|
Name |
Accession |
Description |
Interval |
E-value |
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
68-815 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1338.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 68 RRKLLSTPMFAWFQRVLPPMSDTERDAIEAGTVWWDGELFSGRPDWNKLLAYPRAQLSEEEQAFLDGPTEELCAMVSDWQ 147
Cdd:PRK09463 23 RRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLTAEEQAFLDGPVEELCRMVNDWQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 148 IGQQL-DLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLGPAELLLHYGTDEQRQ 226
Cdd:PRK09463 103 ITHELaDLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGELLLHYGTDEQKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 227 HYLPRLARGDDIPCFALTGPLAGSDAGAMPDSGIVCKGQWQGEEVLGLRLTWEKRYITLGPVATLLGLAFKAYDPDHLLG 306
Cdd:PRK09463 183 HYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYITLAPIATVLGLAFKLYDPDGLLG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 307 EQEDLGISLALVPTDTPGVEIGRRHLPLGAAFMNGPNSGKDVFIPLNYLIGGQDMLGKGWMMLMNCLSVGRSISLPAGAT 386
Cdd:PRK09463 263 DKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQGWRMLMECLSVGRGISLPSNST 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 387 GSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSARILTAGAVDLGEKPSVLSAILKYHLTERGRECV 466
Cdd:PRK09463 343 GGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKPSVLSAIAKYHLTERGRQVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 467 SHAMDVHGGKGIIMGPNNYLARAWQGAPIAITVEGANILSRNLMIFGQGAIRCHPYVLKEMALAGREDKKqALLEFDALL 546
Cdd:PRK09463 423 NDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVLKEMEAAQNNDKQ-ALKAFDKAL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 547 LQHIGFAVSNAASSLILSLGLGGFSEVPGDNLCRPYFRALNRLAAAFALLADLSMLLLGGELKRRERLSARLGDALSHLY 626
Cdd:PRK09463 502 FGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLGGSLKRRERLSARLGDILSQLY 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 627 LASAALKRYHDLDYPAHSRPLLCWAMEESLGHAEQALDELLGNFPNKLLGCALRVLIFPFGRRHKGPSDAQDTQVAEILG 706
Cdd:PRK09463 582 LASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFPLGRRYRAPSDKLDHQVAKLLQ 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 707 RNSgdPALEELLVGCYRPQAENDPVAALQQAVDLLQGAQPLQKKLDEALRKGRVQEVPGQSPLDAAVGAGVLSAEEAQSL 786
Cdd:PRK09463 662 TPS--ATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGKLPFLRLDELADEALAAGVISEEEAALL 739
|
730 740
....*....|....*....|....*....
gi 1222445847 787 HQAETARRVVIDVDDFAKEELKLGRGKVR 815
Cdd:PRK09463 740 REAEEARLRVINVDDFDPEELAAKPVKLP 768
|
|
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
16-808 |
0e+00 |
|
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain acyl-CoA dehydrogenases that includes YafH from Escherichia coli K-12 and Salmonella enterica LT2 (also called FadF), now called FadE.
Pssm-ID: 439499 [Multi-domain] Cd Length: 816 Bit Score: 1078.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 16 LAHRRTAALPALGVVAGYLVLMGLFSNAPTWLLAVFWLLLLAVALPLAlpeqRRKLLSTPMFAWFQRVLPPMSDTERDAI 95
Cdd:NF038187 14 LAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSI----RQSLISAPALKAFRKVMPEMSSTEKEAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 96 EAGTVWWDGELFSGRPDWNKLLAYPRAQLSEEEQAFLDGPTEELCAMVSDWQIGQQL-DLPAKAWQHIKQHGFFALIIPR 174
Cdd:NF038187 90 DAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELaDLPPEVWQYLKDHRFFAMIIKK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 175 EYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLGPAELLLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGA 254
Cdd:NF038187 170 EYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTSPEAGSDAGS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 255 MPDSGIVCKGQWQGEEVLGLRLTWEKRYITLGPVATLLGLAFKAYDPDHLLGEQEDLGISLALVPTDTPGVEIGRRHLPL 334
Cdd:NF038187 250 IPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGVEIGRRHFPL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 335 GAAFMNGPNSGKDVFIPLNYLIGGQDMLGKGWMMLMNCLSVGRSISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFE 414
Cdd:NF038187 330 NVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQFKLPIGKME 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 415 GIQEALARIGGNTWLMDSARILTAGAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGIIMGPNNYLARAWQGAP 494
Cdd:NF038187 410 GIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNFLARGYQGAP 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 495 IAITVEGANILSRNLMIFGQGAIRCHPYVLKEMALAGREDKKQALLEFDALLLQHIGFAVSNAASSLILSLGLGGFSEVP 574
Cdd:NF038187 490 IAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDSEQALNDFDKALFGHIGFVGSNLVRSFWLGLTNGRFSSAP 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 575 GDNLCRPYFRALNRLAAAFALLADLSMLLLGGELKRRERLSARLGDALSHLYLASAALKRYHDLDYPAHSRPLLCWAMEE 654
Cdd:NF038187 570 YKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDLPLVHWAVQD 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 655 SLGHAEQALDELLGNFPNKLLGCALRVLIFPFGRRHKGPSDAQDTQVAEILGRNSgdPALEELLVGCYRPQAENDPVAAL 734
Cdd:NF038187 650 SLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPS--ATRSRLGRGQYLTPSEHNPVGLL 727
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222445847 735 QQAVDLLQGAQPLQKKLDEALRKG----RVQEVPGQspldaAVGAGVLSAEEAQSLHQAETARRVVIDVDDFAKEELK 808
Cdd:NF038187 728 EQALKDILAAEPIHDRVCKAAGKRlpfmRLDKLAEE-----GLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
517-802 |
6.65e-113 |
|
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally uncharacterized and is predominantly found in various prokaryotic acyl-coenzyme A dehydrogenases and seems to be essential for its function.
Pssm-ID: 430522 [Multi-domain] Cd Length: 284 Bit Score: 344.86 E-value: 6.65e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 517 IRCHPYVLKEMALAGREDKKQALLEFDALLLQHIGFAVSNAASSLILSLGLGGFSEVPGDNLCRPYFRALNRLAAAFALL 596
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDKEQALKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 597 ADLSMLLLGGELKRRERLSARLGDALSHLYLASAALKRYHDLDYPAHSRPLLCWAMEESLGHAEQALDELLGNFPNKLLG 676
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 677 CALRVLIFPFGRRHKGPSDAQDTQVAEILGRNSgdPALEELLVGCYRPQAENDPVAALQQAVDLLQGAQPLQKKLDEALR 756
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPG--EARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1222445847 757 KGRVQEVPGQSPLDAAVGAGVLSAEEAQSLHQAETARRVVIDVDDF 802
Cdd:pfam09317 239 AGKLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
123-511 |
3.81e-90 |
|
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: 289.05 E-value: 3.81e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 123 QLSEEEQAFLDgPTEELCAMVSDW---QIGQQLDLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGD 199
Cdd:COG1960 4 ELTEEQRALRD-EVREFAEEEIAPearEWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 200 LASTVMVPNslGPAELLLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAMPdsgivCKGQWQGEevlGLRLTWE 279
Cdd:COG1960 83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALR-----TTAVRDGD---GYVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 280 KRYITLGPVATLLGLAFKAyDPDhlLGEQedlGISLALVPTDTPGVEIGRRHLPLG-AAFMNGPNSGKDVFIPLNYLIGG 358
Cdd:COG1960 153 KTFITNAPVADVILVLART-DPA--AGHR---GISLFLVPKDTPGVTVGRIEDKMGlRGSDTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 359 qdmLGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSARILTA 438
Cdd:COG1960 227 ---EGKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222445847 439 GAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGIImgpNNY-LARAWQGAPIAITVEGANILSRNLMI 511
Cdd:COG1960 303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT---REYpLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
210-510 |
8.31e-44 |
|
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: 161.30 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 210 LGPAELLLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAM-----PDSGivckgqwqgeevlGLRLTWEKRYIT 284
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIrttarKDGD-------------GYVLNGRKIFIS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 285 LGPVATLLGLAFKAYDPDHLLGeqedlGISLALVPTDTPGVEIGRRHLPLGaafMNGPNSG----KDVFIPLNYLIGGQd 360
Cdd:cd00567 109 NGGDADLFIVLARTDEEGPGHR-----GISAFLVPADTPGVTVGRIWDKMG---MRGSGTGelvfDDVRVPEDNLLGEE- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 361 mlGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSARILTAGA 440
Cdd:cd00567 180 --GGGFELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWL 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222445847 441 VDLGE-KPSVLSAILKYHLTERGRECVSHAMDVHGGKGIIMGpnNYLARAWQGAPIAITVEGANILSRNLM 510
Cdd:cd00567 257 LDQGPdEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSRE--YPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
68-815 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1338.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 68 RRKLLSTPMFAWFQRVLPPMSDTERDAIEAGTVWWDGELFSGRPDWNKLLAYPRAQLSEEEQAFLDGPTEELCAMVSDWQ 147
Cdd:PRK09463 23 RRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLTAEEQAFLDGPVEELCRMVNDWQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 148 IGQQL-DLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLGPAELLLHYGTDEQRQ 226
Cdd:PRK09463 103 ITHELaDLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLGPGELLLHYGTDEQKD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 227 HYLPRLARGDDIPCFALTGPLAGSDAGAMPDSGIVCKGQWQGEEVLGLRLTWEKRYITLGPVATLLGLAFKAYDPDHLLG 306
Cdd:PRK09463 183 HYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYITLAPIATVLGLAFKLYDPDGLLG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 307 EQEDLGISLALVPTDTPGVEIGRRHLPLGAAFMNGPNSGKDVFIPLNYLIGGQDMLGKGWMMLMNCLSVGRSISLPAGAT 386
Cdd:PRK09463 263 DKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQGWRMLMECLSVGRGISLPSNST 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 387 GSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSARILTAGAVDLGEKPSVLSAILKYHLTERGRECV 466
Cdd:PRK09463 343 GGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKPSVLSAIAKYHLTERGRQVI 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 467 SHAMDVHGGKGIIMGPNNYLARAWQGAPIAITVEGANILSRNLMIFGQGAIRCHPYVLKEMALAGREDKKqALLEFDALL 546
Cdd:PRK09463 423 NDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVLKEMEAAQNNDKQ-ALKAFDKAL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 547 LQHIGFAVSNAASSLILSLGLGGFSEVPGDNLCRPYFRALNRLAAAFALLADLSMLLLGGELKRRERLSARLGDALSHLY 626
Cdd:PRK09463 502 FGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLGGSLKRRERLSARLGDILSQLY 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 627 LASAALKRYHDLDYPAHSRPLLCWAMEESLGHAEQALDELLGNFPNKLLGCALRVLIFPFGRRHKGPSDAQDTQVAEILG 706
Cdd:PRK09463 582 LASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFPLGRRYRAPSDKLDHQVAKLLQ 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 707 RNSgdPALEELLVGCYRPQAENDPVAALQQAVDLLQGAQPLQKKLDEALRKGRVQEVPGQSPLDAAVGAGVLSAEEAQSL 786
Cdd:PRK09463 662 TPS--ATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGKLPFLRLDELADEALAAGVISEEEAALL 739
|
730 740
....*....|....*....|....*....
gi 1222445847 787 HQAETARRVVIDVDDFAKEELKLGRGKVR 815
Cdd:PRK09463 740 REAEEARLRVINVDDFDPEELAAKPVKLP 768
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
68-809 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 1103.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 68 RRKLLSTPMFAWFQRVLPPMSDTERDAIEAGTVWWDGELFSGRPDWNKLLAYPRAQLSEEEQAFLDGPTEELCAMVSDWQ 147
Cdd:PRK13026 22 RRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAEEQAFIDNEVETLLTMLDDWD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 148 IGQQL-DLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLGPAELLLHYGTDEQRQ 226
Cdd:PRK13026 102 IVQNRkDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPGELLTHYGTQEQKD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 227 HYLPRLARGDDIPCFALTGPLAGSDAGAMPDSGIVCKGQWQGEEVLGLRLTWEKRYITLGPVATLLGLAFKAYDPDHLLG 306
Cdd:PRK13026 182 YWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLAPVATVLGLAFKLRDPDGLLG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 307 EQEDLGISLALVPTDTPGVEIGRRHLPLGAAFMNGPNSGKDVFIPLNYLIGGQDMLGKGWMMLMNCLSVGRSISLPAGAT 386
Cdd:PRK13026 262 DKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGWRMLVECLSAGRGISLPALGT 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 387 GSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSARILTAGAVDLGEKPSVLSAILKYHLTERGRECV 466
Cdd:PRK13026 342 ASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKPSVVTAIAKYHMTELARDVV 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 467 SHAMDVHGGKGIIMGPNNYLARAWQGAPIAITVEGANILSRNLMIFGQGAIRCHPYVLKEMALAGREDKKQALLEFDALL 546
Cdd:PRK13026 422 NDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAEMEAAAMEDEHEGLEAFDSLL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 547 LQHIGFAVSNAASSLILSLGLGGFSEVPGDNLCRPYFRALNRLAAAFALLADLSMLLLGGELKRRERLSARLGDALSHLY 626
Cdd:PRK13026 502 FKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGGDLKRKEMLSARLGDVLSQLY 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 627 LASAALKRYHDLDYPAHSRPLLCWAMEESLGHAEQALDELLGNFPNKLLGCALRVLIFPFGRRHKGPSDAQDTQVAEILG 706
Cdd:PRK13026 582 LASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPLGNHFRAPSDKLARQLAELMM 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 707 RNSgdPALEELLVGCYRPQAENDPVAALQQAVDLLQGAQPLQKKLDEALRKGRVQ-EVPGQSPLDAAVGAGVLSAEEAQS 785
Cdd:PRK13026 662 TPG--PARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQREGKLPrKVPLLELFAKALEKGVITADEAEK 739
|
730 740
....*....|....*....|....
gi 1222445847 786 LHQAETARRVVIDVDDFAKEELKL 809
Cdd:PRK13026 740 LLAADKLRLDAIQVDDFTPDFMEK 763
|
|
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
16-808 |
0e+00 |
|
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain acyl-CoA dehydrogenases that includes YafH from Escherichia coli K-12 and Salmonella enterica LT2 (also called FadF), now called FadE.
Pssm-ID: 439499 [Multi-domain] Cd Length: 816 Bit Score: 1078.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 16 LAHRRTAALPALGVVAGYLVLMGLFSNAPTWLLAVFWLLLLAVALPLAlpeqRRKLLSTPMFAWFQRVLPPMSDTERDAI 95
Cdd:NF038187 14 LAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSI----RQSLISAPALKAFRKVMPEMSSTEKEAI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 96 EAGTVWWDGELFSGRPDWNKLLAYPRAQLSEEEQAFLDGPTEELCAMVSDWQIGQQL-DLPAKAWQHIKQHGFFALIIPR 174
Cdd:NF038187 90 DAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELaDLPPEVWQYLKDHRFFAMIIKK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 175 EYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLGPAELLLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGA 254
Cdd:NF038187 170 EYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTSPEAGSDAGS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 255 MPDSGIVCKGQWQGEEVLGLRLTWEKRYITLGPVATLLGLAFKAYDPDHLLGEQEDLGISLALVPTDTPGVEIGRRHLPL 334
Cdd:NF038187 250 IPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGVEIGRRHFPL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 335 GAAFMNGPNSGKDVFIPLNYLIGGQDMLGKGWMMLMNCLSVGRSISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFE 414
Cdd:NF038187 330 NVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQFKLPIGKME 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 415 GIQEALARIGGNTWLMDSARILTAGAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGIIMGPNNYLARAWQGAP 494
Cdd:NF038187 410 GIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNFLARGYQGAP 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 495 IAITVEGANILSRNLMIFGQGAIRCHPYVLKEMALAGREDKKQALLEFDALLLQHIGFAVSNAASSLILSLGLGGFSEVP 574
Cdd:NF038187 490 IAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDNDSEQALNDFDKALFGHIGFVGSNLVRSFWLGLTNGRFSSAP 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 575 GDNLCRPYFRALNRLAAAFALLADLSMLLLGGELKRRERLSARLGDALSHLYLASAALKRYHDLDYPAHSRPLLCWAMEE 654
Cdd:NF038187 570 YKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDLPLVHWAVQD 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 655 SLGHAEQALDELLGNFPNKLLGCALRVLIFPFGRRHKGPSDAQDTQVAEILGRNSgdPALEELLVGCYRPQAENDPVAAL 734
Cdd:NF038187 650 SLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPS--ATRSRLGRGQYLTPSEHNPVGLL 727
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222445847 735 QQAVDLLQGAQPLQKKLDEALRKG----RVQEVPGQspldaAVGAGVLSAEEAQSLHQAETARRVVIDVDDFAKEELK 808
Cdd:NF038187 728 EQALKDILAAEPIHDRVCKAAGKRlpfmRLDKLAEE-----GLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
517-802 |
6.65e-113 |
|
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally uncharacterized and is predominantly found in various prokaryotic acyl-coenzyme A dehydrogenases and seems to be essential for its function.
Pssm-ID: 430522 [Multi-domain] Cd Length: 284 Bit Score: 344.86 E-value: 6.65e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 517 IRCHPYVLKEMALAGREDKKQALLEFDALLLQHIGFAVSNAASSLILSLGLGGFSEVPGDNLCRPYFRALNRLAAAFALL 596
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNEDKEQALKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 597 ADLSMLLLGGELKRRERLSARLGDALSHLYLASAALKRYHDLDYPAHSRPLLCWAMEESLGHAEQALDELLGNFPNKLLG 676
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 677 CALRVLIFPFGRRHKGPSDAQDTQVAEILGRNSgdPALEELLVGCYRPQAENDPVAALQQAVDLLQGAQPLQKKLDEALR 756
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPG--EARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1222445847 757 KGRVQEVPGQSPLDAAVGAGVLSAEEAQSLHQAETARRVVIDVDDF 802
Cdd:pfam09317 239 AGKLPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
123-511 |
3.81e-90 |
|
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: 289.05 E-value: 3.81e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 123 QLSEEEQAFLDgPTEELCAMVSDW---QIGQQLDLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGD 199
Cdd:COG1960 4 ELTEEQRALRD-EVREFAEEEIAPearEWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 200 LASTVMVPNslGPAELLLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAMPdsgivCKGQWQGEevlGLRLTWE 279
Cdd:COG1960 83 LALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALR-----TTAVRDGD---GYVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 280 KRYITLGPVATLLGLAFKAyDPDhlLGEQedlGISLALVPTDTPGVEIGRRHLPLG-AAFMNGPNSGKDVFIPLNYLIGG 358
Cdd:COG1960 153 KTFITNAPVADVILVLART-DPA--AGHR---GISLFLVPKDTPGVTVGRIEDKMGlRGSDTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 359 qdmLGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSARILTA 438
Cdd:COG1960 227 ---EGKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAA 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222445847 439 GAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGIImgpNNY-LARAWQGAPIAITVEGANILSRNLMI 511
Cdd:COG1960 303 WLLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYT---REYpLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
210-510 |
8.31e-44 |
|
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: 161.30 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 210 LGPAELLLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAM-----PDSGivckgqwqgeevlGLRLTWEKRYIT 284
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIrttarKDGD-------------GYVLNGRKIFIS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 285 LGPVATLLGLAFKAYDPDHLLGeqedlGISLALVPTDTPGVEIGRRHLPLGaafMNGPNSG----KDVFIPLNYLIGGQd 360
Cdd:cd00567 109 NGGDADLFIVLARTDEEGPGHR-----GISAFLVPADTPGVTVGRIWDKMG---MRGSGTGelvfDDVRVPEDNLLGEE- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 361 mlGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSARILTAGA 440
Cdd:cd00567 180 --GGGFELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWL 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222445847 441 VDLGE-KPSVLSAILKYHLTERGRECVSHAMDVHGGKGIIMGpnNYLARAWQGAPIAITVEGANILSRNLM 510
Cdd:cd00567 257 LDQGPdEARLEAAMAKLFATEAAREVADLAMQIHGGRGYSRE--YPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
105-516 |
4.62e-37 |
|
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: 144.15 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 105 ELFSGRPDWNKLLAYPR---AQLSEEEQAFLdGPTEELCAMVSDWQIGQQL-DLPAKAWQHIKQHGFFALIIPREYGGKG 180
Cdd:cd01161 5 NMFLGDIVTKQVFPYPSvltEEQTEELNMLV-GPVEKFFEEVNDPAKNDQLeKIPRKTLTQLKELGLFGLQVPEEYGGLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 181 FSAYAHSQVAMKLAtRSGDLASTVMVPNSLGPAELLLhYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGampdsGI 260
Cdd:cd01161 84 LNNTQYARLAEIVG-MDLGFSVTLGAHQSIGFKGILL-FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAA-----SI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 261 VCKGQWQgEEVLGLRLTWEKRYITLGPVATLLgLAFKAYDPDHLLGEQEDlGISLALVPTDTPGVEIGRRHLPLGaafMN 340
Cdd:cd01161 157 RTTAVLS-EDGKHYVLNGSKIWITNGGIADIF-TVFAKTEVKDATGSVKD-KITAFIVERSFGGVTNGPPEKKMG---IK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 341 GPNSG----KDVFIPLNYLIGgqdMLGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGI 416
Cdd:cd01161 231 GSNTAevyfEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 417 QEALARIGGNTWLMDSARILTAGAVDLGEKP--SVLSAILKYHLTERGRECVSHAMDVHGGKGIIMGPNnyLARAWQGAP 494
Cdd:cd01161 307 QEKLANMAILQYATESMAYMTSGNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYG--VERVLRDLR 384
|
410 420
....*....|....*....|..
gi 1222445847 495 IAITVEGANILSRnLMIFGQGA 516
Cdd:cd01161 385 IFRIFEGTNEILR-LFIALTGL 405
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
155-477 |
5.06e-37 |
|
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: 143.18 E-value: 5.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 155 PAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLgPAELLLHYGTDEQRQHYLPRLAR 234
Cdd:cd01158 32 PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSL-GANPIIKFGTEEQKKKYLPPLAT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 235 GDDIPCFALTGPLAGSDAGAMPDSGIVCKGQWqgeevlglRLTWEKRYITLGPVATLLgLAFKAYDPDhlLGEQedlGIS 314
Cdd:cd01158 111 GEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPS--KGYR---GIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 315 LALVPTDTPGVEIGRRHLPLGaafMNGPNSG----KDVFIPLNYLIGGQdmlGKGWMMLMNCLSVGRsISLPAGATGSAK 390
Cdd:cd01158 177 AFIVERDTPGLSVGKKEDKLG---IRGSSTTelifEDVRVPKENILGEE---GEGFKIAMQTLDGGR-IGIAAQALGIAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 391 FSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNtwlMDSARILTAGAVDL---GEKPSVLSAILKYHLTERGRECVS 467
Cdd:cd01158 250 AALDAAVDYAKERKQFGKPIADFQGIQFKLADMATE---IEAARLLTYKAARLkdnGEPFIKEAAMAKLFASEVAMRVTT 326
|
330
....*....|
gi 1222445847 468 HAMDVHGGKG 477
Cdd:cd01158 327 DAVQIFGGYG 336
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
122-478 |
9.60e-35 |
|
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: 136.72 E-value: 9.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 122 AQLSEEEQAFLDGP----TEELCAMVSDWQIGQQLDLPAkawqhIKQHGFFALI--IPREYGGKGFSAYAHSQVAMKLAT 195
Cdd:cd01151 11 DLLTEEERAIRDTArefcQEELAPRVLEAYREEKFDRKI-----IEEMGELGLLgaTIKGYGCAGLSSVAYGLIAREVER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 196 RSGDLASTVMVPNSLGPAELLLhYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAMpdsgiVCKGQWQGEevlGLR 275
Cdd:cd01151 86 VDSGYRSFMSVQSSLVMLPIYD-FGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGM-----ETRARKDGG---GYK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 276 LTWEKRYITLGPVATLLGLAFKaydpdhllgEQEDLGISLALVPTDTPGVEIGRRHLPLG-AAFMNGPNSGKDVFIPLNY 354
Cdd:cd01151 157 LNGSKTWITNSPIADVFVVWAR---------NDETGKIRGFILERGMKGLSAPKIQGKFSlRASITGEIVMDNVFVPEEN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 355 LIGGQDMLGKGwmmlMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSAR 434
Cdd:cd01151 228 LLPGAEGLRGP----FKCLNNAR-YGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLAC 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1222445847 435 ILTAGAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGI 478
Cdd:cd01151 303 LRVGRLKDQGKATPEQISLLKRNNCGKALEIARTAREMLGGNGI 346
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
124-477 |
3.39e-25 |
|
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: 108.30 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 124 LSEEEQAF----LDGPTEELCAMVSDWQigQQLDLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATrsGD 199
Cdd:cd01162 1 LNEEQRAIqevaRAFAAKEMAPHAADWD--QKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALST--GC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 200 LASTVMVPNSLGPAELLLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAMPDSGIVckgqwQGEEVLglrLTWE 279
Cdd:cd01162 77 VSTAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVR-----EGDHYV---LNGS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 280 KRYITLGPVATLLGLAFKAydpdhllGEQEDLGISLALVPTDTPGVEIGRRHLPLGaaFMNGPNSG---KDVFIPLNYLI 356
Cdd:cd01162 149 KAFISGAGDSDVYVVMART-------GGEGPKGISCFVVEKGTPGLSFGANEKKMG--WNAQPTRAvifEDCRVPVENRL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 357 GGQdmlGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGgnTWLMDSARIL 436
Cdd:cd01162 220 GGE---GQGFGIAMAGLNGGR-LNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMA--TELVASRLMV 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1222445847 437 TAGAVDLGEK---PSVLSAILKYHLTERGRECVSHAMDVHGGKG 477
Cdd:cd01162 294 RRAASALDRGdpdAVKLCAMAKRFATDECFDVANQALQLHGGYG 337
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
137-477 |
4.31e-24 |
|
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: 104.89 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 137 EELCAMVSDWQIGQQLdlPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLAtRSGDLASTVMVPNSLGpAELL 216
Cdd:cd01160 16 KEVAPFHHEWEKAGEV--PREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELA-RAGGSGPGLSLHTDIV-SPYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 217 LHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAgampdSGIVCKGQWQGEEVLglrLTWEKRYITLGPVATLLGLAF 296
Cdd:cd01160 92 TRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDL-----QGIRTTARKDGDHYV---LNGSKTFITNGMLADVVIVVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 297 KAYDPDHLLGeqedlGISLALVPTDTPGVEIGRRHLPLG-------AAFMNgpnsgkDVFIPLNYLIGGQdmlGKGWMML 369
Cdd:cd01160 164 RTGGEARGAG-----GISLFLVERGTPGFSRGRKLKKMGwkaqdtaELFFD------DCRVPAENLLGEE---NKGFYYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 370 MNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIG-----GNTWLMDSARILTAgavdlG 444
Cdd:cd01160 230 MQNLPQER-LLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELAtkvavTRAFLDNCAWRHEQ-----G 303
|
330 340 350
....*....|....*....|....*....|...
gi 1222445847 445 EKPSVLSAILKYHLTERGRECVSHAMDVHGGKG 477
Cdd:cd01160 304 RLDVAEASMAKYWATELQNRVAYECVQLHGGWG 336
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
147-421 |
2.83e-22 |
|
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: 99.79 E-value: 2.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 147 QIGQQLDLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGDLA------STVMVPNslgpaelLLHYG 220
Cdd:cd01156 27 KIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVAlsygahSNLCINQ-------IYRNG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 221 TDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAMPdsgivCKGQWQGEEVLglrLTWEKRYITLGPVATLLgLAFKAYD 300
Cdd:cd01156 100 SAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMK-----LRAEKKGDRYV---LNGSKMWITNGPDADTL-VVYAKTD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 301 PDhllgeQEDLGISLALVPTDTPGVEIGRRHLPLGaafMNGPNSGK----DVFIPLNYLIGGqdmLGKGWMMLMNCLSVG 376
Cdd:cd01156 171 PS-----AGAHGITAFIVEKGMPGFSRAQKLDKLG---MRGSNTCElvfeDCEVPEENILGG---ENKGVYVLMSGLDYE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1222445847 377 RSIsLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALA 421
Cdd:cd01156 240 RLV-LAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLA 283
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
125-236 |
3.23e-19 |
|
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: 83.67 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 125 SEEEQAFLDGP----TEELCAMVSDWQigQQLDLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGDL 200
Cdd:pfam02771 1 TEEQEALRDTVrefaEEEIAPHAAEWD--EEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1222445847 201 ASTVMVPNSLGpAELLLHYGTDEQRQHYLPRLARGD 236
Cdd:pfam02771 79 ALALSVHSSLG-APPILRFGTEEQKERYLPKLASGE 113
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
159-477 |
1.26e-18 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 88.80 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 159 WQHIKQHGFFALI---IPREYGGKGFSAYAHSQVAMKLATRSGDLASTVMVpNSLGPAELLLHyGTDEQRQHYLPRLARG 235
Cdd:cd01157 35 WPLIKRAWELGLMnthIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEA-NSLGQMPVIIS-GNDEQKKKYLGRMTEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 236 DDIPCFALTGPLAGSDAgampdSGIVCKGQWQGEEVLglrLTWEKRYITLGPVATLLGLAFKAyDPDHLLGEQEdlGISL 315
Cdd:cd01157 113 PLMCAYCVTEPGAGSDV-----AGIKTKAEKKGDEYI---INGQKMWITNGGKANWYFLLARS-DPDPKCPASK--AFTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 316 ALVPTDTPGVEIGRRHLPLGAAFMNGPN-SGKDVFIPLNYLIGGQdmlGKGWMMLMNCLSVGRSiSLPAGATGSAKFSSL 394
Cdd:cd01157 182 FIVEADTPGIQPGRKELNMGQRCSDTRGiTFEDVRVPKENVLIGE---GAGFKIAMGAFDKTRP-PVAAGAVGLAQRALD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 395 VSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSARILTAGAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHG 474
Cdd:cd01157 258 EATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFG 337
|
...
gi 1222445847 475 GKG 477
Cdd:cd01157 338 GNG 340
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
176-479 |
3.85e-16 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 81.44 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 176 YGGKGFSAYAHSQVAMKLATRSGDLASTVMVPNSLGPAELLLhYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAM 255
Cdd:PLN02526 82 YGCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 256 PDSGIVCKGQWQgeevlglrLTWEKRYITLGPVATLLGLAFKAYDPDHLLGeqedlgislALVPTDTPGVEIGRRHLPLG 335
Cdd:PLN02526 161 NTTATKVEGGWI--------LNGQKRWIGNSTFADVLVIFARNTTTNQING---------FIVKKGAPGLKATKIENKIG 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 336 AAFM-NGPNSGKDVFIPLNYLIGG----QDmlgkgwmmLMNCLSVGR------SISLPAGATGsakfsslVSGQYCQIRE 404
Cdd:PLN02526 224 LRMVqNGDIVLKDVFVPDEDRLPGvnsfQD--------TNKVLAVSRvmvawqPIGISMGVYD-------MCHRYLKERK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 405 QFNVPLAAFEGIQEALARIGGNT-------W----LMDSARIlTAGAVDLGekpsvlsailKYHLTERGRECVSHAMDVH 473
Cdd:PLN02526 289 QFGAPLAAFQINQEKLVRMLGNIqamflvgWrlckLYESGKM-TPGHASLG----------KAWITKKARETVALGRELL 357
|
....*.
gi 1222445847 474 GGKGII 479
Cdd:PLN02526 358 GGNGIL 363
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
156-477 |
5.79e-14 |
|
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: 74.73 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 156 AKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAmKLATRSgdlASTVMVPNSLGP-AELLLHYGTDEQRQHYLPRLAR 234
Cdd:cd01153 39 KEALDAFAEAGWMALGVPEEYGGQGLPITVYSALA-EIFSRG---DAPLMYASGTQGaAATLLAHGTEAQREKWIPRLAE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 235 GDDIPCFALTGPLAGSDAG-----AMPDSGivckGQWqgeevlglRLTWEKRYITLGPVATLLGLAfkaydpdHL-LGEQ 308
Cdd:cd01153 115 GEWTGTMCLTEPDAGSDLGalrtkAVYQAD----GSW--------RINGVKRFISAGEHDMSENIV-------HLvLARS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 309 EDL-----GISLALVP-----TDTPGVEIGRRHLPLGaafMNGPNSGKDVFIPLNYLIGGQDMLGKGWMM-LMNclsvGR 377
Cdd:cd01153 176 EGAppgvkGLSLFLVPkflddGERNGVTVARIEEKMG---LHGSPTCELVFDNAKGELIGEEGMGLAQMFaMMN----GA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 378 SISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLMDSAR--------ILTAGAVDLGEKPSV 449
Cdd:cd01153 249 RLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYaegsraldLYTATVQDLAERKAT 328
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1222445847 450 --------------LSAILKYHLTERGRECVSHAMDVHGGKG 477
Cdd:cd01153 329 egedrkalsaladlLTPVVKGFGSEAALEAVSDAIQVHGGSG 370
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
159-485 |
5.95e-14 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 74.53 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 159 WQHIKQHGFFALIIPREYGGKGFsAYAHSQVAMKLATR-SGDLASTVMVPNSLGPAELLLHyGTDEQRQHYLPRLARGDD 237
Cdd:PLN02519 65 WKLMGDFNLHGITAPEEYGGLGL-GYLYHCIAMEEISRaSGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLPKLISGEH 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 238 IPCFALTGPLAGSDAGAMPdsgivCKGQWQGEevlGLRLTWEKRYITLGPVATLLGLAFKAydpDHLLGEQedlGISLAL 317
Cdd:PLN02519 143 VGALAMSEPNSGSDVVSMK-----CKAERVDG---GYVLNGNKMWCTNGPVAQTLVVYAKT---DVAAGSK---GITAFI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 318 VPTDTPGVEIGRRHLPLGaafMNGPNSGKDVF----IPLNYLIGGQdmlGKGWMMLMNCLSVGRSIsLPAGATGSAKFSS 393
Cdd:PLN02519 209 IEKGMPGFSTAQKLDKLG---MRGSDTCELVFencfVPEENVLGQE---GKGVYVMMSGLDLERLV-LAAGPLGLMQACL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 394 LVSGQYCQIREQFNVPLAAFEGIQEALARI-----GGNTWLMDSARILTAGAVDlgeKPSVLSAILkyHLTERGRECVSH 468
Cdd:PLN02519 282 DVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDNGKVD---RKDCAGVIL--CAAERATQVALQ 356
|
330
....*....|....*..
gi 1222445847 469 AMDVHGGKGIImgpNNY 485
Cdd:PLN02519 357 AIQCLGGNGYI---NEY 370
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
240-335 |
6.12e-13 |
|
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: 65.38 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 240 CFALTGPLAGSDAGAMPDSGIVCKGqwqgeevLGLRLTWEKRYITLGPVATLLGLAFKAYDPDHllgeqeDLGISLALVP 319
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDG-------GGWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
|
90
....*....|....*.
gi 1222445847 320 TDTPGVEIGRRHLPLG 335
Cdd:pfam02770 68 KDAPGVSVRRIETKLG 83
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
363-503 |
9.02e-13 |
|
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: 66.51 E-value: 9.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 363 GKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTwlmDSARILT---AG 439
Cdd:pfam00441 1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEI---EAARLLVyraAE 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222445847 440 AVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGIImgPNNYLARAWQGAPIAITVEGAN 503
Cdd:pfam00441 77 ALDAGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYL--REYPVERLYRDARVLRIGEGTS 138
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
126-491 |
1.20e-12 |
|
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: 70.45 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 126 EEEQAFLDGPTEELCAMV-SDWQIGQQLDLP-----AKAWQHI-KQHGFFALIIPREYGGKGFSAYAHSQVAMKLAtRSG 198
Cdd:cd01152 1 PSEEAFRAEVRAWLAAHLpPELREESALGYRegredRRRWQRAlAAAGWAAPGWPKEYGGRGASLMEQLIFREEMA-AAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 199 DLASTVMV-PNSLGPAelLLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAMPDSGIVCKGQWQgeevlglrLT 277
Cdd:cd01152 80 APVPFNQIgIDLAGPT--ILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWV--------VN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 278 WEKRYITLGPVATLLGLAFKAyDPDhllgEQEDLGISLALVPTDTPGVEIGRRHLPLGAAFMNgPNSGKDVFIPLNYLIG 357
Cdd:cd01152 150 GQKIWTSGAHYADWAWLLVRT-DPE----APKHRGISILLVDMDSPGVTVRPIRSINGGEFFN-EVFLDDVRVPDANRVG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 358 GQdmlGKGWMMLMNCLSVGRsisLPAGATGSAKFSSLVsgQYCQIREQFNVPLAAFEGIQEALARIGGNtwlMDSARIL- 436
Cdd:cd01152 224 EV---NDGWKVAMTTLNFER---VSIGGSAATFFELLL--ARLLLLTRDGRPLIDDPLVRQRLARLEAE---AEALRLLv 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1222445847 437 --TAGAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGIIMGPNN--YLARAWQ 491
Cdd:cd01152 293 frLASALAAGKPPGAEASIAKLFGSELAQELAELALELLGTAALLRDPAPgaELAGRWE 351
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
124-505 |
1.83e-12 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 69.76 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 124 LSEEEQAFLDGPTEELC-----AMVSDWQigQQLDLPAKAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLAtRSG 198
Cdd:PRK12341 5 LTEEQELLLASIRELITrnfpeEYFRTCD--ENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVS-KCG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 199 dlASTVMVPNSLGPAELLlHYGTDEQ-RQHYLPRLARGDDIPCFALTGPLAGSDAGAMPDSGIVCKGQwqgeevlgLRLT 277
Cdd:PRK12341 82 --APAFLITNGQCIHSMR-RFGSAEQlRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGK--------VYLN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 278 WEKRYITLGPVAT-LLGLAFKAYDPDhllgeqEDLGISLALVPTDTPGV------EIGRRHLPLGAAFMNgpnsgkDVFI 350
Cdd:PRK12341 151 GQKTFITGAKEYPyMLVLARDPQPKD------PKKAFTLWWVDSSKPGIkinplhKIGWHMLSTCEVYLD------NVEV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 351 PLNYLIGGQdmlGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARIGGNTWLM 430
Cdd:PRK12341 219 EESDLVGEE---GMGFLNVMYNFEMER-LINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 431 DSARILTAGAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGIImgPNNYLARAWQGA----------PIAITVE 500
Cdd:PRK12341 295 RNMVYKVAWQADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYT--DEARVSRFWRDVrcerigggtdEIMIYIA 372
|
....*
gi 1222445847 501 GANIL 505
Cdd:PRK12341 373 GRQIL 377
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
141-493 |
4.12e-10 |
|
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: 62.41 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 141 AMVSDWQIGQQL-DLPAKAwqhiKQHGFFALIIPREYGGKGFS--AYAHsqvamkLATRSGD--LASTVM---VPNSlGP 212
Cdd:cd01155 32 GGDRWWTPPPIIeKLKAKA----KAEGLWNLFLPEVSGLSGLTnlEYAY------LAEETGRsfFAPEVFncqAPDT-GN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 213 AELLLHYGTDEQRQHYLPRLARGDDIPCFALTGP-LAGSDAgampdSGIVCKGQWQGEE-VLGLRLTWE--------KRY 282
Cdd:cd01155 101 MEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPdVASSDA-----TNIECSIERDGDDyVINGRKWWSsgagdprcKIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 283 ITLGPVatllglafkayDPDhllGEQEDLGISLALVPTDTPGVEIGRrhlPLGA-AFMNGPN-----SGKDVFIPLNYLI 356
Cdd:cd01155 176 IVMGRT-----------DPD---GAPRHRQQSMILVPMDTPGVTIIR---PLSVfGYDDAPHghaeiTFDNVRVPASNLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 357 GGQdmlGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALA--RIGgntwlMDSAR 434
Cdd:cd01155 239 LGE---GRGFEIAQGRLGPGR-IHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIE-----IEQAR 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222445847 435 ILTAGAVDL-------GEKPSVlsAILKYHLTERGRECVSHAMDVHGGKGIimGPNNYLARAWQGA 493
Cdd:cd01155 310 LLVLKAAHMidtvgnkAARKEI--AMIKVAAPRMALKIIDRAIQVHGAAGV--SQDTPLANMYAWA 371
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
166-477 |
1.15e-08 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 58.03 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 166 GFFALIIPREYGGKGFSAYAHSQVAMKLATRS-----GDLASTVMVPNSLgpaellLHYGTDEQRQHYLPRLARGDDIPC 240
Cdd:PTZ00461 81 GVMGVTVPEADGGAGMDAVAAVIIHHELSKYDpgfclAYLAHSMLFVNNF------YYSASPAQRARWLPKVLTGEHVGA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 241 FALTGPLAGSDAGAMPDSGivcKGQWQGEEVLGLRLTWekryITLGPVATLLglafkaydpdhLLGEQEDLGISLALVPT 320
Cdd:PTZ00461 155 MGMSEPGAGTDVLGMRTTA---KKDSNGNYVLNGSKIW----ITNGTVADVF-----------LIYAKVDGKITAFVVER 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 321 DTPGVEIGRRHLPLGaafMNGPNSGK----DVFIPLNYLIGGQdmlGKGWMMLMNCLSVGRsISLPAGATGSAKFSSLVS 396
Cdd:PTZ00461 217 GTKGFTQGPKIDKCG---MRASHMCQlffeDVVVPAENLLGEE---GKGMVGMMRNLELER-VTLAAMAVGIAERSVELM 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 397 GQYCQIREQFNVPLAAFEGIQEALARIGGNTwlmDSARILT---AGAVDLGEKPSVLSAILKYHLTERGRECVSHAMDVH 473
Cdd:PTZ00461 290 TSYASERKAFGKPISNFGQIQRYIAEGYADT---EAAKALVysvSHNVHPGNKNRLGSDAAKLFATPIAKKVADSAIQVM 366
|
....
gi 1222445847 474 GGKG 477
Cdd:PTZ00461 367 GGMG 370
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
137-481 |
2.53e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 54.10 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 137 EELCAMVSDWQIGQQLDLPAkAWQHIKQHGFFALIIPREYGGKGFSAYAHSQVAMKLATRSGDLAstvMVPN-SLGPAEL 215
Cdd:PTZ00456 84 SEGCVLLKDGNVTTPKGFKE-AYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFS---MYPGlSIGAANT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 216 LLHYGTDEQRQHYLPRLARGDDIPCFALTGPLAGSDAGAMPDSGIVCK-GQWqgeevlglRLTWEKRYITLGP---VATL 291
Cdd:PTZ00456 160 LMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSAdGSY--------KITGTKIFISAGDhdlTENI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 292 LGLAFkAYDPDHLLGEQedlGISLALVPTDTP----------GVEIGRRHLPLG-----AAFMNGPNSgkdvfipLNYLI 356
Cdd:PTZ00456 232 VHIVL-ARLPNSLPTTK---GLSLFLVPRHVVkpdgsletakNVKCIGLEKKMGikgssTCQLSFENS-------VGYLI 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 357 GGQDMLGKGWMMLMNCLSVGRSISlpagATGSAKFSSLVSGQYCQIREQfnvpLAAFEGIQE------------------ 418
Cdd:PTZ00456 301 GEPNAGMKQMFTFMNTARVGTALE----GVCHAELAFQNALRYARERRS----MRALSGTKEpekpadriichanvrqni 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222445847 419 ----ALARiGGNTWLMDSARIL-------TAGAVD-LGEKPSVLSAILKYHLTERGRECVSHAMDVHGGKGIIMG 481
Cdd:PTZ00456 373 lfakAVAE-GGRALLLDVGRLLdihaaakDAATREaLDHEIGFYTPIAKGCLTEWGVEAASRCLQVWGGHGYIKG 446
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
312-506 |
4.76e-03 |
|
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: 40.05 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 312 GISLALVPTDTP-----GVEIGRRHLPLGAAFMNgpnSGKDVFI-PLNYLIGGQdmlGKGWMMLMNCLSVGRsISLPAGA 385
Cdd:cd01154 209 GLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVA---TGEVEFDdAEAYLIGDE---GKGIYYILEMLNISR-LDNAVAA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 386 TGSAKFSSLVSGQYCQIREQFNVPLAAFEGIQEALARI-----GGNTWLMDSARILTAGAVDLGEK---PSVLSAILKYH 457
Cdd:cd01154 282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMevdveAATALTFRAARAFDRAAADKPVEahmARLATPVAKLI 361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1222445847 458 LTERGRECVSHAMDVHGGKGIImgPNNYLARAWQGAPIAITVEG-ANILS 506
Cdd:cd01154 362 ACKRAAPVTSEAMEVFGGNGYL--EEWPVARLHREAQVTPIWEGtGNIQA 409
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
211-377 |
8.61e-03 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 39.78 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 211 GPAELLLHYGTDEQRQHYLPRLARGDDIPCFALTGP-LAGSDAgampdSGIVCKGQWQGEE-VLGLRLTWEKRyiTLGPV 288
Cdd:PLN02876 524 GNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPqVASSDA-----TNIECSIRRQGDSyVINGTKWWTSG--AMDPR 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222445847 289 ATLLGLAFKAyDPDHLLGEQEdlgiSLALVPTDTPGVEIGRRHLPLGaaFMNGPN-----SGKDVFIPLNYLIGGQdmlG 363
Cdd:PLN02876 597 CRVLIVMGKT-DFNAPKHKQQ----SMILVDIQTPGVQIKRPLLVFG--FDDAPHghaeiSFENVRVPAKNILLGE---G 666
|
170
....*....|....
gi 1222445847 364 KGWMMLMNCLSVGR 377
Cdd:PLN02876 667 RGFEIAQGRLGPGR 680
|
|
| |
