|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
1-378 |
3.74e-145 |
|
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: 416.55 E-value: 3.74e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 1 MDLLddsiVPEHARDIKAEAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEF 80
Cdd:COG1960 1 MDFE----LTEEQRALRDEVREFAEEEIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 81 YRADAGIALTLQLASFGCELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWI 160
Cdd:COG1960 77 ARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 161 GNGVEADWITLYARTgdDESNPYANYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWML 240
Cdd:COG1960 157 TNAPVADVILVLART--DPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 241 ADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYW 320
Cdd:COG1960 235 MSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGEDAALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 496171797 321 AALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:COG1960 315 AAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLII 372
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
11-378 |
3.06e-115 |
|
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: 338.49 E-value: 3.06e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 11 EHARDIKAEAREFAREHIEPNAQEYYQAGEYPEEILeagqeanlvaqdipeewggrgldlpqllalteefyrADAGIALT 90
Cdd:cd00567 1 EEQRELRDSAREFAAEELEPYARERRETPEEPWELL------------------------------------AELGLLLG 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 91 LqlasfgcELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIGNGVEADWIT 170
Cdd:cd00567 45 A-------ALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 171 LYARTgDDESNPYANYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRIA 250
Cdd:cd00567 118 VLART-DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 251 VSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENE-GYWAALSKTNAT 329
Cdd:cd00567 197 LAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEaRLEAAMAKLFAT 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496171797 330 ETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
11-378 |
5.21e-113 |
|
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: 334.62 E-value: 5.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 11 EHARDIKAEAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIALT 90
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 91 LQLA-SFGCELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIGNGVEADWI 169
Cdd:cd01158 81 VSVHnSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 170 TLYARTgdDESNPYANYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRI 249
Cdd:cd01158 161 IVFAVT--DPSKGYRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 250 AVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYWAALSKTNAT 329
Cdd:cd01158 239 GIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLFAS 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496171797 330 ETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:cd01158 319 EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVI 367
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
10-378 |
2.37e-84 |
|
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: 261.28 E-value: 2.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 10 PEHA--RDIkaeAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADA-G 86
Cdd:cd01160 1 EEHDafRDV---VRRFFAKEVAPFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGsG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 87 IALTLQLASFGCELTYeYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIGNGVEA 166
Cdd:cd01160 78 PGLSLHTDIVSPYITR-AGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 167 DWITLYARTGDdESNPYANYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNH 246
Cdd:cd01160 157 DVVIVVARTGG-EARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 247 GRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYWAALSKT 326
Cdd:cd01160 236 ERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKY 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 496171797 327 NATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:cd01160 316 WATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELI 367
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
16-378 |
6.74e-82 |
|
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: 255.03 E-value: 6.74e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 16 IKAEAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLD-LPQLLALtEEFYRADAGIALTLQLA 94
Cdd:cd01156 9 LRQSVREFAQKEIAPLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGyLAHVIIM-EEISRASGSVALSYGAH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 95 SFGC-ELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIGNGVEADWITLYA 173
Cdd:cd01156 88 SNLCiNQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVYA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 174 RTGDDESNpyANYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRIAVSG 253
Cdd:cd01156 168 KTDPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 254 HGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYWAALSKTNATETAT 333
Cdd:cd01156 246 GPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMDPKDAAGVILYAAEKAT 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 496171797 334 SVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:cd01156 326 QVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVI 370
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
11-378 |
2.34e-77 |
|
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: 243.26 E-value: 2.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 11 EHARDIKAEAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIALT 90
Cdd:cd01157 3 EQQKEFQETARKFAREEIIPVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 91 LQLASFGCELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIGNGVEADWIT 170
Cdd:cd01157 83 IEANSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 171 LYARTGDDESNPYAN-YSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRI 249
Cdd:cd01157 163 LLARSDPDPKCPASKaFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 250 AVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYWAALSKTNAT 329
Cdd:cd01157 243 PVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAA 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496171797 330 ETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:cd01157 323 DIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLII 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
11-378 |
4.95e-71 |
|
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: 226.94 E-value: 4.95e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 11 EHARDIKAEAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIALT 90
Cdd:cd01162 3 EEQRAIQEVARAFAAKEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 91 LQLASFGCELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIGNGVEADWIT 170
Cdd:cd01162 83 ISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 171 LYARTGDDESNpyaNYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRIA 250
Cdd:cd01162 163 VMARTGGEGPK---GISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 251 VSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENE-GYWAALSKTNAT 329
Cdd:cd01162 240 IASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPDaVKLCAMAKRFAT 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 496171797 330 ETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:cd01162 320 DECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLII 368
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
3-382 |
4.14e-70 |
|
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: 224.93 E-value: 4.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 3 LLDDSIVPEHaRDIKAEAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQdIPEEWGGRGLDLPQLLALTEEFYR 82
Cdd:cd01151 8 NLDDLLTEEE-RAIRDTAREFCQEELAPRVLEAYREEKFDRKIIEEMGELGLLGA-TIKGYGCAGLSSVAYGLIAREVER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 83 ADAGIA--LTLQLaSFGCELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWI 160
Cdd:cd01151 86 VDSGYRsfMSVQS-SLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 161 GNGVEADWITLYARtgDDESNPYANyslFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIgEEGEGFWML 240
Cdd:cd01151 165 TNSPIADVFVVWAR--NDETGKIRG---FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLL-PGAEGLRGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 241 ADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYW 320
Cdd:cd01151 239 FKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKATPEQ 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496171797 321 AALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQrNLIYGQA 382
Cdd:cd01151 319 ISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIH-ALILGRA 379
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
16-378 |
4.52e-64 |
|
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: 209.13 E-value: 4.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 16 IKAEAREFAREHI-----EPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIalt 90
Cdd:cd01152 6 FRAEVRAWLAAHLppelrEESALGYREGREDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPV--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 91 lQLASFGCELT----YEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIGNGVEA 166
Cdd:cd01152 83 -PFNQIGIDLAgptiLAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 167 DWITLYARTgDDESNPYANYSLFIVPTDTDGYEAEhiPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNH 246
Cdd:cd01152 162 DWAWLLVRT-DPEAPKHRGISILLVDMDSPGVTVR--PIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 247 GRIAVSGHGIGLAAAAIESTWEFVHDreqfGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYWAALSKT 326
Cdd:cd01152 239 ERVSIGGSAATFFELLLARLLLLTRD----GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 327 NATETATSVAEQGMQFHGGRSILDE--------RRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:cd01152 315 FGSELAQELAELALELLGTAALLRDpapgaelaGRWEADYLRSRATTIYGGTSEIQRNII 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
22-381 |
3.54e-63 |
|
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: 207.71 E-value: 3.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 22 EFAREHIEPNAQEyyQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRaDAGIALTLQL-ASFGCEL 100
Cdd:cd01161 40 KFFEEVNDPAKND--QLEKIPRKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVGM-DLGFSVTLGAhQSIGFKG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 101 TYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEK--DGDEYVINGEKYWIGNGVEADWITLYART--G 176
Cdd:cd01161 117 ILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTAVLseDGKHYVLNGSKIWITNGGIADIFTVFAKTevK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 177 DDESNPYANYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRIAVSGHGI 256
Cdd:cd01161 197 DATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALI 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 257 GLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYW--AALSKTNATETATS 334
Cdd:cd01161 277 GTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAEYQieAAISKVFASEAAWL 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 496171797 335 VAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLIYGQ 381
Cdd:cd01161 357 VVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFIALT 403
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
3-378 |
1.57e-57 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 192.78 E-value: 1.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 3 LLDDSivpehARDIKAEAREFAREHIEPNAQEYYQAGEYPEEI---LEAGqEANLVAQDIPEEWGGRGLDLPQLLALTEE 79
Cdd:PLN02519 25 LFDDT-----QLQFKESVQQFAQENIAPHAAAIDATNSFPKDVnlwKLMG-DFNLHGITAPEEYGGLGLGYLYHCIAMEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 80 FYRADAGIALTLQLASFGC-ELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKY 158
Cdd:PLN02519 99 ISRASGSVGLSYGAHSNLCiNQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 159 WIGNGVEADWITLYARTgdDESNPYANYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFW 238
Cdd:PLN02519 179 WCTNGPVAQTLVVYAKT--DVAAGSKGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVY 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 239 MLADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEG 318
Cdd:PLN02519 257 VMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDR 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 319 YWAALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:PLN02519 337 KDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
24-373 |
3.16e-54 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 183.39 E-value: 3.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 24 AREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIALTLQLASFGCELTYe 103
Cdd:PRK12341 21 TRNFPEEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLITNGQCIHSMRRF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 104 yGTDEQceeyIRPVAEGEQRSG-----LGVSEPDTGSDLAGMETTA-EKDGDEYvINGEKYWIGNGVEADWITLYARTgD 177
Cdd:PRK12341 100 -GSAEQ----LRKTAESTLETGdpayaLALTEPGAGSDNNSATTTYtRKNGKVY-LNGQKTFITGAKEYPYMLVLARD-P 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 178 DESNPYANYSLFIVPTDTDGYEAEHIpEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRIAVSGHGIG 257
Cdd:PRK12341 173 QPKDPKKAFTLWWVDSSKPGIKINPL-HKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 258 LAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYWAALSKTNATETATSVAE 337
Cdd:PRK12341 252 FAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVID 331
|
330 340 350
....*....|....*....|....*....|....*.
gi 496171797 338 QGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEI 373
Cdd:PRK12341 332 DAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
1-380 |
5.13e-50 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 173.20 E-value: 5.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 1 MDLLDDSivPEHARdIKAEAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEF 80
Cdd:PTZ00461 32 MDLYNPT--PEHAA-LRETVAKFSREVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHEL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 81 YRADAGIALT-LQLASFGCELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDE-YVINGEKY 158
Cdd:PTZ00461 109 SKYDPGFCLAyLAHSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 159 WIGNGVEADWITLYARTGddesnpyANYSLFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIGEEGEGFW 238
Cdd:PTZ00461 189 WITNGTVADVFLIYAKVD-------GKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 239 MLADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEG 318
Cdd:PTZ00461 262 GMMRNLELERVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNR 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496171797 319 YWAALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANE-----IQRNLIYG 380
Cdd:PTZ00461 342 LGSDAAKLFATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEahhknITKDLLKG 408
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
18-374 |
7.32e-47 |
|
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: 164.87 E-value: 7.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 18 AEAREFAREHIEPNAQEYYQAG--------EYPEEILEAGQ---EANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAG 86
Cdd:cd01153 3 EEVARLAENVLAPLNADGDREGpvfddgrvVVPPPFKEALDafaEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 87 iALTLQLASFGCELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGD-EYVINGEKYWIGNGVE 165
Cdd:cd01153 83 -LMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADgSWRINGVKRFISAGEH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 166 --ADWITLY--ARTGddESNPYAN-YSLFIVPTDTDGYE-----AEHIPEKMAMRASKQAHIELEDCRIPeenLIGEEGE 235
Cdd:cd01153 162 dmSENIVHLvlARSE--GAPPGVKgLSLFLVPKFLDDGErngvtVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 236 GFWMLADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAV---QHG-----LSDMLIEFESARSL---T 304
Cdd:cd01153 237 GLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVtiiHHPdvrrsLMTQKAYAEGSRALdlyT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 305 WRACE----KVQNGENEGYWAALS-------KTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEI 373
Cdd:cd01153 317 ATVQDlaerKATEGEDRKALSALAdlltpvvKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
.
gi 496171797 374 Q 374
Cdd:cd01153 397 Q 397
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
24-374 |
7.40e-44 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 156.14 E-value: 7.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 24 AREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIALTLQLASfGCELTYE 103
Cdd:PRK03354 21 ASENWEAYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPG-GFNTFLR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 104 YGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIGNGVEADWITLYARTGDDESNPY 183
Cdd:PRK03354 100 EGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 184 anYSLFIVPTDTDGYEAEHIPeKMAMRASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRIAVSGHGIGLAAAAI 263
Cdd:PRK03354 180 --YTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 264 ESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGYWAALSKTNATETATSVAEQGMQFH 343
Cdd:PRK03354 257 EDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVL 336
|
330 340 350
....*....|....*....|....*....|.
gi 496171797 344 GGRSILDERRIARVYRDVRIPVIYEGANEIQ 374
Cdd:PRK03354 337 GGVGIAGNHRISRFWRDLRVDRVSGGSDEMQ 367
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
11-378 |
4.20e-42 |
|
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: 151.77 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 11 EHARDIKAEAREFAREHIEPNAQE---YYQAGEYP--------EEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEE 79
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEfleYYAEGGDRwwtpppiiEKLKAKAKAEGLWNLFLPEVSGLSGLTNLEYAYLAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 80 FYRAdagialtlQLAS--FGC--------ELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGS-DLAGMETTAEKDG 148
Cdd:cd01155 81 TGRS--------FFAPevFNCqapdtgnmEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASsDATNIECSIERDG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 149 DEYVINGEKYWIGNGVEAD---WITLyARTGDDESNPYANYSLFIVPTDTDGYEaehIPEKMAMRASKQAH-----IELE 220
Cdd:cd01155 153 DDYVINGRKWWSSGAGDPRckiAIVM-GRTDPDGAPRHRQQSMILVPMDTPGVT---IIRPLSVFGYDDAPhghaeITFD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 221 DCRIPEENLIGEEGEGFWMLADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESA 300
Cdd:cd01155 229 NVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 301 RSLTWRACEKVQNGENEG--YWAALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:cd01155 309 RLLVLKAAHMIDTVGNKAarKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSI 388
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
234-378 |
5.83e-41 |
|
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: 141.62 E-value: 5.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 234 GEGFWMLADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQN 313
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496171797 314 GENEGYWAALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQRNLI 378
Cdd:pfam00441 81 GGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNII 145
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
4-373 |
2.62e-38 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 141.91 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 4 LDDSIVPEHaRDIKAEAREFAREHIEPNAQEYYQAGEYPEEILEagQEANL-VAQDIPEEWGGRGLDLPQLLALTEEFYR 82
Cdd:PLN02526 25 FDDLLTPEE-QALRKRVRECMEKEVAPIMTEYWEKAEFPFHIIP--KLGSLgIAGGTIKGYGCPGLSITASAIATAEVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 83 ADAGIALTLQLASFGCELTYEY-GTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKDGDEYVINGEKYWIG 161
Cdd:PLN02526 102 VDASCSTFILVHSSLAMLTIALcGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 162 NGVEADWITLYAR-TGDDESNPyanyslFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEEN-LIGEegEGFWM 239
Cdd:PLN02526 182 NSTFADVLVIFARnTTTNQING------FIVKKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDrLPGV--NSFQD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 240 LADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEGY 319
Cdd:PLN02526 254 TNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVGWRLCKLYESGKMTPG 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 496171797 320 WAALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEI 373
Cdd:PLN02526 334 HASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
125-220 |
1.80e-29 |
|
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: 109.29 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 125 GLGVSEPDTGSDLAGMETTA-EKDGDEYVINGEKYWIGNGVEADWITLYARTGDDEsnPYANYSLFIVPTDTDGYEAEHI 203
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDD--RHGGISLFLVPKDAPGVSVRRI 78
|
90
....*....|....*..
gi 496171797 204 PEKMAMRASKQAHIELE 220
Cdd:pfam02770 79 ETKLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
10-121 |
1.23e-26 |
|
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: 102.54 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 10 PEHARDIKAEAREFAREHIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIAL 89
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 496171797 90 TLQLAS-FGCELTYEYGTDEQCEEYIRPVAEGE 121
Cdd:pfam02771 81 ALSVHSsLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
80-374 |
1.75e-26 |
|
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: 109.38 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 80 FYRADAGIALTLQLASFGCELTYEYGtDEQCEEYIRPVAEGEQRSGL----GVSEPDTGSDLAGMETTAEKD-GDEYVIN 154
Cdd:cd01154 102 LSDAAAGLLCPLTMTDAAVYALRKYG-PEELKQYLPGLLSDRYKTGLlggtWMTEKQGGSDLGANETTAERSgGGVYRLN 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 155 GEKyWIGNGVEADWITLYARTGDDESNPyANYSLFIVP-TDTDG----YEAEHIPEKMAMRASKQAHIELEDCripEENL 229
Cdd:cd01154 181 GHK-WFASAPLADAALVLARPEGAPAGA-RGLSLFLVPrLLEDGtrngYRIRRLKDKLGTRSVATGEVEFDDA---EAYL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 230 IGEEGEGFWMLADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRAC- 308
Cdd:cd01154 256 IGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAAr 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496171797 309 --EKVQNGENEGY-WA----ALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQ 374
Cdd:cd01154 336 afDRAAADKPVEAhMArlatPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
43-374 |
1.62e-21 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 96.09 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 43 EEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIALTLQLASFGCELTYEYGTDEQCEEYIRPVAEGEQ 122
Cdd:PTZ00456 102 KEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEW 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 123 RSGLGVSEPDTGSDLAGMETTAEKDGD-EYVINGEKYWIGNGvEAD------WITLyARTGDdeSNPYA-NYSLFIVP-- 192
Cdd:PTZ00456 182 SGTMCLTEPQCGTDLGQVKTKAEPSADgSYKITGTKIFISAG-DHDltenivHIVL-ARLPN--SLPTTkGLSLFLVPrh 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 193 -TDTDG-YEAEH------IPEKMAMRASKQAHIELEDCRipeENLIGEEGEGFWMLADFFNHGRIAVSGHGIGLAAAAIE 264
Cdd:PTZ00456 258 vVKPDGsLETAKnvkcigLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQ 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 265 STWEFVHDREQFgRTISDFQA--------VQHGLSDMLIEF-----ESARSL------------TWRACEKVQNGENE-G 318
Cdd:PTZ00456 335 NALRYARERRSM-RALSGTKEpekpadriICHANVRQNILFakavaEGGRALlldvgrlldihaAAKDAATREALDHEiG 413
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 496171797 319 YWAALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEIQ 374
Cdd:PTZ00456 414 FYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQ 469
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
99-373 |
5.53e-20 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 91.78 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 99 ELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTG-SDLAGMETTAEKDGDEYVINGEKYWIGNGVEADWITLYARTGD 177
Cdd:PLN02876 527 EVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQVAsSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKT 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 178 DESNP-YANYSLFIVPTDTDGYeaeHIPEKMAM-----RASKQAHIELEDCRIPEENLIGEEGEGFWMLADFFNHGRIAV 251
Cdd:PLN02876 607 DFNAPkHKQQSMILVDIQTPGV---QIKRPLLVfgfddAPHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHH 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 252 SGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQ---NGENEGYwAALSKTNA 328
Cdd:PLN02876 684 CMRLIGAAERGMQLMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDrlgNKKARGI-IAMAKVAA 762
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 496171797 329 TETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEI 373
Cdd:PLN02876 763 PNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLRIADGPDEV 807
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
99-381 |
9.54e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 91.17 E-value: 9.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 99 ELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTA-----EKDGDEYV---INGEKYWIGNGVEADWIT 170
Cdd:PRK13026 169 ELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGivcrgEFEGEEVLglrLTWDKRYITLAPVATVLG 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 171 LYARTGD------DESNPYANYSLfiVPTDTDGYEA--EHIPEKMA-MRASKQAhielEDCRIPEENLIG---EEGEGFW 238
Cdd:PRK13026 249 LAFKLRDpdgllgDKKELGITCAL--IPTDHPGVEIgrRHNPLGMAfMNGTTRG----KDVFIPLDWIIGgpdYAGRGWR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 239 MLADFFNHGR-IAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDM---LIEFESARSLTwraCEKVQNG 314
Cdd:PRK13026 323 MLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIagnTYLLEAARRLT---TTGLDLG 399
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 315 ENEGYWAALSKTNATETATSVAEQGMQFHGGRSILDERR--IARVYRDVRIPVIYEGANEIQRNL-IYGQ 381
Cdd:PRK13026 400 VKPSVVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKnyLGHAYMAVPIAITVEGANILTRNLmIFGQ 469
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
99-381 |
1.10e-16 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 81.79 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 99 ELTYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTA-----EKDGDEYV---INGEKYWIGNGVEADWIT 170
Cdd:PRK09463 170 ELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGvvckgEWQGEEVLgmrLTWNKRYITLAPIATVLG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 171 LYARTGD------DESNPyaNYSLFIVPTDTDGYE--AEHIPekmaMRASKQ-AHIELEDCRIPEENLIGEE---GEGFW 238
Cdd:PRK09463 250 LAFKLYDpdgllgDKEDL--GITCALIPTDTPGVEigRRHFP----LNVPFQnGPTRGKDVFIPLDYIIGGPkmaGQGWR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 239 MLADFFNHGR-IAVSGHGIGLAAAAIESTWEFVHDREQFGRTISDFQAVQHGLSDM-----LIEfeSARSLTwraCEKVQ 312
Cdd:PRK09463 324 MLMECLSVGRgISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIagnayLMD--AARTLT---TAAVD 398
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496171797 313 NGENEGYWAALSKTNATETATSVAEQGMQFHGGRSILDERR--IARVYRDVRIPVIYEGANEIQRNL-IYGQ 381
Cdd:PRK09463 399 LGEKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNnfLARAYQAAPIAITVEGANILTRSLmIFGQ 470
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
18-383 |
1.35e-15 |
|
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: 77.36 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 18 AEAREFAREhIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIALTLQlASFG 97
Cdd:cd01163 1 ARARPLAAR-IAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALR-AHFG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 98 -CELTYEYGTDEQCEEYIRPVAEGeQRSGLGVSEpdTGSDLAGMETTA-EKDGDEYVINGEKYWIGNGVEADWITLYARt 175
Cdd:cd01163 79 fVEALLLAGPEQFRKRWFGRVLNG-WIFGNAVSE--RGSVRPGTFLTAtVRDGGGYVLNGKKFYSTGALFSDWVTVSAL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 176 gDDESNPYAnyslFIVPTDTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLIgeegeGFWMLADFFNHGRIAVSGHG 255
Cdd:cd01163 155 -DEEGKLVF----AAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVL-----PRPNAPDRGTLLTAIYQLVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 256 I----GLAAAAIESTWEFVHDReqfGRTIS---------DFQAVQHgLSDMLIEFESARSLTWRACEKVQNGENEGywAA 322
Cdd:cd01163 225 AavlaGIARAALDDAVAYVRSR---TRPWIhsgaesardDPYVQQV-VGDLAARLHAAEALVLQAARALDAAAAAG--TA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 323 LSKTNATETATSVAE-------QGMQ-----FH--GGRSILDERRIARVYRDVRI-----PVIYEgANEIQRNLIYGQAP 383
Cdd:cd01163 299 LTAEARGEAALAVAAakvvvtrLALDatsrlFEvgGASATAREHNLDRHWRNARThtlhnPVIYK-ERAVGDYALNGELP 377
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
251-372 |
2.71e-14 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 69.30 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 251 VSGHGIGLAAAAIESTWEFVHDREQ--FGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKV--------QNGENEGYW 320
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIeaaaaagkPVTPALRAE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 496171797 321 AALSKTNATETATSVAEQGMQFHGGRSILDERRIARVYRDVRIPVIYEGANE 372
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
18-362 |
8.88e-11 |
|
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: 62.75 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 18 AEAREFAREhIEPNAQEYYQAGEYPEEILEAGQEANLVAQDIPEEWGGRGLDLPQLLALTEEFYRADAGIALTLQLASFG 97
Cdd:cd01159 1 ARAEDLAPL-IRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAWVASIVATH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 98 CELTYEYGTDEQCEEYirpvaegeqrsglgVSEPDT--GSDLAGMEtTAEKDGDEYVINGEKYWIGNGVEADWITLYART 175
Cdd:cd01159 80 SRMLAAFPPEAQEEVW--------------GDGPDTllAGSYAPGG-RAERVDGGYRVSGTWPFASGCDHADWILVGAIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 176 GDDESNPyaNYSLFIVPtdTDGYEAEHIPEKMAMRASKQAHIELEDCRIPEENLI----GEEGEGFWMLADFFN--HGRI 249
Cdd:cd01159 145 EDDDGGP--LPRAFVVP--RAEYEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRTLtagdMMAGDGPGGSTPVYRmpLRQV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 250 AVSGH---GIGLAAAAIESTWEFVHDREQ---FGRTISDFQAVQHGLSDMLIEFESARSLTWRACEKVQNGENEG-YWAA 322
Cdd:cd01159 221 FPLSFaavSLGAAEGALAEFLELAGKRVRqygAAVKMAEAPITQLRLAEAAAELDAARAFLERATRDLWAHALAGgPIDV 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 496171797 323 LSKTNATETATSVAEQGMQ-----FH--GGRSILDERRIARVYRDVR 362
Cdd:cd01159 301 EERARIRRDAAYAAKLSAEavdrlFHaaGGSALYTASPLQRIWRDIH 347
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
117-373 |
6.74e-07 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 51.29 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 117 VAEGEQRSGL----GVSEPDTGSDLAGMETTAEK-DGDEYVINGEKyWIGNGVEADWITLYARTGddesnpyANYSLFIV 191
Cdd:PRK11561 169 LLPGGQKRGLligmGMTEKQGGSDVLSNTTRAERlADGSYRLVGHK-WFFSVPQSDAHLVLAQAK-------GGLSCFFV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 192 PT-----DTDGYEAEHIPEKMAMRASKQAHIELEDCripEENLIGEEGEGFWMLADFFNHGRI--AVSGHGigLAAAAIE 264
Cdd:PRK11561 241 PRflpdgQRNAIRLERLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIRLILKMGGMTRFdcALGSHG--LMRRAFS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 265 STWEFVHDREQFGRTISDFQAVQHGLSDMLIEFESARSLTWR---ACEKVQNgENEGYWAALSkTNATETATS------V 335
Cdd:PRK11561 316 VAIYHAHQRQVFGKPLIEQPLMRQVLSRMALQLEGQTALLFRlarAWDRRAD-AKEALWARLF-TPAAKFVICkrgipfV 393
|
250 260 270
....*....|....*....|....*....|....*...
gi 496171797 336 AEqGMQFHGGRSILDERRIARVYRDVRIPVIYEGANEI 373
Cdd:PRK11561 394 AE-AMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNI 430
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
69-294 |
7.28e-07 |
|
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: 51.18 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 69 DLPQLLALTE--EFYRADAGIALTLQLASFGCELtYEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEK 146
Cdd:cd01150 80 DPEKMLALTNslGGYDLSLGAKLGLHLGLFGNAI-KNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 147 D--GDEYVIN-----GEKYWIGN-GVEADWITLYAR--TGDDesnpyaNYSL--FIVPT-DTD------GYEAEHIPEKM 207
Cdd:cd01150 159 DplTQEFVINtpdftATKWWPGNlGKTATHAVVFAQliTPGK------NHGLhaFIVPIrDPKthqplpGVTVGDIGPKM 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 208 AMRASKQAHIELEDCRIPEENL----------------IGEEGEGFWMLADFFNHGRIAVSGHGIGLA--AAAIESTWEF 269
Cdd:cd01150 233 GLNGVDNGFLQFRNVRIPRENLlnrfgdvspdgtyvspFKDPNKRYGAMLGTRSGGRVGLIYDAAMSLkkAATIAIRYSA 312
|
250 260 270
....*....|....*....|....*....|..
gi 496171797 270 VhdREQFGRT-------ISDFQAVQHGLSDML 294
Cdd:cd01150 313 V--RRQFGPKpsdpevqILDYQLQQYRLFPQL 342
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
86-294 |
1.04e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 50.63 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 86 GIALTLQLASFGCELTyEYGTDEQCEEYIRPVAEGEQRSGLGVSEPDTGSDLAGMETTAEKD--GDEYVIN-----GEKY 158
Cdd:PLN02636 138 GIKLGVQYSLWGGSVI-NLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDplTDEFVINtpndgAIKW 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 159 WIGN-GVEADWITLYAR----TGDDESNPYANYSLFIVPTDT-------DGYEAEHIPEKMAMRASKQAHIELEDCRIPE 226
Cdd:PLN02636 217 WIGNaAVHGKFATVFARlklpTHDSKGVSDMGVHAFIVPIRDmkthqvlPGVEIRDCGHKVGLNGVDNGALRFRSVRIPR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496171797 227 ENLIGEEGE----------------GFWMLADFFNHGRIAVSGHGIGLAAAAIESTWEFVHDREQFGR------TISDFQ 284
Cdd:PLN02636 297 DNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGPpkqpeiSILDYQ 376
|
250
....*....|
gi 496171797 285 AVQHGLSDML 294
Cdd:PLN02636 377 SQQHKLMPML 386
|
|
| |
