|
Name |
Accession |
Description |
Interval |
E-value |
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
16-403 |
5.14e-98 |
|
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: 297.35 E-value: 5.14e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 16 FYSDLYNYAEDLTDGEKEVLQEVEKVLKEDIYPVLDEHWDKATFPLEEMQKIIDIDLIQNPklLEGREDGTISQLFRGFR 95
Cdd:cd01151 2 NWEDPLNLDDLLTEEERAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT--IKGYGCAGLSSVAYGLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 96 AYTLAKTDPVIGTFYTSNGGLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDiAGGMAATAKREGDTWILN 175
Cdd:cd01151 80 AREVERVDSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSD-PGGMETRARKDGGGYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 176 GHKKWIGGGTLAKWHAFFARDVDDGQVKMFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPESQRAQNVNSWKDA 255
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARNDETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAEGLRGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 256 ANILRNTRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEEN 335
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 984928820 336 SSMAKMHNGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGRYYTGQQAF 403
Cdd:cd01151 319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHALILGRAITGIQAF 386
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
26-402 |
7.52e-91 |
|
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: 278.65 E-value: 7.52e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 26 DLTDGEKEVLQEVEKVLKEDIYPVLDEHWDKATFPLEEMQKIIDIDL--IQNPKLLEGREdGTISQLFRGFRAytLAKTD 103
Cdd:COG1960 4 ELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLlgLTIPEEYGGLG-LSLVELALVLEE--LARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 104 PVIGTFYTSNGGlFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDiAGGMAATAKREGDTWILNGHKKWIGG 183
Cdd:COG1960 81 ASLALPVGVHNG-AAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSD-AAALRTTAVRDGDGYVLNGQKTFITN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 184 GTLAKWHAFFARDVDDGQVK---MFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPESQRAQNVN-SWKDAANIL 259
Cdd:COG1960 159 APVADVILVLARTDPAAGHRgisLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGkGFKIAMSTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 260 RNTRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSSMA 339
Cdd:COG1960 239 NAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMA 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984928820 340 KMHNGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGRYYTGQQA 402
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
18-403 |
1.37e-83 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 261.33 E-value: 1.37e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 18 SDLYNYAEDLTDGEKEVLQEVEKVLKEDIYPVLDEHWDKATFPLEEMQKIIDIdliqnpklleGREDGTI--------SQ 89
Cdd:PLN02526 20 SDYYQFDDLLTPEEQALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSL----------GIAGGTIkgygcpglSI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 90 LFRGFRAYTLAKTDPVIGTFYTSNGGLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDiAGGMAATAKREG 169
Cdd:PLN02526 90 TASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSD-ASSLNTTATKVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 170 DTWILNGHKKWIGGGTLAKWHAFFARDVDDGQVKMFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPESQRAQNV 249
Cdd:PLN02526 169 GGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 250 NSWKDAANILRNTRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERG 329
Cdd:PLN02526 249 NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESG 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984928820 330 IYKEENSSMAKMHNGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGRYYTGQQAF 403
Cdd:PLN02526 329 KMTPGHASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREITGIASF 402
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
123-395 |
1.44e-66 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 214.46 E-value: 1.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 123 IGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGgMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFAR----DVD 198
Cdd:cd00567 50 AYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAG-IRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARtdeeGPG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 199 DGQVKMFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPESQRAQNVNS-WKDAANILRNTRSDVAWLLAGATAGA 277
Cdd:cd00567 129 HRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGgFELAMKGLNVGRLLLAAVALGAARAA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 278 FEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAI---AVRLAQQQERGIykEENSSMAKMHNGYRARENAALA 354
Cdd:cd00567 209 LDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLlyrAAWLLDQGPDEA--RLEAAMAKLFATEAAREVADLA 286
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 984928820 355 REVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:cd00567 287 MQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
29-395 |
6.08e-52 |
|
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: 177.85 E-value: 6.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 29 DGEKEVLQEVEKVLKEDIYPVLDEHWDKATFPLEEMQKIIDIDL--IQNPKLLEGREDGtisqlfrgFRAYT-----LAK 101
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLmgIPIPEEYGGAGLD--------FLAYAiaieeLAK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 102 TDPVIGTFYTSNGGLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDiAGGMAATAKREGDTWILNGHKKWI 181
Cdd:cd01158 73 VDASVAVIVSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSD-AAALKTTAKKDGDDYVLNGSKMWI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 182 GGGTLAKWHAFFAR-DVDDGQ--VKMFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPESQRAQNVN-SWKDAAN 257
Cdd:cd01158 152 TNGGEADFYIVFAVtDPSKGYrgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGeGFKIAMQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 258 ILRNTRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSS 337
Cdd:cd01158 232 TLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAA 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 984928820 338 MAKMHNGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:cd01158 312 MAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAK 369
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
10-393 |
8.30e-42 |
|
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: 151.85 E-value: 8.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 10 DAVEKMFYSDLYNYAEDLTDGEKEVLQEVEKVLKEDIYPVLDEHWDKatFPLEEMQKIIDIDL--IQNPKLLEGREDGTI 87
Cdd:cd01161 10 DIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEK--IPRKTLTQLKELGLfgLQVPEEYGGLGLNNT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 88 SQLfrgfRAYTLAKTDPVIGTFYTSNGGLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDiAGGMAATAKR 167
Cdd:cd01161 88 QYA----RLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSD-AASIRTTAVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 168 --EGDTWILNGHKKWIGGGTLAKWHAFFAR---DVDDGQVK----MFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDV 238
Cdd:cd01161 163 seDGKHYVLNGSKIWITNGGIADIFTVFAKtevKDATGSVKdkitAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 239 KVPESQRAQNV-NSWKDAANILRNTRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLA 317
Cdd:cd01161 243 KIPVENVLGEVgDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATES 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 318 IAVRLAQQQERGIYKEEN--SSMAKMHngyrARENAAL----AREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSL 391
Cdd:cd01161 323 MAYMTSGNMDRGLKAEYQieAAISKVF----ASEAAWLvvdeAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
..
gi 984928820 392 II 393
Cdd:cd01161 399 FI 400
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
27-400 |
3.74e-39 |
|
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: 143.88 E-value: 3.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 27 LTDGEKEVLQEVEKVLKEDIYPVLDEHWDKATFPLEEMQKIIDIDLIQN--PKLLEGREDGTISQLFRgfrAYTLAKTDP 104
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNThiPEDCGGLGLGTFDTCLI---TEELAYGCT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 105 VIGTFYTSNGgLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGgMAATAKREGDTWILNGHKKWIGGG 184
Cdd:cd01157 78 GVQTAIEANS-LGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAG-IKTKAEKKGDEYIINGQKMWITNG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 185 TLAKWHAFFARDVDDGQVKM------FFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPesqrAQNV-----NSWK 253
Cdd:cd01157 156 GKANWYFLLARSDPDPKCPAskaftgFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVP----KENVligegAGFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 254 DAANILRNTRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKE 333
Cdd:cd01157 232 IAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNT 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 984928820 334 ENSSMAKMHNGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGRYYTGQ 400
Cdd:cd01157 312 YYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
125-395 |
6.46e-37 |
|
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: 138.02 E-value: 6.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGgMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFARDVDDGQ--- 201
Cdd:cd01160 95 GSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQG-IRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGGEARgag 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 202 -VKMFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPESQRAQNVNswKDAANILRNTRSDVAWLLAGATAGA--- 277
Cdd:cd01160 174 gISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEEN--KGFYYLMQNLPQERLLIAAGALAAAefm 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 278 FEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSSMAKMHNGYRARENAALAREV 357
Cdd:cd01160 252 LEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAYECVQL 331
|
250 260 270
....*....|....*....|....*....|....*...
gi 984928820 358 CGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:cd01160 332 HGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
125-395 |
1.27e-35 |
|
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: 134.49 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDiAGGMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFARDVDDGQ--V 202
Cdd:cd01162 97 GNDEQRERFLPDLCTMEKLASYCLTEPGSGSD-AAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTGGEGPkgI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 203 KMFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVP-ESQRAQNVNSWKDAANILRNTRSDVAWLLAGATAGAFEAA 281
Cdd:cd01162 176 SCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPvENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 282 LKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERG-IYKEENSSMAKMHNGYRARENAALAREVCGG 360
Cdd:cd01162 256 RAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGdPDAVKLCAMAKRFATDECFDVANQALQLHGG 335
|
250 260 270
....*....|....*....|....*....|....*
gi 984928820 361 NGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:cd01162 336 YGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIAR 370
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
125-395 |
2.79e-35 |
|
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: 133.69 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGgMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFAR-DVDDGQ-- 201
Cdd:cd01156 99 GSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVS-MKLRAEKKGDRYVLNGSKMWITNGPDADTLVVYAKtDPSAGAhg 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 202 VKMFFVERESEGvetFNTEP---KAFFRMMPNAEIIYTDVKVPESQRAQNVNSwkdAANILRNTRSDVAWLLAGATAG-- 276
Cdd:cd01156 178 ITAFIVEKGMPG---FSRAQkldKLGMRGSNTCELVFEDCEVPEENILGGENK---GVYVLMSGLDYERLVLAGGPIGim 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 277 --AFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSSMAKMHNGYRARENAALA 354
Cdd:cd01156 252 qaALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAAEKATQVALDA 331
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 984928820 355 REVCGGNGILLEYDVPRFMADIEgmyTYE---GTHEVNSLIIGR 395
Cdd:cd01156 332 IQILGGNGYINDYPTGRLLRDAK---LYEigaGTSEIRRMVIGR 372
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
109-395 |
6.67e-30 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 118.68 E-value: 6.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 109 FYTSNGGLFHECVKIGgSKEQQEKLMPGVLsweGKG----VLAMTEPEHGSDiAGGMAATAKREGDTWILNGHKKWIGGG 184
Cdd:PRK12341 85 FLITNGQCIHSMRRFG-SAEQLRKTAESTL---ETGdpayALALTEPGAGSD-NNSATTTYTRKNGKVYLNGQKTFITGA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 185 TLAKWHAFFARDVDDGQVK----MFFVERESEGVeTFNTEPKAFFRMMPNAEIIYTDVKVPESQRAqNVNSWkDAANILR 260
Cdd:PRK12341 160 KEYPYMLVLARDPQPKDPKkaftLWWVDSSKPGI-KINPLHKIGWHMLSTCEVYLDNVEVEESDLV-GEEGM-GFLNVMY 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 261 N---TRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSS 337
Cdd:PRK12341 237 NfemERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAA 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 984928820 338 MAKMHNGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:PRK12341 317 LAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGR 374
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
125-395 |
8.95e-29 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 115.70 E-value: 8.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIaGGMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFARDVDDGQVKM 204
Cdd:PRK03354 101 GTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDV-GSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 205 F---FVERESEGVeTFNTEPKAFFRMMPNAEIIYTDVKVPESQR-AQNVNSWKDAANILRNTRSDVAWLLAGATAGAFEA 280
Cdd:PRK03354 180 YtewFVDMSKPGI-KVTKLEKLGLRMDSCCEITFDDVELDEKDMfGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFED 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 281 ALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSSMAKMHNGYRARENAALAREVCGG 360
Cdd:PRK03354 259 AARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGG 338
|
250 260 270
....*....|....*....|....*....|....*
gi 984928820 361 NGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:PRK03354 339 VGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGR 373
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
125-395 |
4.58e-28 |
|
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: 113.60 E-value: 4.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGgMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFARdvDDGQVK- 203
Cdd:cd01152 100 GTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAG-LRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVR--TDPEAPk 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 204 -----MFFVERESEGVET---FNTEPKAFFrmmpnAEIIYTDVKVPESQRAQNVNS-WKDAANILRNTRSdvawLLAGAT 274
Cdd:cd01152 177 hrgisILLVDMDSPGVTVrpiRSINGGEFF-----NEVFLDDVRVPDANRVGEVNDgWKVAMTTLNFERV----SIGGSA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 275 AGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSSMAKMHNGYRARENAALA 354
Cdd:cd01152 248 ATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELA 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 984928820 355 REVCGGNGILLE-YDVPRFMADIEGMY-------TYEGTHEVNSLIIGR 395
Cdd:cd01152 328 LELLGTAALLRDpAPGAELAGRWEADYlrsrattIYGGTSEIQRNIIAE 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
125-395 |
1.58e-27 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 112.66 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGgMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFAR-DVDDGQ-- 201
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVS-MKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKtDVAAGSkg 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 202 VKMFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPESqraqnvnswkdaaNILRNTRSDVAWLLAG--------- 272
Cdd:PLN02519 204 ITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEE-------------NVLGQEGKGVYVMMSGldlerlvla 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 273 -----ATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSSMAKMHNGYRA 347
Cdd:PLN02519 271 agplgLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCAGVILCAAERA 350
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 984928820 348 RENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:PLN02519 351 TQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGR 398
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
252-395 |
2.91e-27 |
|
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: 105.80 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 252 WKDAANILRNTRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIY 331
Cdd:pfam00441 4 FRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984928820 332 KEENSSMAKMHNGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:pfam00441 84 DGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
97-387 |
3.59e-22 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 97.32 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 97 YTLAKTDPVIGTFYTSNGGLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGgMAATAKREGD-TWILN 175
Cdd:PTZ00461 106 HELSKYDPGFCLAYLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLG-MRTTAKKDSNgNYVLN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 176 GHKKWIGGGTLAKWHAFFARdvDDGQVKMFFVERESEGVETFNTEPKAFFRMMPNAEIIYTDVKVPesqrAQNV--NSWK 253
Cdd:PTZ00461 185 GSKIWITNGTVADVFLIYAK--VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVP----AENLlgEEGK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 254 DAANILRN---TRSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGI 330
Cdd:PTZ00461 259 GMVGMMRNlelERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGN 338
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 984928820 331 YKEENSSMAKMHNGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHE 387
Cdd:PTZ00461 339 KNRLGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
125-391 |
3.56e-20 |
|
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: 91.66 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKlMPGVLS----WEGKGVLAMTEPEHGSDIAGGMAATAKREGDTWILNGHKkWIGGGTLAKWHAFFAR--DVD 198
Cdd:cd01154 127 GPEELKQY-LPGLLSdrykTGLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHK-WFASAPLADAALVLARpeGAP 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 199 DGQ--VKMFFVERESE-----GVETFNTEPKAFFRMMPNAEIIYTDVkvpESQR-AQNVNSWKDAANILRNTRSDVAWLL 270
Cdd:cd01154 205 AGArgLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATGEVEFDDA---EAYLiGDEGKGIYYILEMLNISRLDNAVAA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 271 AGATAGAFEAALKYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQ-QERGIYKEENSSMA-------KMH 342
Cdd:cd01154 282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAfDRAAADKPVEAHMArlatpvaKLI 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 984928820 343 NGYRARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSL 391
Cdd:cd01154 362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
146-235 |
2.49e-18 |
|
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: 79.25 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 146 LAMTEPEHGSDIAGGMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFARDVDD---GQVKMFFVERESEGVETFNTEPK 222
Cdd:pfam02770 2 FALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDdrhGGISLFLVPKDAPGVSVRRIETK 81
|
90
....*....|...
gi 984928820 223 AFFRMMPNAEIIY 235
Cdd:pfam02770 82 LGVRGLPTGELVF 94
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
125-395 |
6.59e-16 |
|
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: 78.97 E-value: 6.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGGMAATAKREGDTWILNGHKKWIGGGTLAKW----HAFFARDVDDG 200
Cdd:cd01153 100 GTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGEHDMSenivHLVLARSEGAP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 201 Q----VKMFFVER-----ESEGVETFNTEPKAFFRMMPNAEIIYTDVKVP---ESQRAqnvnsWKDAANILRNTRSDVAW 268
Cdd:cd01153 180 PgvkgLSLFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGEligEEGMG-----LAQMFAMMNGARLGVGT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 269 LLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKLS----RMAMNAQATL----------AIAVRLAQQQE-----RG 329
Cdd:cd01153 255 QGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIIHHpdvrRSLMTQKAYAegsraldlytATVQDLAERKAtegedRK 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 330 IYKEENSSMAKMHNGY---RARENAALAREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSL-IIGR 395
Cdd:cd01153 335 ALSALADLLTPVVKGFgseAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGR 404
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
125-395 |
3.46e-12 |
|
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: 67.41 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGGMAATAKREGDTWILNGHKKWIGGGT--LAKWHAFFARDVDDG-- 200
Cdd:cd01155 108 GSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDPDGap 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 201 ---QVKMFFVERESEGVETfntepkafFRMMP----------NAEIIYTDVKVPesqrAQNV-----NSWKDAANILRNT 262
Cdd:cd01155 188 rhrQQSMILVPMDTPGVTI--------IRPLSvfgyddaphgHAEITFDNVRVP----ASNLilgegRGFEIAQGRLGPG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 263 RSDVAWLLAGATAGAFEAALKYTREREAFGKTVASFQLIQEKL--SRMAMNaQA---TLAIAVRLAQQQERGIYKEenSS 337
Cdd:cd01155 256 RIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIakSRIEIE-QArllVLKAAHMIDTVGNKAARKE--IA 332
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984928820 338 MAKMhngyrARENAAL-----AREVCGGNGILLEYDVPRFMADIEGMYTYEGTHEVNSLIIGR 395
Cdd:cd01155 333 MIKV-----AAPRMALkiidrAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIAR 390
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
113-396 |
8.90e-08 |
|
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: 54.26 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 113 NGGLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAG-GMAATAKREGDTWILN-----GHKKWIGG-GT 185
Cdd:cd01150 105 HLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGlETTATYDPLTQEFVINtpdftATKWWPGNlGK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 186 LAKWHAFFARDVDDGQ---VKMFFVE-RESE------GVETFNTEPKAFFRMMPNAEIIYTDVKVPE-------SQRA-- 246
Cdd:cd01150 185 TATHAVVFAQLITPGKnhgLHAFIVPiRDPKthqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRenllnrfGDVSpd 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 247 -QNVNSWKDaaNILR-----NTRSDVAWLLAGATAG----AFEAALKYTREREAFGKT-------VASFQLIQEKLsrma 309
Cdd:cd01150 265 gTYVSPFKD--PNKRygamlGTRSGGRVGLIYDAAMslkkAATIAIRYSAVRRQFGPKpsdpevqILDYQLQQYRL---- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 310 MNAQATlAIAVRLAQQQERGIYKEEN-----------------SSMAKMHNGYRARENAALAREVCGGNGILLEYDVPRF 372
Cdd:cd01150 339 FPQLAA-AYAFHFAAKSLVEMYHEIIkellqgnsellaelhalSAGLKAVATWTAAQGIQECREACGGHGYLAMNRLPTL 417
|
330 340
....*....|....*....|....
gi 984928820 373 MADIEGMYTYEGTHEVNSLIIGRY 396
Cdd:cd01150 418 RDDNDPFCTYEGDNTVLLQQTANY 441
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
125-363 |
9.50e-08 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 54.03 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAGGMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFARDVDD----- 199
Cdd:PLN02876 533 GNKEQQLEWLIPLLEGKIRSGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKTDfnapk 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 200 -GQVKMFFVERESEGVET--------FNTEPKAffrmmpNAEIIYTDVKVPesqrAQNV-----NSWKDAANILRNTRSD 265
Cdd:PLN02876 613 hKQQSMILVDIQTPGVQIkrpllvfgFDDAPHG------HAEISFENVRVP----AKNIllgegRGFEIAQGRLGPGRLH 682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 266 VAWLLAGATAGAFEAALKYTREREAFGKTVA---SF-------QLIQEKLSRMAMNAQATLAiavRLAQQQERGIYkeen 335
Cdd:PLN02876 683 HCMRLIGAAERGMQLMVQRALSRKAFGKLIAqhgSFlsdlakcRVELEQTRLLVLEAADQLD---RLGNKKARGII---- 755
|
250 260 270
....*....|....*....|....*....|...
gi 984928820 336 sSMAKMhngyrARENAAL-----AREVCGGNGI 363
Cdd:PLN02876 756 -AMAKV-----AAPNMALkvldmAMQVHGAAGV 782
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
47-396 |
2.27e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 49.84 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 47 YPVLDEHWDKATFPLEEMQKIIDIDLIQNPKLLE--------------------GREDGTIS---QLFRGFRAYTLAKTD 103
Cdd:PTZ00460 1 TQMLEEARKQVQFPVLEMTHLLYGNKEQFETFLErqkfidnepmfkvhpdyynwSRQDQILLnaeKTREAHKHLNLANPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 104 ---PVI----GTFYTS-NGGLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAG-GMAATAKREGDTWIL 174
Cdd:PTZ00460 81 yytPNLlcpqGTFISTvHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNlETTATYDKQTNEFVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 175 N-----GHKKWIGG-GTLAKWHAFFARDVDDGQ---VKMFFVE-------RESEGVETFNTEPKAFFRMMPNAEIIYTDV 238
Cdd:PTZ00460 161 HtpsveAVKFWPGElGFLCNFALVYAKLIVNGKnkgVHPFMVRirdkethKPLQGVEVGDIGPKMGYAVKDNGFLSFDHY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 239 KVP-ESQRAQNVNSWKD--------------AANILRNTRSDVAWLLAGAtagAFEAALKYTREREAFGK------TVAS 297
Cdd:PTZ00460 241 RIPlDSLLARYIKVSEDgqverqgnpkvsyaSMMYMRNLIIDQYPRFAAQ---ALTVAIRYSIYRQQFTNdnkqenSVLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 298 FQLIQEKLSRMAMNAQATLAIAVRLAQQQERG---IYKEENSSMAKMH---------NGYRARENAALAREVCGGNGILL 365
Cdd:PTZ00460 318 YQTQQQKLLPLLAEFYACIFGGLKIKELVDDNfnrVQKNDFSLLQLTHailsaakanYTYFVSNCAEWCRLSCGGHGYAH 397
|
410 420 430
....*....|....*....|....*....|.
gi 984928820 366 EYDVPRFMADIEGMYTYEGTHEVNSLIIGRY 396
Cdd:PTZ00460 398 YSGLPAIYFDMSPNITLEGENQIMYLQLARY 428
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
146-400 |
1.42e-05 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 47.05 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 146 LAMTEPEHGSDIAGGMAATAKREGDTWILNGHKkWIGGGTLAKWHAFFARDvdDGQVKMFFVER-----ESEGVETFNTE 220
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHK-WFFSVPQSDAHLVLAQA--KGGLSCFFVPRflpdgQRNAIRLERLK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 221 PKAFFRMMPNAEIIYtdvkvpesqraQNVNSW------KDAANILRN---TRSDVAWLLAGATAGAFEAALKYTREREAF 291
Cdd:PRK11561 259 DKLGNRSNASSEVEF-----------QDAIGWllgeegEGIRLILKMggmTRFDCALGSHGLMRRAFSVAIYHAHQRQVF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 292 GKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQE-RGIYKEENSS-----MAKMHNGYRARENAALAREVCGGNGILL 365
Cdd:PRK11561 328 GKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDrRADAKEALWArlftpAAKFVICKRGIPFVAEAMEVLGGIGYCE 407
|
250 260 270
....*....|....*....|....*....|....*
gi 984928820 366 EYDVPRFMADIEGMYTYEGTHEVNSLIIGRYYTGQ 400
Cdd:PRK11561 408 ESELPRLYREMPVNSIWEGSGNIMCLDVLRVLNKQ 442
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
81-325 |
1.53e-05 |
|
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: 46.55 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 81 GREDGTISQLFRGFRayTLAKTDPVIGTFYTSNGGlFHECVKIGGSKEQQEKLMPGVLS--WEGKGVlamtePEHGSDIA 158
Cdd:cd01163 46 GGLGASLPDLYEVVR--ELAAADSNIAQALRAHFG-FVEALLLAGPEQFRKRWFGRVLNgwIFGNAV-----SERGSVRP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 159 GGMAATAKREGDTWILNGHKKWIGGGTLAKWHAFFARDvDDGQVKMFFVERESEGVeTFNTEPKAF-FRMMPNAEIIYTD 237
Cdd:cd01163 118 GTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALD-EEGKLVFAAVPTDRPGI-TVVDDWDGFgQRLTASGTVTFDN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 238 VKVPESQRAQNVNSWkDAANILRNTRSDV-AWLLAGATAGAFEAALKYTRER-----EAFGKTVASFQLIQEKLSRMAMN 311
Cdd:cd01163 196 VRVEPDEVLPRPNAP-DRGTLLTAIYQLVlAAVLAGIARAALDDAVAYVRSRtrpwiHSGAESARDDPYVQQVVGDLAAR 274
|
250
....*....|....
gi 984928820 312 AQATLAIAVRLAQQ 325
Cdd:cd01163 275 LHAAEALVLQAARA 288
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
115-396 |
1.57e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 44.06 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 115 GLFHECVKIGGSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAG-GMAATAKREGDTWILN-----GHKKWIGGGTLAK 188
Cdd:PLN02443 104 GMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGlETTATFDPKTDEFVIHsptltSSKWWPGGLGKVS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 189 WHAF-FARDVDDGQ---VKMFFVERES-------EGVETFNTEPK---AFFRMMPNAEIIYTDVKVPESQRAQNVnswkd 254
Cdd:PLN02443 184 THAVvYARLITNGKdhgIHGFIVQLRSlddhsplPGVTVGDIGMKfgnGAYNTMDNGFLRFDHVRIPRDQMLMRL----- 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 255 aANILRN---TRSDVAWLLAGAT----------------AGAFEAALKYTREREAFGKTVA--SFQLIQEKLSRMAMNAQ 313
Cdd:PLN02443 259 -SKVTREgkyVQSDVPRQLVYGTmvyvrqtivadastalSRAVCIATRYSAVRRQFGSQDGgpETQVIDYKTQQSRLFPL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 314 ATLAIAVRLAQQQERGIYKE--------ENSSMAKMH---NGYRARENAALA------REVCGGNGILLEYDVPRFMADI 376
Cdd:PLN02443 338 LASAYAFRFVGEWLKWLYTDvtqrleanDFSTLPEAHactAGLKSLTTSATAdgieecRKLCGGHGYLCSSGLPELFAVY 417
|
330 340
....*....|....*....|
gi 984928820 377 EGMYTYEGTHEVNSLIIGRY 396
Cdd:PLN02443 418 VPACTYEGDNVVLLLQVARF 437
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
269-365 |
1.84e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 43.65 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 269 LLAGATAGAFEAAL---KYTREREAFGKTVASFQLIQEKLSRMAMNAQATLAIAVRLAQQQERGIYKEENSSMAKMHNGY 345
Cdd:PRK09463 337 LPSNSTGGAKLAALatgAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKPSVLSAIAKYHLTE 416
|
90 100
....*....|....*....|
gi 984928820 346 RARENAALAREVCGGNGILL 365
Cdd:PRK09463 417 RGRQVINDAMDIHGGKGICL 436
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
125-362 |
2.56e-04 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 43.31 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIAG-GMAATAKREGDTWILN-----GHKKWIGGGTL-AKWHAFFAR-- 195
Cdd:PLN02636 156 GTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGlQTTATFDPLTDEFVINtpndgAIKWWIGNAAVhGKFATVFARlk 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 196 -------DVDDGQVKMFFVE-RESE------GVETFNTEPKAFFRMMPNAEIIYTDVKVPesqRAQNVNSWKD------- 254
Cdd:PLN02636 236 lpthdskGVSDMGVHAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNGALRFRSVRIP---RDNLLNRFGDvsrdgky 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984928820 255 -----------AANI--LRNTRSDVAWLLAGATAGAFEAALKYTREREAFGK------TVASFQLIQEKLsrMAMNAQat 315
Cdd:PLN02636 313 tsslptinkrfAATLgeLVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQSQQHKL--MPMLAS-- 388
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 984928820 316 lAIAVRLAQQQERGIYKEenssMAKMHN------------GYRARENAALA------REVCGGNG 362
Cdd:PLN02636 389 -TYAFHFATEYLVERYSE----MKKTHDdqlvadvhalsaGLKAYITSYTAkalstcREACGGHG 448
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
125-184 |
5.07e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 42.16 E-value: 5.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 984928820 125 GSKEQQEKLMPGVLSWEGKGVLAMTEPEHGSDIaGGMAATAKREGD-TWILNGHKKWIGGG 184
Cdd:PTZ00456 164 GSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDL-GQVKTKAEPSADgSYKITGTKIFISAG 223
|
|
| |
