTAIEG-NSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSD 201
Cdd:cd01158 62 --------------AYAIAIEELAKVDASVAVIVSVhNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 202 VAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKapaNKAFTGFIVEADTPGIQIGRKELNMGQRCSDTR 281
Cdd:cd01158 128 AAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSKG---YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 282 GIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAM 361
Cdd:cd01158 205 ELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 362 KVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQR 441
Cdd:cd01158 285 EIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQR 364
|
410
....*....|
gi 554506556 442 LIVAReHIDK 451
Cdd:cd01158 365 LVIAK-HLLK 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
43-446 |
4.72e-129 |
|
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: 376.24 E-value: 4.72e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 43 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGlmnthipencdysvcplleactlyldaffllltgsnl 122
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 123 nlhlnlgglglgtfdacliseelaygctgvqtaiegnslGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDV 202
Cdd:cd00567 44 ---------------------------------------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDL 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 203 AGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRG 282
Cdd:cd00567 85 AGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEG--PGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 283 IVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMK 362
Cdd:cd00567 163 LVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAE 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 363 VELARMSYQRAAWEVDSGRRN-TYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQR 441
Cdd:cd00567 243 LEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQR 322
|
....*
gi 554506556 442 LIVAR 446
Cdd:cd00567 323 LIIAR 327
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
42-447 |
7.47e-101 |
|
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: 306.29 E-value: 7.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 42 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCDYSVCPLLeactlyldaffllltgsn 121
Cdd:cd01162 2 NEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRL------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 122 lnlhlnlgglglgtfDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSD 201
Cdd:cd01162 64 ---------------DASIIFEALSTGCVSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 202 VAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDpdpkAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTR 281
Cdd:cd01162 129 AAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTG----GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 282 GIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAM 361
Cdd:cd01162 205 AVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 362 KVELARMSYQRAAWEVDSGRRN-TYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQ 440
Cdd:cd01162 285 ELVASRLMVRRAASALDRGDPDaVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIM 364
|
....*..
gi 554506556 441 RLIVARE 447
Cdd:cd01162 365 RLIIARA 371
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
41-447 |
5.89e-100 |
|
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: 303.95 E-value: 5.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 41 FTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPE-----NCDYsvcplleactlyldaffl 115
Cdd:cd01156 2 LDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEeyggsGMGY------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 116 lltgsnlnlhlnlgglglgtFDACLISEELAYGCTGVQTAIEGNS---LGQmpIIIAGNDQQKKKYLGRMTEEPLMCAYC 192
Cdd:cd01156 64 --------------------LAHVIIMEEISRASGSVALSYGAHSnlcINQ--IYRNGSAAQKEKYLPKLISGEHIGALA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 193 VTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGRKELN 272
Cdd:cd01156 122 MSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVYAKTDPSAGA---HGITAFIVEKGMPGFSRAQKLDK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 273 MGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAI 352
Cdd:cd01156 199 LGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 353 SFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQI 432
Cdd:cd01156 279 QGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEI 358
|
410
....*....|....*
gi 554506556 433 YEGTSQIQRLIVARE 447
Cdd:cd01156 359 GAGTSEIRRMVIGRE 373
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
43-447 |
3.82e-93 |
|
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: 286.32 E-value: 3.82e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 43 EQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPEncdysvcplleactlyldaffllltgsnl 122
Cdd:cd01160 1 EEHDAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPE----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 123 nlhlNLGGLGLGTFDACLISEELAY-GCTGVQTAIEgNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSD 201
Cdd:cd01160 52 ----EYGGIGGDLLSAAVLWEELARaGGSGPGLSLH-TDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 202 VAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFtgFIVEADTPGIQIGRKELNMGQRCSDTR 281
Cdd:cd01160 127 LQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEARGAGGISL--FLVERGTPGFSRGRKLKKMGWKAQDTA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 282 GIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAM 361
Cdd:cd01160 205 ELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELAT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 362 KVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQR 441
Cdd:cd01160 285 KVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMK 364
|
....*.
gi 554506556 442 LIVARE 447
Cdd:cd01160 365 ELISRQ 370
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
40-445 |
9.98e-82 |
|
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: 258.17 E-value: 9.98e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 40 EFTEQQKEFQATARKFAREEIIPvaAEYDKTGEYPVPLIRRAWELGLMNTHIPE--------NCDYSVCplleactlyld 111
Cdd:cd01161 26 EQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEeygglglnNTQYARL----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 112 affllltgsnlnlhlnlgglglgtfdACLISEELAYGCT-GVQTAIegnslGQMPIIIAGNDQQKKKYLGRMTEEPLMCA 190
Cdd:cd01161 93 --------------------------AEIVGMDLGFSVTlGAHQSI-----GFKGILLFGTEAQKEKYLPKLASGEWIAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 191 YCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWITNGGKANWYFLLARSD-PDPKAPANKAFTGFIVEADTPGIQIG 267
Cdd:cd01161 142 FALTEPSSGSDAASIRTTAVLSedGKHYVLNGSKIWITNGGIADIFTVFAKTEvKDATGSVKDKITAFIVERSFGGVTNG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 268 RKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLV 347
Cdd:cd01161 222 PPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 348 EHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYY--ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMR 425
Cdd:cd01161 302 EFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQieAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLR 381
|
410 420
....*....|....*....|
gi 554506556 426 DAKIYQIYEGTSQIQRLIVA 445
Cdd:cd01161 382 DLRIFRIFEGTNEILRLFIA 401
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
23-447 |
4.95e-73 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 235.54 E-value: 4.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 23 QHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYP--VPLIRRAWELGLMNTHIPEncdysvc 100
Cdd:PLN02519 8 ARRRGLARRFSSSSSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPkdVNLWKLMGDFNLHGITAPE------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 101 pllEACTLYLDAFFllltgsnlnlhlnlgglglgtfdACLISEEL--AYGCTGVQTAIEGNsLGQMPIIIAGNDQQKKKY 178
Cdd:PLN02519 81 ---EYGGLGLGYLY-----------------------HCIAMEEIsrASGSVGLSYGAHSN-LCINQLVRNGTPAQKEKY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 179 LGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPdpkAPANKAFTGFIVE 258
Cdd:PLN02519 134 LPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDV---AAGSKGITAFIIE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 259 ADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALE 338
Cdd:PLN02519 211 KGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 339 RKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEY 418
Cdd:PLN02519 291 REQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERATQVALQAIQCLGGNGYINEY 370
|
410 420
....*....|....*....|....*....
gi 554506556 419 PVEKLMRDAKIYQIYEGTSQIQRLIVARE 447
Cdd:PLN02519 371 PTGRLLRDAKLYEIGAGTSEIRRMLIGRE 399
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
35-447 |
8.74e-66 |
|
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: 216.07 E-value: 8.74e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 35 LGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPEncdYSvCPLLEACTLyldaff 114
Cdd:cd01151 7 LNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGATIKG---YG-CAGLSSVAY------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 115 llltgsnlnlhlnlgglglgtfdaCLISEELAYGCTGVQTAIE-GNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCV 193
Cdd:cd01151 77 ------------------------GLIAREVERVDSGYRSFMSvQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 194 TEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKapankaFTGFIVEADTPGIQIGRKELNM 273
Cdd:cd01151 133 TEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDETGK------IRGFILERGMKGLSAPKIQGKF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 274 GQRCSDTRGIVFEDVKVPKENVLIGdGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAIS 353
Cdd:cd01151 207 SLRASITGEIVMDNVFVPEENLLPG-AEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 354 FMLAEMAMKVELArmsyQRAAWEV----DSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKI 429
Cdd:cd01151 286 KKLADMLTEIALG----LLACLRVgrlkDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLES 361
|
410
....*....|....*...
gi 554506556 430 YQIYEGTSQIQRLIVARE 447
Cdd:cd01151 362 VNTYEGTHDIHALILGRA 379
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
136-440 |
5.41e-56 |
|
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: 191.06 E-value: 5.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 136 FDACLISEELAYGCTGvqtAIEGnslgqmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD- 214
Cdd:cd01153 76 FSRGDAPLMYASGTQG---AAAT-------LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADg 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 215 EYIINGQKMWITNGGKANW----YFLLARSDPDPkaPANKAFTGFIV-----EADTPGIQIGRKELNMGQRCSDTRGIVF 285
Cdd:cd01153 146 SWRINGVKRFISAGEHDMSenivHLVLARSEGAP--PGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSPTCELVF 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 286 EDVKVPkenvLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVE--------HQAISFML 356
Cdd:cd01153 224 DNAKGE----LIGEeGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 357 AEMAMKVELARMSYQRAAWEVDSGRR--------------NTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEK 422
Cdd:cd01153 300 MTQKAYAEGSRALDLYTATVQDLAERkategedrkalsalADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQ 379
|
330
....*....|....*...
gi 554506556 423 LMRDAKIYQIYEGTSQIQ 440
Cdd:cd01153 380 YYRDARITTIYEGTTGIQ 397
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
140-453 |
7.66e-56 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 189.94 E-value: 7.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 140 LISEELAYgcTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLgRMTEEPLMCAYC--VTEPGAGSDVAGIKTKAEKKGDEYI 217
Cdd:PRK12341 72 LVLEEVSK--CGAPAFLITNGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYAlaLTEPGAGSDNNSATTTYTRKNGKVY 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 218 INGQKMWITNGGKANWYFLLARsDPDPKAPaNKAFTGFIVEADTPGIQIGRKElNMGQRCSDTRGIVFEDVKVPKENVLI 297
Cdd:PRK12341 149 LNGQKTFITGAKEYPYMLVLAR-DPQPKDP-KKAFTLWWVDSSKPGIKINPLH-KIGWHMLSTCEVYLDNVEVEESDLVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 298 GDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEV 377
Cdd:PRK12341 226 EEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQA 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 554506556 378 DSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYK 453
Cdd:PRK12341 306 DNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQILKDYQ 381
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
141-446 |
4.80e-55 |
|
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: 187.55 E-value: 4.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 141 ISEELAYGCTGVQtaieGNSLGQM---PIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEY 216
Cdd:cd01152 71 FREEMAAAGAPVP----FNQIGIDlagPTILAyGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDW 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 217 IINGQKMWITNGGKANWYFLLARSDPDpkAPANKAFTGFIVEADTPGIQIgR--KELNMGqrcSDTRGIVFEDVKVPKEN 294
Cdd:cd01152 147 VVNGQKIWTSGAHYADWAWLLVRTDPE--APKHRGISILLVDMDSPGVTV-RpiRSINGG---EFFNEVFLDDVRVPDAN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 295 VLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDeatkYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAA 374
Cdd:cd01152 221 RVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLA----RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLA 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 375 WEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILG--------GNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 446
Cdd:cd01152 297 SALAAGKPPGAEASIAKLFGSELAQELAELALELLGtaallrdpAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAE 376
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
300-446 |
1.85e-53 |
|
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: 175.91 E-value: 1.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 300 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDS 379
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554506556 380 GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 446
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
42-436 |
4.37e-52 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 180.52 E-value: 4.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 42 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPEncdysvcpllEACTLYLDAFfllltgsn 121
Cdd:PTZ00461 38 TPEHAALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPE----------ADGGAGMDAV-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 122 lnlhlnlgglglgtfDACLISEELAYGCTGVQTAIEGNS-LGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGS 200
Cdd:PTZ00461 100 ---------------AAVIIHHELSKYDPGFCLAYLAHSmLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 201 DVAGIKTKAEKKGDE-YIINGQKMWITNGGKANWYFLLARSDpdpkapanKAFTGFIVEADTPGIQIGRKELNMGQRCSD 279
Cdd:PTZ00461 165 DVLGMRTTAKKDSNGnYVLNGSKIWITNGTVADVFLIYAKVD--------GKITAFVVERGTKGFTQGPKIDKCGMRASH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 280 TRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEM 359
Cdd:PTZ00461 237 MCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEG 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554506556 360 AMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGT 436
Cdd:PTZ00461 317 YADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
43-446 |
9.71e-46 |
|
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: 163.33 E-value: 9.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 43 EQQKEFQATARKFAREEIIPVAAEYDktgEYPVPLIRRAW--------------ELGLMNTHIPENCDysvcplLEACTl 108
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEFL---EYYAEGGDRWWtpppiieklkakakAEGLWNLFLPEVSG------LSGLT- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 109 yldaffllltgsnlnlhlnlgglglgTFDACLISEEL--------AYGCTGVQTaiegnslGQMPIIIA-GNDQQKKKYL 179
Cdd:cd01155 71 --------------------------NLEYAYLAEETgrsffapeVFNCQAPDT-------GNMEVLHRyGSEEQKKQWL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 180 grmteEPLM-----CAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGG--KANWYFLLARSDPDpKAPANKA 251
Cdd:cd01155 118 -----EPLLdgkirSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDPD-GAPRHRQ 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 252 FTGFIVEADTPGIQIGRKELNMGQrcSDTRG----IVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQR 327
Cdd:cd01155 192 QSMILVPMDTPGVTIIRPLSVFGY--DDAPHghaeITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAER 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 328 ALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIA--KAFAGDIANQLATDA 405
Cdd:cd01155 270 ALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKEIAmiKVAAPRMALKIIDRA 349
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 554506556 406 VQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 446
Cdd:cd01155 350 IQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
39-453 |
5.80e-41 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 149.98 E-value: 5.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 39 FEFTEQQKEFQATARKF-AREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCDYsvcplleactlyLDAFFLLL 117
Cdd:PRK03354 3 FNLNDEQELFVAGIRELmASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGG------------LDAGFVTL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 118 TGsnlnlhlnlgglglgtfdaclISEELayGCTGVQTAIegnsLGQMP-----IIIAGNDQQKKKYLGRMTEEPLMCAYC 192
Cdd:PRK03354 71 AA---------------------VWMEL--GRLGAPTYV----LYQLPggfntFLREGTQEQIDKIMAFRGTGKQMWNSA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 193 VTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPAnkaFTGFIVEADTPGIQIGRKElN 272
Cdd:PRK03354 124 ITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPV---YTEWFVDMSKPGIKVTKLE-K 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 273 MGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAI 352
Cdd:PRK03354 200 LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 353 SFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQI 432
Cdd:PRK03354 280 QEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRV 359
|
410 420
....*....|....*....|.
gi 554506556 433 YEGTSQIQRLIVAREHIDKYK 453
Cdd:PRK03354 360 SGGSDEMQILTLGRAVLKQYR 380
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
42-447 |
5.70e-40 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 148.08 E-value: 5.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 42 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPencDYSvCPLLEactlyldafflLLTGSN 121
Cdd:PLN02526 30 TPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTIK---GYG-CPGLS-----------ITASAI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 122 LNLHLNLGGLGLGTFdaCLISeelaygctgvqtaiegNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSD 201
Cdd:PLN02526 95 ATAEVARVDASCSTF--ILVH----------------SSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 202 VAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSdpdpkaPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTR 281
Cdd:PLN02526 157 ASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARN------TTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 282 GIVFEDVKVPKENVLIGDGAgFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAM 361
Cdd:PLN02526 231 DIVLKDVFVPDEDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 362 KVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQR 441
Cdd:PLN02526 310 NIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINA 389
|
....*.
gi 554506556 442 LIVARE 447
Cdd:PLN02526 390 LVTGRE 395
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
178-446 |
8.16e-35 |
|
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: 134.04 E-value: 8.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 178 YLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEK-KGDEYIINGQKmWITNGGKANWYFLLARsdPDPKAPANKAFTGFI 256
Cdd:cd01154 138 LLSDRYKTGLLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLAR--PEGAPAGARGLSLFL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 257 VEADTP-----GIQIGRKELNMGQRCSDTRGIVFEDVkvpkENVLIGD-GAGFKVAMGAFDKTRPVVAAGAVGLAQRALD 330
Cdd:cd01154 215 VPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA----EAYLIGDeGKGIYYILEMLNISRLDNAVAALGIMRRALS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 331 EATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAA--WEVDSGRRNTYYA------SIAKAFAGDIANQLA 402
Cdd:cd01154 291 EAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAraFDRAAADKPVEAHmarlatPVAKLIACKRAAPVT 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 554506556 403 TDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 446
Cdd:cd01154 371 SEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDVLR 414
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
162-439 |
4.74e-32 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 129.53 E-value: 4.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 162 GQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLAR 239
Cdd:PLN02876 524 GNMEVLLRyGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVM 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 240 SDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGqrCSDT----RGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRP 315
Cdd:PLN02876 604 GKTDFNAPKHKQQSMILVDIQTPGVQIKRPLLVFG--FDDAphghAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRL 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 316 VVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVD--SGRRNTYYASIAKAF 393
Cdd:PLN02876 682 HHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlGNKKARGIIAMAKVA 761
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 554506556 394 AGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQI 439
Cdd:PLN02876 762 APNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
190-286 |
7.13e-30 |
|
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: 111.60 E-value: 7.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 190 AYCVTEPGAGSDVAGIKTKA-EKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKApanKAFTGFIVEADTPGIQIGR 268
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRH---GGISLFLVPKDAPGVSVRR 77
|
90
....*....|....*...
gi 554506556 269 KELNMGQRCSDTRGIVFE 286
Cdd:pfam02770 78 IETKLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
42-182 |
1.16e-27 |
|
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: 106.01 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 42 TEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPE-----NCDYsvcplleactlyldaffll 116
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEeyggaGLDY------------------- 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554506556 117 ltgsnlnlhlnlgglglgtFDACLISEELAYGCTGVQTAIE-GNSLGQMPIIIAGNDQQKKKYLGRM 182
Cdd:pfam02771 62 -------------------LAYALVAEELARADASVALALSvHSSLGAPPILRFGTEEQKERYLPKL 109
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
158-442 |
1.06e-20 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 94.93 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 158 GNSLGQMPIIIA-GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGG---KAN 232
Cdd:PTZ00456 151 GLSIGAANTLMAwGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDhdlTEN 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 233 -WYFLLARSDPDPkaPANKAFTGFIVEADTP----------GIQIGRKELNMGQRCSDTRGIVFEDVKvpkeNVLIGD-G 300
Cdd:PTZ00456 231 iVHIVLARLPNSL--PTTKGLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGIKGSSTCQLSFENSV----GYLIGEpN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 301 AGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF------------GKLLVEHQAISFML------AE--MA 360
Cdd:PTZ00456 305 AGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARERRSMralsgtkepekpADRIICHANVRQNIlfakavAEggRA 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 361 MKVELAR-MSYQRAAWEVDS----GRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEG 435
Cdd:PTZ00456 385 LLLDVGRlLDIHAAAKDAATrealDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEG 464
|
....*..
gi 554506556 436 TSQIQRL 442
Cdd:PTZ00456 465 TTGIQAL 471
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
316-438 |
6.00e-19 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 82.78 E-value: 6.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 316 VVAAGAVGLAQRALDEATKYALERKT--FGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWE----VDSGRRNTYY--- 386
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARieaaAAAGKPVTPAlra 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 554506556 387 -ASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQ 438
Cdd:pfam08028 81 eARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
164-453 |
4.87e-14 |
|
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: 74.29 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 164 MPIIIA-GNDQQKKKYL-GRMTEEPLMCaYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGK-ANW 233
Cdd:cd01150 110 GNAIKNlGTDEHQDYWLqGANNLEIIGC-FAQTELGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNLGKtATH 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 234 YFLLARSDPDPKapaNKAFTGFIV---EADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG 300
Cdd:cd01150 189 AVVFAQLITPGK---NHGLHAFIVpirDPKThqplPGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLnrfgdvSPDG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 301 A----------GFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG--------KLLvEHQ------------ 350
Cdd:cd01150 266 TyvspfkdpnkRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGpkpsdpevQIL-DYQlqqyrlfpqlaa 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 351 --AISFMLAEMAMKVelarMSYQRAAWEVDSGRRNTYYASIA--KAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRD 426
Cdd:cd01150 345 ayAFHFAAKSLVEMY----HEIIKELLQGNSELLAELHALSAglKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDD 420
|
330 340
....*....|....*....|....*..
gi 554506556 427 AKIYQIYEGTSQIQRLIVAREHIDKYK 453
Cdd:cd01150 421 NDPFCTYEGDNTVLLQQTANYLLKKYA 447
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
194-446 |
5.16e-13 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 70.94 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 194 TEPGAGSDVAGIKTKAEKKGDE-YIINGQKmwitnggkanWYFLLARSDPD-PKAPANKAFTGFIVEADTP-----GIQI 266
Cdd:PRK11561 185 TEKQGGSDVLSNTTRAERLADGsYRLVGHK----------WFFSVPQSDAHlVLAQAKGGLSCFFVPRFLPdgqrnAIRL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 267 GRKELNMGQRCSDTRGIVFEDVK---VPKEnvliGDGAGFKVAMGAFdkTRPVVAAGAVGLAQRALDEATKYALERKTFG 343
Cdd:PRK11561 255 ERLKDKLGNRSNASSEVEFQDAIgwlLGEE----GEGIRLILKMGGM--TRFDCALGSHGLMRRAFSVAIYHAHQRQVFG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 344 KLLVEHQAISFMLAEMAMKVE--------LARMSYQRA-AWEVDSGRRNTYYA--SIAKAFAGDIAnqlatDAVQILGGN 412
Cdd:PRK11561 329 KPLIEQPLMRQVLSRMALQLEgqtallfrLARAWDRRAdAKEALWARLFTPAAkfVICKRGIPFVA-----EAMEVLGGI 403
|
250 260 270
....*....|....*....|....*....|....
gi 554506556 413 GFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAR 446
Cdd:PRK11561 404 GYCEESELPRLYREMPVNSIWEGSGNIMCLDVLR 437
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
208-427 |
3.35e-10 |
|
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: 61.60 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 208 KAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFtgFIVEADtpgIQIGRKELNMGQRCSDTRGIVFED 287
Cdd:cd01159 112 RAERVDGGYRVSGTWPFASGCDHADWILVGAIVEDDDGGPLPRAF--VVPRAE---YEIVDTWHVVGLRGTGSNTVVVDD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 288 VKVPKENVLIGDGA-----------GFKVAMGAFDKtrPVVAAGAVGLAQRALDEATKYALER---KTFGKLLVEHQAIS 353
Cdd:cd01159 187 VFVPEHRTLTAGDMmagdgpggstpVYRMPLRQVFP--LSFAAVSLGAAEGALAEFLELAGKRvrqYGAAVKMAEAPITQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 354 FMLAEMAMKVELARMSYQRAAWEVDS---------------GRRNTYYASIAKAFAGDIANQLAtdavqilGGNGFNTEY 418
Cdd:cd01159 265 LRLAEAAAELDAARAFLERATRDLWAhalaggpidveerarIRRDAAYAAKLSAEAVDRLFHAA-------GGSALYTAS 337
|
....*....
gi 554506556 419 PVEKLMRDA 427
Cdd:cd01159 338 PLQRIWRDI 346
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
166-428 |
2.69e-09 |
|
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: 58.87 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 166 IIIAGNDQQKKKYLGRMTEEPLM-CAycVTEPGaGSDVAGIKTKAEKKGDEYIINGQKmWITNGGKANWYFLLARSDPDP 244
Cdd:cd01163 83 LLLAGPEQFRKRWFGRVLNGWIFgNA--VSERG-SVRPGTFLTATVRDGGGYVLNGKK-FYSTGALFSDWVTVSALDEEG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 245 KApankafTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAM-GAFDKTrpVVAAGAVG 323
Cdd:cd01163 159 KL------VFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPRPNAPDRGTLlTAIYQL--VLAAVLAG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 324 LAQRALDEATKYALER-KTFGKLLVEH--------QAIsfmlAEMAMKVELARMSYQRAAWEVD----SGRRNTYYASI- 389
Cdd:cd01163 231 IARAALDDAVAYVRSRtRPWIHSGAESarddpyvqQVV----GDLAARLHAAEALVLQAARALDaaaaAGTALTAEARGe 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 554506556 390 -------AKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAK 428
Cdd:cd01163 307 aalavaaAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNAR 352
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
151-343 |
8.98e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 57.56 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 151 GVQTAIEGNSlgqmpIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKM 223
Cdd:PLN02636 142 GVQYSLWGGS-----VINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVINtpndgAIKW 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 224 WITNG---GK-ANWYFLLARSDPDPKAPANKAFTGFIV-------EADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPK 292
Cdd:PLN02636 217 WIGNAavhGKfATVFARLKLPTHDSKGVSDMGVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 554506556 293 ENVL--IGD--------------GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG 343
Cdd:PLN02636 297 DNLLnrFGDvsrdgkytsslptiNKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFG 363
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
170-343 |
3.21e-08 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 56.00 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 170 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITNGGKANWYFLL-ARSD 241
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGLGKVSTHAVVyARLI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 242 PDPKapaNKAFTGFIVEADT-------PGI---QIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------------IGD 299
Cdd:PLN02443 194 TNGK---DHGIHGFIVQLRSlddhsplPGVtvgDIGMKFGNGAYNTMDNGFLRFDHVRIPRDQMLmrlskvtregkyVQS 270
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 554506556 300 GAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFG 343
Cdd:PLN02443 271 DVPRQLVYGTMVYVRQTIVADASTALSRAVCIATRYSAVRRQFG 314
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
159-413 |
5.05e-08 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 55.35 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 159 NSLGQMPIIIA-GNDQQKKKYLGRM---TEEPlmCaYCVTEPGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWIT 226
Cdd:PRK13026 163 NSLGPGELLTHyGTQEQKDYWLPRLadgTEIP--C-FALTGPEAGSDAGaipdtGIVCRGEFEGEEVLglrLTWDKRYIT 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 227 NGGKANWYFLLAR-SDPDP--KAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSD--TRGivfEDVKVPKEnVLIGD-- 299
Cdd:PRK13026 240 LAPVATVLGLAFKlRDPDGllGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNgtTRG---KDVFIPLD-WIIGGpd 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 300 --GAGFKVAMGAFDKTRPV-VAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMK---VELARMSYQRA 373
Cdd:PRK13026 316 yaGRGWRMLVECLSAGRGIsLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNtylLEAARRLTTTG 395
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 554506556 374 aweVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNG 413
Cdd:PRK13026 396 ---LDLGVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
170-413 |
1.07e-07 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 54.44 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 170 GNDQQKKKYLGRM---TEEPlmCaYCVTEPGAGSDVA-----GIKTKAEKKGDEYI---INGQKMWITNG------GKAn 232
Cdd:PRK09463 176 GTDEQKDHYLPRLargEEIP--C-FALTSPEAGSDAGsipdtGVVCKGEWQGEEVLgmrLTWNKRYITLApiatvlGLA- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 233 wyFLLarSDPDpkapankaftGFI------------VEADTPGIQIGRKELNMGQRCSD--TRGivfEDVKVPKENVlIG 298
Cdd:PRK09463 252 --FKL--YDPD----------GLLgdkedlgitcalIPTDTPGVEIGRRHFPLNVPFQNgpTRG---KDVFIPLDYI-IG 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 299 D----GAGFKVAMGAFDKTR----PVVAAGAVGLAQRAldeATKYALERKTFGKLLVEHQAISFMLAEMAMKvelarmsy 370
Cdd:PRK09463 314 GpkmaGQGWRMLMECLSVGRgislPSNSTGGAKLAALA---TGAYARIRRQFKLPIGKFEGIEEPLARIAGN-------- 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 554506556 371 qraAWEVDSGRRNTYYA-----------SIAKAFAGDIANQLATDAVQILGGNG 413
Cdd:PRK09463 383 ---AYLMDAARTLTTAAvdlgekpsvlsAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
170-342 |
1.32e-07 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 54.01 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 170 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWItnGGKAN---WYFLLAR 239
Cdd:PLN02312 168 GTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQKYWI--GGAANhatHTIVFSQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 240 SDPDPKAPANKAFTGFIVEAD---TPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL------IGDG---------- 300
Cdd:PLN02312 246 LHINGKNEGVHAFIAQIRDQDgniCPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLnsvadvSPDGkyvsaikdpd 325
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 554506556 301 AGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF 342
Cdd:PLN02312 326 QRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
140-331 |
6.57e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 48.34 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 140 LISEELAYGCTGVQTAIEGNSlGQMPIIIA--GNDQQKKKYLGRMTEEPLMCAYCVTEpGAGSDVAGIKTKAEKKGD-EY 216
Cdd:PTZ00457 86 LIYEEVGTNCDSKLLSTIQHS-GFCTYLLStvGSKELKGKYLTAMSDGTIMMGWATEE-GCGSDISMNTTKASLTDDgSY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 217 IINGQKMWItNGGKANWYFLLAR------SDPDPKAPANKAFtgFIVEADTPGIQIgrkelnmgqrcsDTRGIVFEDvkV 290
Cdd:PTZ00457 164 VLTGQKRCE-FAASATHFLVLAKtltqtaAEEGATEVSRNSF--FICAKDAKGVSV------------NGDSVVFEN--T 226
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 554506556 291 PKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDE 331
Cdd:PTZ00457 227 PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQE 267
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
170-342 |
1.13e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 47.92 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 170 GNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKA--EKKGDEYIIN-----GQKMWITN-GGKANWYFLLARSD 241
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554506556 242 PDPKAPANKAFTGFIVEADT----PGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVL-----IGDGAGF------KVA 306
Cdd:PTZ00460 190 VNGKNKGVHPFMVRIRDKEThkplQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLaryikVSEDGQVerqgnpKVS 269
|
170 180 190
....*....|....*....|....*....|....*.
gi 554506556 307 MGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTF 342
Cdd:PTZ00460 270 YASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQF 305
|
|
| |
