|
Name |
Accession |
Description |
Interval |
E-value |
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
9-384 |
0e+00 |
|
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: 751.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 9 ALGETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASV 88
Cdd:cd01156 1 GLDDEIEMLRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 89 ALSYGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDA 168
Cdd:cd01156 81 ALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 169 NTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDYER 248
Cdd:cd01156 161 DTLVVYAKTDPSAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 249 VVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYS 328
Cdd:cd01156 241 LVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 495256245 329 AERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFN 384
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIGRELFK 376
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
5-385 |
0e+00 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 609.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 5 SLNFALGETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPAD--LWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEIS 82
Cdd:PLN02519 21 SSSLLFDDTQLQFKESVQQFAQENIAPHAAAIDATNSFPKDvnLWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 83 RGSASVALSYGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWI 162
Cdd:PLN02519 101 RASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 163 TNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMS 242
Cdd:PLN02519 181 TNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 243 GLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAA 322
Cdd:PLN02519 261 GLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRKDCA 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495256245 323 GVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNE 385
Cdd:PLN02519 341 GVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLIGRELFKE 403
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
7-387 |
4.57e-172 |
|
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: 484.73 E-value: 4.57e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 7 NFALGETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSA 86
Cdd:COG1960 2 DFELTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 87 SVALSYGAHsNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGP 166
Cdd:COG1960 82 SLALPVGVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 167 DANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDY 246
Cdd:COG1960 161 VADVILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 247 ERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVIL 326
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALEAAMAKL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495256245 327 YSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR 387
Cdd:COG1960 321 FATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
12-383 |
6.29e-158 |
|
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: 448.64 E-value: 6.29e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 12 ETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALS 91
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 92 YGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTY 171
Cdd:cd01158 81 VSVHNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 172 VIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDYERVVL 251
Cdd:cd01158 161 IVFAVTDPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 252 SGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAER 331
Cdd:cd01158 241 AAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFASEV 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 495256245 332 ATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELF 383
Cdd:cd01158 321 AMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLL 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
12-380 |
8.08e-118 |
|
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: 345.04 E-value: 8.08e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 12 ETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGllgitvpeeyggaglgylahvvameeisrgsasvals 91
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELLAELGLLL------------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 92 ygahsnlCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTY 171
Cdd:cd00567 44 -------GAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLF 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 172 VIYAKTDLE-KGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDYERVV 250
Cdd:cd00567 117 IVLARTDEEgPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 251 LSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGET-TRKDAAGVILYSA 329
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDeARLEAAMAKLFAT 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 495256245 330 ERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGR 380
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
15-382 |
6.38e-115 |
|
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: 339.48 E-value: 6.38e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 15 DMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASvALSYGA 94
Cdd:cd01160 4 DAFRDVVRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGS-GPGLSL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 95 HSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIY 174
Cdd:cd01160 83 HTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 175 AKTDLEKGP-HGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDYERVVLSG 253
Cdd:cd01160 163 ARTGGEARGaGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 254 GPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERAT 333
Cdd:cd01160 243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQN 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 495256245 334 QMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGREL 382
Cdd:cd01160 323 RVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQM 371
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
16-387 |
5.37e-113 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 336.14 E-value: 5.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 16 MLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAH 95
Cdd:PTZ00461 43 ALRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLAH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 96 SNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGD-HYVLNGSKTWITNGPDANTYVIY 174
Cdd:PTZ00461 123 SMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNgNYVLNGSKIWITNGTVADVFLIY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 175 AKTDLEkgphgITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDYERVVLSGG 254
Cdd:PTZ00461 203 AKVDGK-----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 255 PTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQ 334
Cdd:PTZ00461 278 AVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAKK 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 495256245 335 MALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR 387
Cdd:PTZ00461 358 VADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITKDLLKGLK 410
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
3-378 |
1.53e-104 |
|
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: 314.41 E-value: 1.53e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 3 YPS-LNFALGETIDMLRDQVQSFVAKEIAPraAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEI 81
Cdd:cd01161 19 YPSvLTEEQTEELNMLVGPVEKFFEEVNDP--AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 82 SRgSASVALSYGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKR--GDHYVLNGSK 159
Cdd:cd01161 97 GM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLSedGKHYVLNGSK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 160 TWITNGPDANTYVIYAKTDLEKGP----HGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNG 235
Cdd:cd01161 176 IWITNGGIADIFTVFAKTEVKDATgsvkDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 236 GVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGE 315
Cdd:cd01161 256 GFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGL 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495256245 316 TTR--KDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLI 378
Cdd:cd01161 336 KAEyqIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
10-385 |
1.65e-97 |
|
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: 295.12 E-value: 1.65e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 10 LGETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVA 89
Cdd:cd01162 1 LNEEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 90 lSYGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDAN 169
Cdd:cd01162 81 -AYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 170 TYVIYAKTDlEKGPHGITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDYERV 249
Cdd:cd01162 160 VYVVMARTG-GEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 250 VLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGettRKDA----AGVI 325
Cdd:cd01162 239 NIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRG---DPDAvklcAMAK 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 326 LYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNE 385
Cdd:cd01162 316 RFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
16-381 |
1.24e-89 |
|
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: 275.39 E-value: 1.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 16 MLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITvPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAH 95
Cdd:cd01151 19 AIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIAREVERVDSGYRSFMSVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 96 SNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYA 175
Cdd:cd01151 98 SSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 176 KTDLEKGPHGitaFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNgGVKVLMSGLDYERVVLSGGP 255
Cdd:cd01151 178 RNDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGAE-GLRGPFKCLNNARYGIAWGA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 256 TGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERATQM 335
Cdd:cd01151 254 LGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQISLLKRNNCGKALEI 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 495256245 336 ALDAIQILGGNGYINEFPAGRLLRDAK---LYEigaGTSEIRRMLIGRE 381
Cdd:cd01151 334 ARTAREMLGGNGISDEYHIIRHMVNLEsvnTYE---GTHDIHALILGRA 379
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
10-383 |
7.52e-88 |
|
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: 270.61 E-value: 7.52e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 10 LGETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVA 89
Cdd:cd01157 1 LTEQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 90 LSYGAHSnLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDAN 169
Cdd:cd01157 81 TAIEANS-LGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 170 TYVIYAKTDLE-KGPHG--ITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDY 246
Cdd:cd01157 160 WYFLLARSDPDpKCPASkaFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 247 ERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVIL 326
Cdd:cd01157 240 TRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 495256245 327 YSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELF 383
Cdd:cd01157 320 FAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
6-382 |
5.84e-71 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 226.92 E-value: 5.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 6 LNFALGETIDMLRDQVQSFVAKEIaPRA--AQIDIDNLFPADLWRKFGD--MGLLGItvPEEYGGAGLGYLAHVVAMEEI 81
Cdd:PRK12341 1 MDFSLTEEQELLLASIRELITRNF-PEEyfRTCDENGTYPREFMRALADngISMLGV--PEEFGGTPADYVTQMLVLEEV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 82 SRGSASVALSYGAhsnLCVNQINRNGNHEQKSK-YLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKT 160
Cdd:PRK12341 78 SKCGAPAFLITNG---QCIHSMRRFGSAEQLRKtAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 161 WITNGPDANTYVIYAKTDLEKGPH-GITAFIVERDWKGFSRsNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKV 239
Cdd:PRK12341 155 FITGAKEYPYMLVLARDPQPKDPKkAFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 240 LMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRK 319
Cdd:PRK12341 234 VMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRT 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495256245 320 DAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGREL 382
Cdd:PRK12341 314 SAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYIAGRQI 376
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
17-383 |
1.72e-56 |
|
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: 189.48 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 17 LRDQVQSFVAKEIAP----RAAQIDIDNLFPADLW-RKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALS 91
Cdd:cd01152 6 FRAEVRAWLAAHLPPelreESALGYREGREDRRRWqRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 92 yGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTY 171
Cdd:cd01152 86 -QIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 172 VIYAKTDLEKGPH-GITAFIVERDWKGFSRsnKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGLDYERVV 250
Cdd:cd01152 165 WLLVRTDPEAPKHrGISILLVDMDSPGVTV--RPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 251 LSGGPTgimQACMDLIVpYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAE 330
Cdd:cd01152 243 IGGSAA---TFFELLLA-RLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSE 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495256245 331 RATQMALDAIQILGGNGYINEFPAG--------RLLRDAKLYEIGAGTSEIRRMLIGRELF 383
Cdd:cd01152 319 LAQELAELALELLGTAALLRDPAPGaelagrweADYLRSRATTIYGGTSEIQRNIIAERLL 379
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
6-387 |
5.13e-55 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 185.81 E-value: 5.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 6 LNFALGETIDMLRDQVQSFVAKE-IAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRG 84
Cdd:PRK03354 1 MDFNLNDEQELFVAGIRELMASEnWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 85 SASVALSYGAHSNLcvNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITN 164
Cdd:PRK03354 81 GAPTYVLYQLPGGF--NTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 165 GPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRsNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNGGVKVLMSGL 244
Cdd:PRK03354 159 SAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 245 DYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGV 324
Cdd:PRK03354 238 DHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMC 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495256245 325 ILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGRELFNETR 387
Cdd:PRK03354 318 KYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR 380
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
12-123 |
5.27e-55 |
|
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: 176.88 E-value: 5.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 12 ETIDMLRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALS 91
Cdd:pfam02771 2 EEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALA 81
|
90 100 110
....*....|....*....|....*....|..
gi 495256245 92 YGAHSNLCVNQINRNGNHEQKSKYLPKLISGE 123
Cdd:pfam02771 82 LSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
17-382 |
6.17e-50 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 173.11 E-value: 6.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 17 LRDQVQSFVAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVpEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHS 96
Cdd:PLN02526 36 LRKRVRECMEKEVAPIMTEYWEKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAIATAEVARVDASCSTFILVHS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 97 NLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAK 176
Cdd:PLN02526 115 SLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFAR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 177 -TDLEKgphgITAFIVERDWKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILGVLNG---GVKVLMsgldYERVVLS 252
Cdd:PLN02526 195 nTTTNQ----INGFIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGVNSfqdTNKVLA----VSRVMVA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 253 GGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSAERA 332
Cdd:PLN02526 267 WQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPGHASLGKAWITKKA 346
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 495256245 333 TQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGREL 382
Cdd:PLN02526 347 RETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINALVTGREI 396
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
44-382 |
3.37e-48 |
|
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: 168.34 E-value: 3.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 44 ADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSnlCVNQINRNGNHEQKSKYLPKLISGE 123
Cdd:cd01153 39 KEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 124 HIGALAMSEPNAGSDVVSMKLRADKRGD-HYVLNGSKTWITNG----PDANTYVIYAKT-DLEKGPHGITAFIVERDWKG 197
Cdd:cd01153 117 WTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGehdmSENIVHLVLARSeGAPPGVKGLSLFLVPKFLDD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 198 FSRSNKF-----DKLGMRGSNTCELFFDDVQVPeenILGVLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHD 272
Cdd:cd01153 197 GERNGVTvarieEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 273 RKQFGQSIGEF-QLIQGKVADMYTQLNASRAYL---------YAVAQACERGETTRKDAAG------------VILYSAE 330
Cdd:cd01153 274 RKQGGDLIKAApAVTIIHHPDVRRSLMTQKAYAegsraldlyTATVQDLAERKATEGEDRKalsaladlltpvVKGFGSE 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 495256245 331 RATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRM-LIGREL 382
Cdd:cd01153 354 AALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGIQALdLIGRKI 406
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
234-382 |
6.60e-46 |
|
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: 154.33 E-value: 6.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 234 NGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACER 313
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495256245 314 GETTRKDAAGVILYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLIGREL 382
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIARRL 149
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
127-220 |
3.15e-33 |
|
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: 119.31 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 127 ALAMSEPNAGSDVVSMKLRA-DKRGDHYVLNGSKTWITNGPDANTYVIYAKTDLEKGPHGITAFIVERDWKGFSRSNKFD 205
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIET 80
|
90
....*....|....*
gi 495256245 206 KLGMRGSNTCELFFD 220
Cdd:pfam02770 81 KLGVRGLPTGELVFD 95
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
114-373 |
4.00e-30 |
|
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: 119.78 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 114 KYLPKLISGEH----IGALAMSEPNAGSDVVSMKLRADK-RGDHYVLNGSKtWITNGPDANTYVIYAKT-DLEKGPHGIT 187
Cdd:cd01154 133 QYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERsGGGVYRLNGHK-WFASAPLADAALVLARPeGAPAGARGLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 188 AFIVERDWKGFSRsNKF------DKLGMRGSNTCELFFDDVqvpEENILGVLNGGVKVLMSGLDYERVVLSGGPTGIMQA 261
Cdd:cd01154 212 LFLVPRLLEDGTR-NGYrirrlkDKLGTRSVATGEVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRR 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 262 CMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVI--------LYSAERAT 333
Cdd:cd01154 288 ALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAHMArlatpvakLIACKRAA 367
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 495256245 334 QMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEI 373
Cdd:cd01154 368 PVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNI 407
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
17-380 |
8.60e-23 |
|
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: 98.62 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 17 LRDQVQSFVAKEIAP--------RAAQIDIDNLFPA---DLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGS 85
Cdd:cd01155 6 LRARVKAFMEEHVYPaeqefleyYAEGGDRWWTPPPiieKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEETGRSF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 86 -ASVALSYGA--HSNLCVnqINRNGNHEQKSKYLPKLISGEHIGALAMSEPN-AGSDVVSMKLRADKRGDHYVLNGSKTW 161
Cdd:cd01155 86 fAPEVFNCQApdTGNMEV--LHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDDYVINGRKWW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 162 ITNG--PDANTYVIYAKTDLEKGP-HGITAFI-VERDWKGFSrsnKFDKLGMRGSNT-----CELFFDDVQVPEENILGV 232
Cdd:cd01155 164 SSGAgdPRCKIAIVMGRTDPDGAPrHRQQSMIlVPMDTPGVT---IIRPLSVFGYDDaphghAEITFDNVRVPASNLILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 233 LNGGVKVLMSGLdyervvlsgGPtGIMQACM----------DLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRa 302
Cdd:cd01155 241 EGRGFEIAQGRL---------GP-GRIHHCMrligaaeralELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQAR- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 303 yLYAVAQACERGETTRKDAAGVILYSAERATQMALD----AIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRMLI 378
Cdd:cd01155 310 -LLVLKAAHMIDTVGNKAARKEIAMIKVAAPRMALKiidrAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSI 388
|
..
gi 495256245 379 GR 380
Cdd:cd01155 389 AR 390
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
25-339 |
8.51e-22 |
|
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: 95.47 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 25 VAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGY--LAHVVAmeEISRGSASVALSYGAHSNLcVNQ 102
Cdd:cd01163 6 LAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLpdLYEVVR--ELAAADSNIAQALRAHFGF-VEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 103 INRNGNHEQKSKYLPKLISGEHIGAlAMSE---PNAGSDVVsmklRADKRGDHYVLNGSKTWITNGPDANTYVIYAKtdL 179
Cdd:cd01163 83 LLLAGPEQFRKRWFGRVLNGWIFGN-AVSErgsVRPGTFLT----ATVRDGGGYVLNGKKFYSTGALFSDWVTVSAL--D 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 180 EKGPHgiTAFIVERDWKGFSRSNKFDKLGMR--GSNTCElfFDDVQVPEENILGVLNGGVKVLMSGLdYERVVLSGGPTG 257
Cdd:cd01163 156 EEGKL--VFAAVPTDRPGITVVDDWDGFGQRltASGTVT--FDNVRVEPDEVLPRPNAPDRGTLLTA-IYQLVLAAVLAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 258 IMQACMDLIV--------PYIH-------DRKQFGQSIGEFQlIQGKVADMYTqLNASRAYLYAVAQACERGETTRKDAA 322
Cdd:cd01163 231 IARAALDDAVayvrsrtrPWIHsgaesarDDPYVQQVVGDLA-ARLHAAEALV-LQAARALDAAAAAGTALTAEARGEAA 308
|
330
....*....|....*..
gi 495256245 323 GVILYSAERATQMALDA 339
Cdd:cd01163 309 LAVAAAKVVVTRLALDA 325
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
54-382 |
3.07e-21 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 95.71 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 54 GLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVA----LSYGAhsnlcVNQINRNGNHEQKSKYLPKLISGEHIGALA 129
Cdd:PTZ00456 112 GWTGISEPEEYGGQALPLSVGFITRELMATANWGFSmypgLSIGA-----ANTLMAWGSEEQKEQYLTKLVSGEWSGTMC 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 130 MSEPNAGSDVVSMKLRADKRGD-HYVLNGSKTWITNGPDANT----YVIYAKT-DLEKGPHGITAFIVER---DWKGFSR 200
Cdd:PTZ00456 187 LTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAGDHDLTenivHIVLARLpNSLPTTKGLSLFLVPRhvvKPDGSLE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 201 SNKF-------DKLGMRGSNTCELFFDDvqvPEENILGVLNGGVKVLMS-----------------------GLDYER-- 248
Cdd:PTZ00456 267 TAKNvkcigleKKMGIKGSSTCQLSFEN---SVGYLIGEPNAGMKQMFTfmntarvgtalegvchaelafqnALRYARer 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 249 ---VVLSGGPTGIMQAcmDLIVPYIHDRKQ--FGQSIGE----FQLIQGKVADMYtqLNASRAYLYAvAQACERGETTRK 319
Cdd:PTZ00456 344 rsmRALSGTKEPEKPA--DRIICHANVRQNilFAKAVAEggraLLLDVGRLLDIH--AAAKDAATRE-ALDHEIGFYTPI 418
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495256245 320 DAAGVILYSAERATQMaldaIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEIRRM-LIGREL 382
Cdd:PTZ00456 419 AKGCLTEWGVEAASRC----LQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALdFIGRKV 478
|
|
| sulfur_SfnB |
TIGR04022 |
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the ... |
25-339 |
4.43e-21 |
|
sulfur acquisition oxidoreductase, SfnB family; Members of this protein family belong to the greater family of acyl-CoA dehydrogenases. This family includes the sulfate starvation induced protein SfnB of Pseudomonas putida strain DS1, which is both encoded nearby to and phylogenetically closely correlated with the dimethyl sulphone monooxygenase SfnG. This family shows considerable sequence similarity to the Rhodococcus dibenzothiophene desulfurization enzyme DszC, although that enzyme falls outside of the scope of this family. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 274924 [Multi-domain] Cd Length: 391 Bit Score: 93.87 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 25 VAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGY--LAHVVAMeeISRGSASVALSYGAHSNLcVNQ 102
Cdd:TIGR04022 17 LAAEFAPGAAERDRERRLPWAELDAFSQSGLWGITVPRAYGGAGVSYatLAEVIAI--ISAADPSLGQIPQNHFYA-LEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 103 INRNGNHEQKSKYLPKLISGEHIGalamsepNAGSDV-------VSMKLRADkrGDHYVLNGSKT---------WITN-- 164
Cdd:TIGR04022 94 LRLTGSEEQKRFFFGEVLAGERFG-------NAFSERgtrnvldFQTRLRRD--GDGYRLNGRKFystgalfahWIPVla 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 165 -GPDANTYVIYAKTDLEkgphGITafiVERDWKGFsrsnkfdklGMR--GSNTCELffDDVQVPEENILGVLNGgvkvlm 241
Cdd:TIGR04022 165 lDDEGRAVLAFVPRDAP----GLT---VIDDWSGF---------GQRttASGTVLL--DDVRVPAEHVVPIQRA------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 242 sgldYERVVLSGGPTGIMQACMDL---------IVPYIHDR-------KQfgQSIGEFQLIQGKVADMYTQLNASRAYLY 305
Cdd:TIGR04022 221 ----FDRPTAAGPVAQIIHAAIDAgiaraaladTLAFVRERarpwidsGV--ERASDDPLTIAEVGDLAIRLHAAEALLE 294
|
330 340 350
....*....|....*....|....*....|....*....
gi 495256245 306 AVAQACE--RGETTRKDAAGVILYSAER---ATQMALDA 339
Cdd:TIGR04022 295 RAGRAVDaaRAEPTEESVAAASIAVAEAkvlTTEIALLA 333
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
17-301 |
6.21e-17 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 82.70 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 17 LRDQVQSFVAKEIAPRAAQIDIDNLF------PADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVAL 90
Cdd:PRK13026 78 LTAEEQAFIDNEVETLLTMLDDWDIVqnrkdlPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 91 SYGAHSNLCVNQ-INRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKlraDK----RGDH-------YVLNGS 158
Cdd:PRK13026 158 TVMVPNSLGPGElLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIP---DTgivcRGEFegeevlgLRLTWD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 159 KTWITNGPDAnTYVIYA------------KTDLekgphGITAFIVERDWKGFSRSNKFDKLGMR---GSNTCElffdDVQ 223
Cdd:PRK13026 235 KRYITLAPVA-TVLGLAfklrdpdgllgdKKEL-----GITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGK----DVF 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 224 VPEENILGvlnG------GVKVLMSGLDYER-VVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADM--Y 294
Cdd:PRK13026 305 IPLDWIIG---GpdyagrGWRMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIagN 381
|
....*...
gi 495256245 295 T-QLNASR 301
Cdd:PRK13026 382 TyLLEAAR 389
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
43-347 |
1.33e-16 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 81.40 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 43 PADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISrgSASVAL--------SYGAHSNLCvnqinRNGNHEQKSK 114
Cdd:PRK09463 111 PPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLA--SRSGTLavtvmvpnSLGPGELLL-----HYGTDEQKDH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 115 YLPKLISGEHIGALAMSEPNAGSDVVSMK-----LRADKRGDHYV---LNGSKTWITNGPDAnTYVIYA----------- 175
Cdd:PRK09463 184 YLPRLARGEEIPCFALTSPEAGSDAGSIPdtgvvCKGEWQGEEVLgmrLTWNKRYITLAPIA-TVLGLAfklydpdgllg 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 176 -KTDLekgphGITAFIVERDWKGFSRSNKFDKLG---MRGSNTCElffdDVQVPEENILGvlnG------GVKVLMSGLD 245
Cdd:PRK09463 263 dKEDL-----GITCALIPTDTPGVEIGRRHFPLNvpfQNGPTRGK----DVFIPLDYIIG---GpkmagqGWRMLMECLS 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 246 YER-VVLSGGPTGIMQACMDLIVPYIHDRKQFGQSIGEFQLIQGKVADMytqlnASRAYL-----YAVAQACERGETTRK 319
Cdd:PRK09463 331 VGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARI-----AGNAYLmdaarTLTTAAVDLGEKPSV 405
|
330 340
....*....|....*....|....*...
gi 495256245 320 DAAGVILYSAERATQMALDAIQILGGNG 347
Cdd:PRK09463 406 LSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
25-361 |
4.25e-16 |
|
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: 78.93 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 25 VAKEIAPRAAQIDIDNLFPADLWRKFGDMGLLGITVPEEYGGAGLGYLAHVVAMEEISRGSAS---VALSYGAHSNLCVn 101
Cdd:cd01159 6 LAPLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSaawVASIVATHSRMLA- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 102 qinrngnheqkskYLPKL----ISGEHIGALAmsepnagSDVVSMKLRADKRGDHYVLNGSKTWITNGPDANTYVIYAKT 177
Cdd:cd01159 85 -------------AFPPEaqeeVWGDGPDTLL-------AGSYAPGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 178 DLEKGPHGITAFIVERdwKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENIL--GVLNGGVKVLMSGLDYERVVLSGGP 255
Cdd:cd01159 145 EDDDGGPLPRAFVVPR--AEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtaGDMMAGDGPGGSTPVYRMPLRQVFP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 256 T-------GIMQACMDLIVPYIHDRKQ---FGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGV- 324
Cdd:cd01159 223 LsfaavslGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGGPIDVEe 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 495256245 325 ---ILYSAERATQMALDAIQIL----GGNGYINEFPAGRLLRDA 361
Cdd:cd01159 303 rarIRRDAAYAAKLSAEAVDRLfhaaGGSALYTASPLQRIWRDI 346
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
53-356 |
1.38e-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: 75.06 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 53 MGLLGITVPEEYggaglgylahVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSE 132
Cdd:cd01150 73 MGELMADDPEKM----------LALTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 133 PNAGSDVVSMKLRA--DKRGDHYVLN-----GSKTWITN-GPDANTYVIYAKTDLEKGPHGITAFIVE-RDWKGFSRSNK 203
Cdd:cd01150 143 LGHGSNLQGLETTAtyDPLTQEFVINtpdftATKWWPGNlGKTATHAVVFAQLITPGKNHGLHAFIVPiRDPKTHQPLPG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 204 FD------KLGMRGSNTCELFFDDVQVPEENIlgvLNGGVKVLMSGLdYERV-------------VLSGGPTGIMQA--- 261
Cdd:cd01150 223 VTvgdigpKMGLNGVDNGFLQFRNVRIPRENL---LNRFGDVSPDGT-YVSPfkdpnkrygamlgTRSGGRVGLIYDaam 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 262 ----CMDLIVPYIHDRKQFGQ-------SIGEFQLIQGKVadmYTQLnaSRAYLYAVAQACERG---ETTRKDAAGVILY 327
Cdd:cd01150 299 slkkAATIAIRYSAVRRQFGPkpsdpevQILDYQLQQYRL---FPQL--AAAYAFHFAAKSLVEmyhEIIKELLQGNSEL 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 495256245 328 SAE----------RATQMALDAIQIL----GGNGYI--NEFPAGR 356
Cdd:cd01150 374 LAElhalsaglkaVATWTAAQGIQECreacGGHGYLamNRLPTLR 418
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
105-373 |
3.51e-14 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 74.06 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 105 RNGNHEQKSKYLPKLISGEHIGALAMSEPN-AGSDVVSMKLRADKRGDHYVLNGSKTWiTNG---PDANTYVIYAKTDLE 180
Cdd:PLN02876 531 RYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSYVINGTKWW-TSGamdPRCRVLIVMGKTDFN 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 181 KGPHGITAFI-VERDWKGFSRSNKFDKLGMRGS--NTCELFFDDVQVPEENILgvlnggvkvLMSGLDYERVVLSGGPtG 257
Cdd:PLN02876 610 APKHKQQSMIlVDIQTPGVQIKRPLLVFGFDDAphGHAEISFENVRVPAKNIL---------LGEGRGFEIAQGRLGP-G 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 258 IMQAC----------MDLIVPYIHDRKQFGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERgeTTRKDAAGVILY 327
Cdd:PLN02876 680 RLHHCmrligaaergMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDR--LGNKKARGIIAM 757
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495256245 328 SAERATQMAL----DAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSEI 373
Cdd:PLN02876 758 AKVAAPNMALkvldMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
55-260 |
1.92e-12 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 68.37 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 55 LLGITVPEEYGGAGLGYLAHVVAMEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPN 134
Cdd:PTZ00457 65 LYGARIATEYGGLGLGHTAHALIYEEVGTNCDSKLLSTIQHSGFCTYLLSTVGSKELKGKYLTAMSDGTIMMGWATEEGC 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 135 aGSDVVSMKLRADKRGD-HYVLNGSKTWItNGPDANTYVIYAKT----DLEKGPHGI---TAFIVERDWKGFSrsnkfdk 206
Cdd:PTZ00457 145 -GSDISMNTTKASLTDDgSYVLTGQKRCE-FAASATHFLVLAKTltqtAAEEGATEVsrnSFFICAKDAKGVS------- 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495256245 207 lgmrgSNTCELFFDDvqVPEENILGVLNGGVKVLMSGLDYERVVLSGGPTGIMQ 260
Cdd:PTZ00457 216 -----VNGDSVVFEN--TPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMK 262
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
125-373 |
1.08e-11 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 66.31 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 125 IGaLAMSEPNAGSDVVSMKLRADK-RGDHYVLNGSKtWITNGPDANTYVIYAKTdleKGphGITAFIVERDWKGFSRsNK 203
Cdd:PRK11561 180 IG-MGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQA---KG--GLSCFFVPRFLPDGQR-NA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 204 F------DKLGMRGSNTCELFFDDVQvpeENILGVLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFG 277
Cdd:PRK11561 252 IrlerlkDKLGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQVFG 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 278 QSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERGETTRKDAAGVILYSA------ERATQMALDAIQILGGNGYINE 351
Cdd:PRK11561 329 KPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWDRRADAKEALWARLFTPAakfvicKRGIPFVAEAMEVLGGIGYCEE 408
|
250 260
....*....|....*....|..
gi 495256245 352 FPAGRLLRDAKLYEIGAGTSEI 373
Cdd:PRK11561 409 SELPRLYREMPVNSIWEGSGNI 430
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
256-372 |
5.79e-10 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 56.97 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 256 TGIMQACMDLIVPYIHDRKQ--FGQSIGEFQLIQGKVADMYTQLNASRAYLYAVAQACERG--------ETTRKDAAGVI 325
Cdd:pfam08028 7 LGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAaaagkpvtPALRAEARRAA 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 495256245 326 LYSAERATQMALDAIQILGGNGYINEFPAGRLLRDAKLYEIGAGTSE 372
Cdd:pfam08028 87 AFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
78-313 |
4.23e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 51.78 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 78 MEEISRGSASVALSYGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--DKRGDHYVL 155
Cdd:PLN02636 127 TEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTAtfDPLTDEFVI 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 156 N-----GSKTWITNGPDANTYV-IYAKTDL----EKGPH--GITAFIVE-RDWK------GFSRSNKFDKLGMRGSNTCE 216
Cdd:PLN02636 207 NtpndgAIKWWIGNAAVHGKFAtVFARLKLpthdSKGVSdmGVHAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNGA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 217 LFFDDVQVPEENILG----------------VLNGGVKVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQFGQ-- 278
Cdd:PLN02636 287 LRFRSVRIPRDNLLNrfgdvsrdgkytsslpTINKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpk 366
|
250 260 270
....*....|....*....|....*....|....*....
gi 495256245 279 ----SIGEFQLIQGKVADMytqLNASRAYLYAVAQACER 313
Cdd:PLN02636 367 qpeiSILDYQSQQHKLMPM---LASTYAFHFATEYLVER 402
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
95-230 |
9.76e-07 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 50.61 E-value: 9.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 95 HSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--DKRGDHYVLN-----GSKTWITNGPD 167
Cdd:PLN02443 102 HWGMFVPAIKGQGTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTAtfDPKTDEFVIHsptltSSKWWPGGLGK 181
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495256245 168 ANTY-VIYAKTDLEKGPHGITAFIVE----RDWK---GFSRSNKFDKLGMRGSNTCE---LFFDDVQVPEENIL 230
Cdd:PLN02443 182 VSTHaVVYARLITNGKDHGIHGFIVQlrslDDHSplpGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQML 255
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
92-290 |
1.80e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 43.68 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 92 YGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--DKRGDHYVLN-----GSKTWITN 164
Cdd:PTZ00460 95 STVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTAtyDKQTNEFVIHtpsveAVKFWPGE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 165 -GPDANTYVIYAKTDLEKGPHGITAFIVE-RD------WKGFSRSNKFDKLGMRGSNTCELFFDDVQVPEENILG----- 231
Cdd:PTZ00460 175 lGFLCNFALVYAKLIVNGKNKGVHPFMVRiRDkethkpLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryikv 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495256245 232 VLNGGV------KVLMSGLDYERVVLSGGPTGIMQACMDLIVPYIHDRKQF----GQ--SIGEFQLIQGKV 290
Cdd:PTZ00460 255 SEDGQVerqgnpKVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFtndnKQenSVLEYQTQQQKL 325
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
87-230 |
1.33e-03 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 40.91 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495256245 87 SVALSYGAHSNLCVNQINRNGNHEQKSKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--DKRGDHYVLN-----GSK 159
Cdd:PLN02312 148 SLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTtyDPKTEEFVINtpcesAQK 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495256245 160 TWITNGPDANTYVI-YAKTDLEKGPHGITAFIVE-RDWKGFSRSNKF-----DKLGMRGSNTCELFFDDVQVPEENIL 230
Cdd:PLN02312 228 YWIGGAANHATHTIvFSQLHINGKNEGVHAFIAQiRDQDGNICPNIRiadcgHKIGLNGVDNGRIWFDNLRIPRENLL 305
|
|
| |
