|
Name |
Accession |
Description |
Interval |
E-value |
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
4-805 |
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: 1694.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 4 LLSLLAMTLILGVTLYHRMSLVKSVTLLTATMLLLTFSGYVGSIGWLSYFLALAVFAMPSVRQSLISAKALGLFKQVLPA 83
Cdd:NF038187 1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 84 MSQTEKEALDAGTVWWEAELFKGKPEWKKLHAIPAPKLSAEEQAFLDGPVNEVCAMVSDYQVTHELADLPPEVWQYLKDH 163
Cdd:NF038187 81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 164 KFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTVGVPNSLGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTS 243
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 244 PEAGSDAGSIPDDGVVCKGEWEGKEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPEGLLGEQEDLGITCALIPTDIKGV 323
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 324 EIGNRHFPLNVPFQNGPTRGQNIFVPIDFIIGGQKMAGQGWRMLVECLSVGRGITLPSNSTGGIKSAALATGAYSRIRRQ 403
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 404 FKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGPSNF 483
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 484 LARGYQGSPIAVTVEGANILTRSMIIYGQGAIRCHPYVLKEMEAAYS-DKSDAVEQFDAALAGHVSFTMSNLVRSIWFGL 562
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDnDSEQALNDFDKALFGHIGFVGSNLVRSFWLGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 563 TDGFGSNAPTHDATKRYYQKLNRYSANMALLSDISMAVLGGSLKRRERLSARLGDILSQLYLSSATLKRFEQDGRPVEDL 642
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 643 PLVHWGLQDSLKQTEVAIDEFLANFPNPIIGKALRVLIMPFGRVRKAPSDKIDSQVARILQTPSATRSRIGRNQYLQPTE 722
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 723 HNAAGKIELALSVILQAEPVFDKVCKAQGKRRPFLRLDAIAEEGLAQGIISQDEADLLKEAEQHRLYTINVDDFEPEHLA 802
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
|
...
gi 516400656 803 AKK 805
Cdd:NF038187 801 AKP 803
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
43-807 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1528.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 43 YVGSIGWLSYFLALAVFAMPSVRQSLISAKALGLFKQVLPAMSQTEKEALDAGTVWWEAELFKGKPEWKKLHAIPAPKLS 122
Cdd:PRK09463 1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 123 AEEQAFLDGPVNEVCAMVSDYQVTHELADLPPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTV 202
Cdd:PRK09463 81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 203 GVPNSLGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSIPDDGVVCKGEWEGKEVLGMRLTWNKRYIT 282
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 283 LAPVATVLGLAFKLRDPEGLLGEQEDLGITCALIPTDIKGVEIGNRHFPLNVPFQNGPTRGQNIFVPIDFIIGGQKMAGQ 362
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 363 GWRMLVECLSVGRGITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAGIDLG 442
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 443 EKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGPSNFLARGYQGSPIAVTVEGANILTRSMIIYGQGAIRCHPYVL 522
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 523 KEMEAAYSDKSDAVEQFDAALAGHVSFTMSNLVRSIWFGLTDGFGSNAPTHDATKRYYQKLNRYSANMALLSDISMAVLG 602
Cdd:PRK09463 481 KEMEAAQNNDKQALKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 603 GSLKRRERLSARLGDILSQLYLSSATLKRFEQDGRPVEDLPLVHWGLQDSLKQTEVAIDEFLANFPNPIIGKALRVLIMP 682
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 683 FGRVRKAPSDKIDSQVARILQTPSATRSRIGRNQYLQPTEHNAAGKIELALSVILQAEPVFDKVCKAQGKRR-PFLRLDA 761
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGKlPFLRLDE 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 516400656 762 IAEEGLAQGIISQDEADLLKEAEQHRLYTINVDDFEPEHLAAKKSH 807
Cdd:PRK09463 721 LADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVK 766
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
515-796 |
1.15e-157 |
|
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: 460.42 E-value: 1.15e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 515 IRCHPYVLKEMEAAYS-DKSDAVEQFDAALAGHVSFTMSNLVRSIWFGLTDGFGSNAPTHDATKRYYQKLNRYSANMALL 593
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNeDKEQALKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 594 SDISMAVLGGSLKRRERLSARLGDILSQLYLSSATLKRFEQDGRPVEDLPLVHWGLQDSLKQTEVAIDEFLANFPNPIIG 673
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 674 KALRVLIMPFGRVRKAPSDKIDSQVARILQTPSATRSRIGRNQYLQPTEHNAAGKIELALSVILQAEPVFDKVCKAQGKR 753
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 516400656 754 R-PFLRLDAIAEEGLAQGIISQDEADLLKEAEQHRLYTINVDDF 796
Cdd:pfam09317 241 KlPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
121-509 |
1.01e-84 |
|
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: 274.80 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 121 LSAEEQAFLDgPVNEVCA-MVSDYQVTHELA-DLPPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVL 198
Cdd:COG1960 5 LTEEQRALRD-EVREFAEeEIAPEAREWDREgEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 199 SSTVGVPNslGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSIPddgvvCKGEWEGKevlGMRLTWNK 278
Cdd:COG1960 84 ALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALR-----TTAVRDGD---GYVLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 279 RYITLAPVATVLGLAFKLRDPEGllgeqeDLGITCALIPTDIKGVEIGNRHFPLNV-PFQNGPTRGQNIFVPIDFIIGGq 357
Cdd:COG1960 154 TFITNAPVADVILVLARTDPAAG------HRGISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 358 kmAGQGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVA 437
Cdd:COG1960 227 --EGKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAW 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516400656 438 GIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGpsNFLARGYQGSPIAVTVEGANILTRSMII 509
Cdd:COG1960 304 LLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTRE--YPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
208-501 |
9.26e-35 |
|
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: 135.49 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 208 LGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSI-----PDDgvvckGEWegkevlgmRLTWNKRYIT 282
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIrttarKDG-----DGY--------VLNGRKIFIS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 283 LAPVATVLGLAFKLrDPEGLLGEqedlGITCALIPTDIKGVEIGNrhfPLNVPFQNG-PTRG---QNIFVPIDFIIGGqk 358
Cdd:cd00567 109 NGGDADLFIVLART-DEEGPGHR----GISAFLVPADTPGVTVGR---IWDKMGMRGsGTGElvfDDVRVPEDNLLGE-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 359 mAGQGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAG 438
Cdd:cd00567 179 -EGGGFELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWL 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516400656 439 IDLGE-KPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGicLGPSNFLARGYQGSPIAVTVEGAN 501
Cdd:cd00567 257 LDQGPdEARLEAAMAKLFATEAAREVADLAMQIHGGRG--YSREYPVERYLRDARAARIAEGTA 318
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FadE_coli |
NF038187 |
acyl-CoA dehydrogenase FadE; This HMM describes a narrow clade of medium-chain and long-chain ... |
4-805 |
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: 1694.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 4 LLSLLAMTLILGVTLYHRMSLVKSVTLLTATMLLLTFSGYVGSIGWLSYFLALAVFAMPSVRQSLISAKALGLFKQVLPA 83
Cdd:NF038187 1 LLSILAMLVLLGALAYHRVSLLTSSLILAAVMAAGTAAGLWSLWLWLPFLIIALPLNVPSIRQSLISAPALKAFRKVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 84 MSQTEKEALDAGTVWWEAELFKGKPEWKKLHAIPAPKLSAEEQAFLDGPVNEVCAMVSDYQVTHELADLPPEVWQYLKDH 163
Cdd:NF038187 81 MSSTEKEAIDAGTTWWEADLFRGNPDWKKLHNYPKPRLTAEEQAFLDGPVEEVCRMVNDFQITHELADLPPEVWQYLKDH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 164 KFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTVGVPNSLGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTS 243
Cdd:NF038187 161 RFFAMIIKKEYGGLEFSAYAQSRVLQKLAGVSSILASTVGVPNSLGPGELLQHYGTEEQKDHYLPRLARGEEIPCFALTS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 244 PEAGSDAGSIPDDGVVCKGEWEGKEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPEGLLGEQEDLGITCALIPTDIKGV 323
Cdd:NF038187 241 PEAGSDAGSIPDFGVVCKGEWQGEEVLGMRLTWNKRYITLAPVATVLGLAFKLRDPDHLLGDKEELGITCALIPTDTPGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 324 EIGNRHFPLNVPFQNGPTRGQNIFVPIDFIIGGQKMAGQGWRMLVECLSVGRGITLPSNSTGGIKSAALATGAYSRIRRQ 403
Cdd:NF038187 321 EIGRRHFPLNVPFQNGPTRGKDIFVPLDFIIGGPKMAGQGWRMLVECLSVGRGITLPSNSTGGLKSAALATGAYARIRRQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 404 FKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGPSNF 483
Cdd:NF038187 401 FKLPIGKMEGIEEPLARIAGNAYLMDAAATLTTTGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIHGGKGICLGPNNF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 484 LARGYQGSPIAVTVEGANILTRSMIIYGQGAIRCHPYVLKEMEAAYS-DKSDAVEQFDAALAGHVSFTMSNLVRSIWFGL 562
Cdd:NF038187 481 LARGYQGAPIAITVEGANILTRSMIIYGQGAIRCHPYVLAEMEAAQDnDSEQALNDFDKALFGHIGFVGSNLVRSFWLGL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 563 TDGFGSNAPTHDATKRYYQKLNRYSANMALLSDISMAVLGGSLKRRERLSARLGDILSQLYLSSATLKRFEQDGRPVEDL 642
Cdd:NF038187 561 TNGRFSSAPYKDATRRYYQQLNRLSANLALLSDVSMAVLGGSLKRRERISARLGDILSQLYLASATLKRYEDEGRQKEDL 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 643 PLVHWGLQDSLKQTEVAIDEFLANFPNPIIGKALRVLIMPFGRVRKAPSDKIDSQVARILQTPSATRSRIGRNQYLQPTE 722
Cdd:NF038187 641 PLVHWAVQDSLYQAEQALDDLLRNFPNRLVAGLLRVIIFPFGRPLKAPSDKLDHKVAKILQTPSATRSRLGRGQYLTPSE 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 723 HNAAGKIELALSVILQAEPVFDKVCKAQGKRRPFLRLDAIAEEGLAQGIISQDEADLLKEAEQHRLYTINVDDFEPEHLA 802
Cdd:NF038187 721 HNPVGLLEQALKDILAAEPIHDRVCKAAGKRLPFMRLDKLAEEGLALGVITEEEAALLERAEASRLRSINVDDFDPDELA 800
|
...
gi 516400656 803 AKK 805
Cdd:NF038187 801 AKP 803
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
43-807 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 1528.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 43 YVGSIGWLSYFLALAVFAMPSVRQSLISAKALGLFKQVLPAMSQTEKEALDAGTVWWEAELFKGKPEWKKLHAIPAPKLS 122
Cdd:PRK09463 1 LWSLWLLVPLAIILLPLNLPPLRRSLISAPLLKWFRKVLPPMSQTEREALEAGTVWWEGELFSGKPDWKKLLNYPKPTLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 123 AEEQAFLDGPVNEVCAMVSDYQVTHELADLPPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTV 202
Cdd:PRK09463 81 AEEQAFLDGPVEELCRMVNDWQITHELADLPPEVWQFIKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 203 GVPNSLGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSIPDDGVVCKGEWEGKEVLGMRLTWNKRYIT 282
Cdd:PRK09463 161 MVPNSLGPGELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSIPDTGVVCKGEWQGEEVLGMRLTWNKRYIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 283 LAPVATVLGLAFKLRDPEGLLGEQEDLGITCALIPTDIKGVEIGNRHFPLNVPFQNGPTRGQNIFVPIDFIIGGQKMAGQ 362
Cdd:PRK09463 241 LAPIATVLGLAFKLYDPDGLLGDKEDLGITCALIPTDTPGVEIGRRHFPLNVPFQNGPTRGKDVFIPLDYIIGGPKMAGQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 363 GWRMLVECLSVGRGITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAGIDLG 442
Cdd:PRK09463 321 GWRMLMECLSVGRGISLPSNSTGGAKLAALATGAYARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 443 EKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGPSNFLARGYQGSPIAVTVEGANILTRSMIIYGQGAIRCHPYVL 522
Cdd:PRK09463 401 EKPSVLSAIAKYHLTERGRQVINDAMDIHGGKGICLGPNNFLARAYQAAPIAITVEGANILTRSLMIFGQGAIRCHPYVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 523 KEMEAAYSDKSDAVEQFDAALAGHVSFTMSNLVRSIWFGLTDGFGSNAPTHDATKRYYQKLNRYSANMALLSDISMAVLG 602
Cdd:PRK09463 481 KEMEAAQNNDKQALKAFDKALFGHIGFVVSNAVRSFWLGLTGGRLSAAPVDDATKRYYRQLNRLSANLALLADVSMLVLG 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 603 GSLKRRERLSARLGDILSQLYLSSATLKRFEQDGRPVEDLPLVHWGLQDSLKQTEVAIDEFLANFPNPIIGKALRVLIMP 682
Cdd:PRK09463 561 GSLKRRERLSARLGDILSQLYLASAVLKRYEDEGRPEADLPLVHWAVQDALYQAEQALDGLLRNFPNRVVAGLLRVLVFP 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 683 FGRVRKAPSDKIDSQVARILQTPSATRSRIGRNQYLQPTEHNAAGKIELALSVILQAEPVFDKVCKAQGKRR-PFLRLDA 761
Cdd:PRK09463 641 LGRRYRAPSDKLDHQVAKLLQTPSATRDRLTRGQYLPPSENNPVGRLEEALLDVIAAEPIEKKICKALKKGKlPFLRLDE 720
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 516400656 762 IAEEGLAQGIISQDEADLLKEAEQHRLYTINVDDFEPEHLAAKKSH 807
Cdd:PRK09463 721 LADEALAAGVISEEEAALLREAEEARLRVINVDDFDPEELAAKPVK 766
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
45-798 |
0e+00 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 1183.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 45 GSIGWLSYFLALAVFAMPSVRQSLISAKALGLFKQVLPAMSQTEKEALDAGTVWWEAELFKGKPEWKKLHAIPAPKLSAE 124
Cdd:PRK13026 2 MTLIILLLIAIVLVFAVKPLRRQFITRPVFKFFKKVLPPLSDTEREAMEAGDVWWEGELFSGKPDWQKLHSYPKPTLTAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 125 EQAFLDGPVNEVCAMVSDYQVTHELADLPPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTVGV 204
Cdd:PRK13026 82 EQAFIDNEVETLLTMLDDWDIVQNRKDLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 205 PNSLGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSIPDDGVVCKGEWEGKEVLGMRLTWNKRYITLA 284
Cdd:PRK13026 162 PNSLGPGELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRGEFEGEEVLGLRLTWDKRYITLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 285 PVATVLGLAFKLRDPEGLLGEQEDLGITCALIPTDIKGVEIGNRHFPLNVPFQNGPTRGQNIFVPIDFIIGGQKMAGQGW 364
Cdd:PRK13026 242 PVATVLGLAFKLRDPDGLLGDKKELGITCALIPTDHPGVEIGRRHNPLGMAFMNGTTRGKDVFIPLDWIIGGPDYAGRGW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 365 RMLVECLSVGRGITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAGIDLGEK 444
Cdd:PRK13026 322 RMLVECLSAGRGISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 445 PSVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGPSNFLARGYQGSPIAVTVEGANILTRSMIIYGQGAIRCHPYVLKE 524
Cdd:PRK13026 402 PSVVTAIAKYHMTELARDVVNDAMDIHAGKGIQLGPKNYLGHAYMAVPIAITVEGANILTRNLMIFGQGATRCHPYVLAE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 525 MEAA-YSDKSDAVEQFDAALAGHVSFTMSNLVRSIWFGLTDGFGSNAPTHDATKRYYQKLNRYSANMALLSDISMAVLGG 603
Cdd:PRK13026 482 MEAAaMEDEHEGLEAFDSLLFKHIGYAARNAFRALFSALTGSRFISAPVSGETAQYYKDMSRLSAALALLADLSMLILGG 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 604 SLKRRERLSARLGDILSQLYLSSATLKRFEQDGRPVEDLPLVHWGLQDSLKQTEVAIDEFLANFPNPIIGKALRVLIMPF 683
Cdd:PRK13026 562 DLKRKEMLSARLGDVLSQLYLASATLKRFEDNGRQQDDLPAVHYAMQDCLHLAAKALDEFLRNFPNRPVAWLLRALIFPL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 684 GRVRKAPSDKIDSQVARILQTPSATRSRIGRNQYLQPTEHNAAGKIELALSVILQAEPVFDKVCKAQ--GKRRPFLRLDA 761
Cdd:PRK13026 642 GNHFRAPSDKLARQLAELMMTPGPARDRLTALCYIFEGDKDGVARVEQAFLAQYAVKPLYKKLKKAQreGKLPRKVPLLE 721
|
730 740 750
....*....|....*....|....*....|....*..
gi 516400656 762 IAEEGLAQGIISQDEADLLKEAEQHRLYTINVDDFEP 798
Cdd:PRK13026 722 LFAKALEKGVITADEAEKLLAADKLRLDAIQVDDFTP 758
|
|
| ACDH_C |
pfam09317 |
Acyl-CoA dehydrogenase, C-terminal, bacterial type; This C-terminal domain is functionally ... |
515-796 |
1.15e-157 |
|
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: 460.42 E-value: 1.15e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 515 IRCHPYVLKEMEAAYS-DKSDAVEQFDAALAGHVSFTMSNLVRSIWFGLTDGFGSNAPTHDATKRYYQKLNRYSANMALL 593
Cdd:pfam09317 1 IRCHPYVLKEMEAAQNeDKEQALKAFDRALFGHIGFALSNAARSLVLGLTGGRFASAPVAGETARYYRQLNRLSAAFALL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 594 SDISMAVLGGSLKRRERLSARLGDILSQLYLSSATLKRFEQDGRPVEDLPLVHWGLQDSLKQTEVAIDEFLANFPNPIIG 673
Cdd:pfam09317 81 ADLAMLVLGGSLKRRERLSARLGDVLSQLYLASAVLKRFEDEGRPEADLPLVHWAMQDALYQAQQALDGVLRNFPNRPVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 674 KALRVLIMPFGRVRKAPSDKIDSQVARILQTPSATRSRIGRNQYLQPTEHNAAGKIELALSVILQAEPVFDKVCKAQGKR 753
Cdd:pfam09317 161 WLLRVLVFPLGRRYRKPSDKLGHEVAQLLQEPGEARDRLTAGVYLPDDPDDPVGRLEAAFQAVLAAEPLEKKLKKAIKAG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 516400656 754 R-PFLRLDAIAEEGLAQGIISQDEADLLKEAEQHRLYTINVDDF 796
Cdd:pfam09317 241 KlPKLTLEELIEEALEKGVITEEEAELLREAEALRLDVIQVDDF 284
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
121-509 |
1.01e-84 |
|
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: 274.80 E-value: 1.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 121 LSAEEQAFLDgPVNEVCA-MVSDYQVTHELA-DLPPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVL 198
Cdd:COG1960 5 LTEEQRALRD-EVREFAEeEIAPEAREWDREgEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 199 SSTVGVPNslGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSIPddgvvCKGEWEGKevlGMRLTWNK 278
Cdd:COG1960 84 ALPVGVHN--GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALR-----TTAVRDGD---GYVLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 279 RYITLAPVATVLGLAFKLRDPEGllgeqeDLGITCALIPTDIKGVEIGNRHFPLNV-PFQNGPTRGQNIFVPIDFIIGGq 357
Cdd:COG1960 154 TFITNAPVADVILVLARTDPAAG------HRGISLFLVPKDTPGVTVGRIEDKMGLrGSDTGELFFDDVRVPAENLLGE- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 358 kmAGQGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVA 437
Cdd:COG1960 227 --EGKGFKIAMSTLNAGR-LGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAW 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516400656 438 GIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGpsNFLARGYQGSPIAVTVEGANILTRSMII 509
Cdd:COG1960 304 LLDAGEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTRE--YPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
208-501 |
9.26e-35 |
|
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: 135.49 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 208 LGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSI-----PDDgvvckGEWegkevlgmRLTWNKRYIT 282
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIrttarKDG-----DGY--------VLNGRKIFIS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 283 LAPVATVLGLAFKLrDPEGLLGEqedlGITCALIPTDIKGVEIGNrhfPLNVPFQNG-PTRG---QNIFVPIDFIIGGqk 358
Cdd:cd00567 109 NGGDADLFIVLART-DEEGPGHR----GISAFLVPADTPGVTVGR---IWDKMGMRGsGTGElvfDDVRVPEDNLLGE-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 359 mAGQGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAG 438
Cdd:cd00567 179 -EGGGFELAMKGLNVGR-LLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWL 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516400656 439 IDLGE-KPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGicLGPSNFLARGYQGSPIAVTVEGAN 501
Cdd:cd00567 257 LDQGPdEARLEAAMAKLFATEAAREVADLAMQIHGGRG--YSREYPVERYLRDARAARIAEGTA 318
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
153-475 |
2.06e-33 |
|
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: 132.78 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 153 PPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTVGVPNSLGPGELLQhYGTEEQKNYYLPRLAE 232
Cdd:cd01158 32 PREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPIIK-FGTEEQKKKYLPPLAT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 233 GKEIPCFALTSPEAGSDAGSIPDDGVVCKGEWegkevlgmRLTWNKRYITLAPVATVLgLAFKLRDPEglLGEQedlGIT 312
Cdd:cd01158 111 GEKIGAFALSEPGAGSDAAALKTTAKKDGDDY--------VLNGSKMWITNGGEADFY-IVFAVTDPS--KGYR---GIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 313 CALIPTDIKGVEIGNRHFPLNVpfQNGPT---RGQNIFVPIDFIIGGQkmaGQGWRMLVECLSVGRgITLPSNSTgGIKS 389
Cdd:cd01158 177 AFIVERDTPGLSVGKKEDKLGI--RGSSTtelIFEDVRVPKENILGEE---GEGFKIAMQTLDGGR-IGIAAQAL-GIAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 390 AAL-ATGAYSRIRRQFKQPIGHLEGVEEALARLggnAYVMDAASNLTVAGIDL---GEKPSVISAIVKYHCTHRGQRSII 465
Cdd:cd01158 250 AALdAAVDYAKERKQFGKPIADFQGIQFKLADM---ATEIEAARLLTYKAARLkdnGEPFIKEAAMAKLFASEVAMRVTT 326
|
330
....*....|
gi 516400656 466 DAMDIVGGKG 475
Cdd:cd01158 327 DAVQIFGGYG 336
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
101-514 |
1.48e-32 |
|
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: 131.05 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 101 AELFKGKPEWKKLhaIPAPKLSAEEQA----FLDGPVNEVCAMVSDYQVTHELADLPPEVWQYLKDHKFFAMIIKKKYGG 176
Cdd:cd01161 4 LNMFLGDIVTKQV--FPYPSVLTEEQTeelnMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 177 LEFSAyAQSLVLQKLTGVSGVLSSTVGVPNSLG-PGELLqhYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSIPd 255
Cdd:cd01161 82 LGLNN-TQYARLAEIVGMDLGFSVTLGAHQSIGfKGILL--FGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIR- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 256 dgvvCKGEW--EGKEVLgmrLTWNKRYIT---LAPVATVLGlAFKLRDPEGLLGEqedlGITCALIPTDIKGVEIGNRHF 330
Cdd:cd01161 158 ----TTAVLseDGKHYV---LNGSKIWITnggIADIFTVFA-KTEVKDATGSVKD----KITAFIVERSFGGVTNGPPEK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 331 PLNVPFQNGPT-RGQNIFVPIDFIIGgqkMAGQGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIG 409
Cdd:cd01161 226 KMGIKGSNTAEvYFEDVKIPVENVLG---EVGDGFKVAMNILNNGR-FGMGAALIGTMKRCIEKAVDYANNRKQFGKKIH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 410 HLEGVEEALARLGGNAYVMDAASNLTVAGIDLGEKP--SVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGPSnfLARG 487
Cdd:cd01161 302 EFGLIQEKLANMAILQYATESMAYMTSGNMDRGLKAeyQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYG--VERV 379
|
410 420
....*....|....*....|....*..
gi 516400656 488 YQGSPIAVTVEGANILTRsMIIYGQGA 514
Cdd:cd01161 380 LRDLRIFRIFEGTNEILR-LFIALTGL 405
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
121-479 |
1.53e-26 |
|
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: 112.45 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 121 LSAEEQAFLDGpVNEVCA-----MVSDYqvtHELADLPPEVWQYLKDHKFFAMIIKKkYGGLEFSAYAQSLVLQKLTGVS 195
Cdd:cd01151 13 LTEEERAIRDT-AREFCQeelapRVLEA---YREEKFDRKIIEEMGELGLLGATIKG-YGCAGLSSVAYGLIAREVERVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 196 GVLSSTVGVPNSLGPGELlQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGsipddGVVCKGEWEGKevlGMRLT 275
Cdd:cd01151 88 SGYRSFMSVQSSLVMLPI-YDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPG-----GMETRARKDGG---GYKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 276 WNKRYITLAPVATVLGLAFKLrdpegllgeQEDLGITCALIPTDIKGVE---IGNRhFPLNVPfQNGPTRGQNIFVPIDF 352
Cdd:cd01151 159 GSKTWITNSPIADVFVVWARN---------DETGKIRGFILERGMKGLSapkIQGK-FSLRAS-ITGEIVMDNVFVPEEN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 353 IIGGQKmagqGWRMLVECLSVGR-GItlpsnSTG--GIKSAALATG-AYSRIRRQFKQPIGHLEGVEEALArlggnayvm 428
Cdd:cd01151 228 LLPGAE----GLRGPFKCLNNARyGI-----AWGalGAAEDCYHTArQYVLDRKQFGRPLAAFQLVQKKLA--------- 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516400656 429 DAASNLTV---AGIDLGE-------KPSVISAIVKYHCthRGQRSIID-AMDIVGGKGICLG 479
Cdd:cd01151 290 DMLTEIALgllACLRVGRlkdqgkaTPEQISLLKRNNC--GKALEIARtAREMLGGNGISDE 349
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
153-475 |
7.19e-21 |
|
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: 95.56 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 153 PPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTVGVPNSLGPGELLQHyGTEEQKNYYLPRLAE 232
Cdd:cd01156 35 PRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNLCINQIYRN-GSAAQKEKYLPKLIS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 233 GKEIPCFALTSPEAGSDAGSIPddgvvCKGEWEGKEVLgmrLTWNKRYITLAPVATVLgLAFKLRDPegllgEQEDLGIT 312
Cdd:cd01156 114 GEHIGALAMSEPNAGSDVVSMK-----LRAEKKGDRYV---LNGSKMWITNGPDADTL-VVYAKTDP-----SAGAHGIT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 313 CALIPTDIKGVEIGNRHFPLNVpfqngptRG--------QNIFVPIDFIIGGQkmaGQGWRMLVECLSVGRGItLPSNST 384
Cdd:cd01156 180 AFIVEKGMPGFSRAQKLDKLGM-------RGsntcelvfEDCEVPEENILGGE---NKGVYVLMSGLDYERLV-LAGGPI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 385 GGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARL-----GGNAYVMDAAsnltvAGIDLGEKPSVISAIVKYHCTHR 459
Cdd:cd01156 249 GIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMytrlnASRSYLYTVA-----KACDRGNMDPKDAAGVILYAAEK 323
|
330
....*....|....*.
gi 516400656 460 GQRSIIDAMDIVGGKG 475
Cdd:cd01156 324 ATQVALDAIQILGGNG 339
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
122-234 |
4.15e-18 |
|
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: 80.58 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 122 SAEEQAFLDgpvnevcaMVSDYqVTHELADL----------PPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKL 191
Cdd:pfam02771 1 TEEQEALRD--------TVREF-AEEEIAPHaaewdeegefPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEEL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 516400656 192 TGVSGVLSSTVGVPNSLGpGELLQHYGTEEQKNYYLPRLAEGK 234
Cdd:pfam02771 72 ARADASVALALSVHSSLG-APPILRFGTEEQKERYLPKLASGE 113
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
151-475 |
5.88e-17 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 83.77 E-value: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 151 DLPPEV--WQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTVGVPNSLGPGELLQHyGTEEQKNYYLP 228
Cdd:PLN02519 57 SFPKDVnlWKLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRN-GTPAQKEKYLP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 229 RLAEGKEIPCFALTSPEAGSDAGSIPddgvvCKGEWEGKevlGMRLTWNKRYITLAPVATVLGLAFKLRDPEGllgeqeD 308
Cdd:PLN02519 136 KLISGEHVGALAMSEPNSGSDVVSMK-----CKAERVDG---GYVLNGNKMWCTNGPVAQTLVVYAKTDVAAG------S 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 309 LGITCALIPTDIKGVEIGNRHFPLNVpfqngptRG--------QNIFVPIDFIIGGQkmaGQGWRMLVECLSVGRgITLP 380
Cdd:PLN02519 202 KGITAFIIEKGMPGFSTAQKLDKLGM-------RGsdtcelvfENCFVPEENVLGQE---GKGVYVMMSGLDLER-LVLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 381 SNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARL-----GGNAYVMDAASNLTVAGIDLGEKPSVIsaivkYH 455
Cdd:PLN02519 271 AGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMytslqSSRSYVYSVARDCDNGKVDRKDCAGVI-----LC 345
|
330 340
....*....|....*....|
gi 516400656 456 CTHRGQRSIIDAMDIVGGKG 475
Cdd:PLN02519 346 AAERATQVALQAIQCLGGNG 365
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
152-475 |
2.02e-16 |
|
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: 82.11 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 152 LPPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLTGVSGVLSSTVGVPNSLGpgELLQHYGTEEQKNYYLPRLA 231
Cdd:cd01162 33 FPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCA--WMIDSFGNDEQRERFLPDLC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 232 EGKEIPCFALTSPEAGSDAGSIPDDGVVckgewEGKEVLgmrLTWNKRYITLAPVATVLGLAFKlrdpeglLGEQEDLGI 311
Cdd:cd01162 111 TMEKLASYCLTEPGSGSDAAALRTRAVR-----EGDHYV---LNGSKAFISGAGDSDVYVVMAR-------TGGEGPKGI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 312 TCALIPTDIKGVEIGNRHFPLNVPFQngPTRgQNIF----VPIDFIIGGQkmaGQGWRMLVECLSVGRgITLPSNSTGGI 387
Cdd:cd01162 176 SCFVVEKGTPGLSFGANEKKMGWNAQ--PTR-AVIFedcrVPVENRLGGE---GQGFGIAMAGLNGGR-LNIASCSLGAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 388 KSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAY-----VMDAASNLtvagiDLGEKPSV-ISAIVKYHCTHRGQ 461
Cdd:cd01162 249 QAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVasrlmVRRAASAL-----DRGDPDAVkLCAMAKRFATDECF 323
|
330
....*....|....
gi 516400656 462 RSIIDAMDIVGGKG 475
Cdd:cd01162 324 DVANQALQLHGGYG 337
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
153-475 |
2.06e-14 |
|
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: 75.61 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 153 PPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLtGVSGVLSSTVGVPNSLGpGELLQHYGTEEQKNYYLPRLAE 232
Cdd:cd01160 32 PREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEEL-ARAGGSGPGLSLHTDIV-SPYITRAGSPEQKERVLPQMVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 233 GKEIPCFALTSPEAGSDAGSI----PDDG--VVCKGEwegkevlgmrltwnKRYITLAPVATVLGLAFKLRDPEGLLGeq 306
Cdd:cd01160 110 GKKIGAIAMTEPGAGSDLQGIrttaRKDGdhYVLNGS--------------KTFITNGMLADVVIVVARTGGEARGAG-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 307 edlGITCALIPTDIKGVEIGNRHFPLNVPFQNGPTRG-QNIFVPIDFIIGGQkmaGQGWRMLVECLSVGRgITLPSNSTG 385
Cdd:cd01160 174 ---GISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFfDDCRVPAENLLGEE---NKGFYYLMQNLPQER-LLIAAGALA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 386 GIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAGIDLGEKPSVISAIVKYHCTHRGQRSII 465
Cdd:cd01160 247 AAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWATELQNRVAY 326
|
330
....*....|
gi 516400656 466 DAMDIVGGKG 475
Cdd:cd01160 327 ECVQLHGGWG 336
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
170-475 |
1.75e-12 |
|
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: 69.92 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 170 IKKKYGGLEFSAYAQSLVLQKLT-GVSGVLSSTVGvpNSLGPGELLQHyGTEEQKNYYLPRLAEGKEIPCFALTSPEAGS 248
Cdd:cd01157 51 IPEDCGGLGLGTFDTCLITEELAyGCTGVQTAIEA--NSLGQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 249 DAGsipddGVVCKGEWEGKEVLgmrLTWNKRYITLAPVAT-VLGLAFKLRDPEGLLGEqedlGITCALIPTDIKGVEIGN 327
Cdd:cd01157 128 DVA-----GIKTKAEKKGDEYI---INGQKMWITNGGKANwYFLLARSDPDPKCPASK----AFTGFIVEADTPGIQPGR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 328 RHfpLNVPFQNGPTRG---QNIFVPIDFIIGGQkmaGQGWRMLVECLSVGRgitlPSNSTG--GIKSAALATGA-YSRIR 401
Cdd:cd01157 196 KE--LNMGQRCSDTRGitfEDVRVPKENVLIGE---GAGFKIAMGAFDKTR----PPVAAGavGLAQRALDEATkYALER 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516400656 402 RQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKG 475
Cdd:cd01157 267 KTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIAKAFAADIANQLATDAVQIFGGNG 340
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
121-428 |
2.56e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 69.50 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 121 LSAEEQAfLDGPV-----NEVCAMVSDYQvthELADLPPEVWQYLKDHKFFAMIIKKkYG--GLEFSAYAqsLVLQKLTG 193
Cdd:PLN02526 29 LTPEEQA-LRKRVrecmeKEVAPIMTEYW---EKAEFPFHIIPKLGSLGIAGGTIKG-YGcpGLSITASA--IATAEVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 194 VSGVLSSTVGVPNSLGPGELLQhYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSIPDDGVVCKGEWegkevlgmR 273
Cdd:PLN02526 102 VDASCSTFILVHSSLAMLTIAL-CGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGW--------I 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 274 LTWNKRYI---TLAPVATVLGLAFKLRDPEGLLGEQEDLGITCALIPTDIkGVEIgnrhfplnvpFQNGPTRGQNIFVPI 350
Cdd:PLN02526 173 LNGQKRWIgnsTFADVLVIFARNTTTNQINGFIVKKGAPGLKATKIENKI-GLRM----------VQNGDIVLKDVFVPD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516400656 351 DfiiggQKMAG-QGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVM 428
Cdd:PLN02526 242 E-----DRLPGvNSFQDTNKVLAVSR-VMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVRMLGNIQAM 314
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
361-508 |
6.38e-12 |
|
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: 64.20 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 361 GQGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAGID 440
Cdd:pfam00441 1 GRGFRVAMETLNHER-LAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALD 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516400656 441 LGEKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGICLGPSnfLARGYQGSPIAVTVEGANILTRSMI 508
Cdd:pfam00441 80 AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYP--VERLYRDARVLRIGEGTSEIQRNII 145
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
124-475 |
1.05e-10 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 64.36 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 124 EEQAFLDGPVNEVCAMV---SDYQVTHELADLPPEVWQYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLtgvsgvlSS 200
Cdd:PRK12341 7 EEQELLLASIRELITRNfpeEYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEV-------SK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 201 TVGVPNSLGPGELL---QHYGTEEQK----NYYLPRlaeGKEIPCFALTSPEAGSDAGSIPDDGVvckgEWEGKEVLGMR 273
Cdd:PRK12341 80 CGAPAFLITNGQCIhsmRRFGSAEQLrktaESTLET---GDPAYALALTEPGAGSDNNSATTTYT----RKNGKVYLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 274 LTWnkryITLAPVAT-VLGLAfklRDPEGLLGEQedlGITCALIPTDIKGVEIGNRHfplNVPFQNGPTRG---QNIFVP 349
Cdd:PRK12341 153 KTF----ITGAKEYPyMLVLA---RDPQPKDPKK---AFTLWWVDSSKPGIKINPLH---KIGWHMLSTCEvylDNVEVE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 350 IDFIIGGQkmaGQGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARLggnAYVMD 429
Cdd:PRK12341 220 ESDLVGEE---GMGFLNVMYNFEMER-LINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLM---AIKIE 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 516400656 430 AASNLTVAG---IDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKG 475
Cdd:PRK12341 293 NMRNMVYKVawqADNGQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLG 341
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
238-326 |
1.20e-10 |
|
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: 58.83 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 238 CFALTSPEAGSDAGSIPDDGVVCKGEwegkevlGMRLTWNKRYITLAPVATVLGLAFKLRDPEGllgeqeDLGITCALIP 317
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGG-------GWVLNGTKWWITNAGIADLFLVLARTGGDDR------HGGISLFLVP 67
|
....*....
gi 516400656 318 TDIKGVEIG 326
Cdd:pfam02770 68 KDAPGVSVR 76
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
172-511 |
1.31e-08 |
|
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: 57.74 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 172 KKYGGLEFSAyAQSLVLQKLTGVSGVLSSTVGV-PNSLGPgeLLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDA 250
Cdd:cd01152 56 KEYGGRGASL-MEQLIFREEMAAAGAPVPFNQIgIDLAGP--TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 251 GSIPDDGVVCKGEWegkevlgmRLTWNKRYITLAPVATVLGLAFKlRDPEGllgeQEDLGITCALIPTDIKGVEI----- 325
Cdd:cd01152 133 AGLRTRAVRDGDDW--------VVNGQKIWTSGAHYADWAWLLVR-TDPEA----PKHRGISILLVDMDSPGVTVrpirs 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 326 --GNRHFplNVPFQNgptrgqNIFVPIDFIIGGQkmaGQGWRMLVECLSVGRGITLPSNSTGGIKSAALATGAYSRIRRQ 403
Cdd:cd01152 200 inGGEFF--NEVFLD------DVRVPDANRVGEV---NDGWKVAMTTLNFERVSIGGSAATFFELLLARLLLLTRDGRPL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 404 FKQPIGHLEgveeaLARLGGNAYVMDAASNLTVAGIDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIvggkgicLGPSNF 483
Cdd:cd01152 269 IDDPLVRQR-----LARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFGSELAQELAELALEL-------LGTAAL 336
|
330 340
....*....|....*....|....*...
gi 516400656 484 LARGYQGSPIAVTVEGANILTRSMIIYG 511
Cdd:cd01152 337 LRDPAPGAELAGRWEADYLRSRATTIYG 364
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
212-329 |
4.89e-05 |
|
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: 46.61 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 212 ELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSI-----PDDGvvckGEWegkevlgmRLTWNKRYIT---- 282
Cdd:cd01153 94 ATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALrtkavYQAD----GSW--------RINGVKRFISageh 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516400656 283 ----------LA----PVATVLGLAFKLRDPEGLLGE---------QEDLGI----TCALIPTDIKGVEIGNRH 329
Cdd:cd01153 162 dmsenivhlvLArsegAPPGVKGLSLFLVPKFLDDGErngvtvariEEKMGLhgspTCELVFDNAKGELIGEEG 235
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
212-419 |
2.76e-04 |
|
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: 44.30 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 212 ELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPE-AGSDAGSIPddgvvCKGEWEGKEVLgmrLTWNKRYITLA--P--- 285
Cdd:cd01155 102 EVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIE-----CSIERDGDDYV---INGRKWWSSGAgdPrck 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 286 VATVLGLAfklrDPEGLLGEQEDLGItcaLIPTDIKGVEIGNrhfPLNV------PFQNGPTRGQNIFVPIDFIIGGQkm 359
Cdd:cd01155 174 IAIVMGRT----DPDGAPRHRQQSMI---LVPMDTPGVTIIR---PLSVfgyddaPHGHAEITFDNVRVPASNLILGE-- 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 360 aGQGWRMLVECLSVGRgitlpsnstggIKSAALATGAYSRI----------RRQFKQPIGHLEGVEEALA 419
Cdd:cd01155 242 -GRGFEIAQGRLGPGR-----------IHHCMRLIGAAERAlelmcqravsREAFGKKLAQHGVVAHWIA 299
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
154-476 |
2.79e-04 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 44.05 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 154 PEVW-QYLKDHKFFAMIIKKKYGGLEFSAYAQSLVLQKLtgvsGVLSSTVGVPNSL--GPGELLQHyGTEEQKNYYLPRL 230
Cdd:PRK03354 39 PERFvKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMEL----GRLGAPTYVLYQLpgGFNTFLRE-GTQEQIDKIMAFR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 231 AEGKEIPCFALTSPEAGSDAGSIP-----DDGVVckgewegkevlgmRLTWNKRYIT-LAPVATVLGLAFKLRDPE---- 300
Cdd:PRK03354 114 GTGKQMWNSAITEPGAGSDVGSLKttytrRNGKV-------------YLNGSKCFITsSAYTPYIVVMARDGASPDkpvy 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 301 ----------GL-LGEQEDLGI---TCA--------LIPTDIKGVEignrhfplnvpfQNGPTRGQNIFvpiDFiiggqk 358
Cdd:PRK03354 181 tewfvdmskpGIkVTKLEKLGLrmdSCCeitfddveLDEKDMFGRE------------GNGFNRVKEEF---DH------ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 359 magqgWRMLVECLSVGRGITlpsnstgGIKSAAlatgAYSRIRRQFKQPIGHLEGVEEALARLGGNAYVMDAASNLTVAG 438
Cdd:PRK03354 240 -----ERFLVALTNYGTAMC-------AFEDAA----RYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWK 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 516400656 439 IDLGEKPSVISAIVKYHCTHRGQRSIIDAMDIVGGKGI 476
Cdd:PRK03354 304 ADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGI 341
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
135-253 |
6.22e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 43.32 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 135 EVCAMVSDYQVTheladLPP---EVWQYLKDHKFFAMIIKKKYGGlefsayaQSLVLQkltgVSGVLSSTVGVPN----- 206
Cdd:PTZ00456 85 EGCVLLKDGNVT-----TPKgfkEAYQALKAGGWTGISEPEEYGG-------QALPLS----VGFITRELMATANwgfsm 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 516400656 207 ----SLGPGELLQHYGTEEQKNYYLPRLAEGKEIPCFALTSPEAGSDAGSI 253
Cdd:PTZ00456 149 ypglSIGAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQV 199
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
213-503 |
4.08e-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: 40.43 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 213 LLQHYGTEEQKNYYLPRLAEGKEIPCFA---LTSPEAGSDAGSIPDDGVV-CKGEWegkevlgmRLTWNKrYITLAPVAT 288
Cdd:cd01154 122 ALRKYGPEELKQYLPGLLSDRYKTGLLGgtwMTEKQGGSDLGANETTAERsGGGVY--------RLNGHK-WFASAPLAD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 289 VlglAFKLRDPEGLLGEQEdlGITCALIPT-----DIKGVEI-------GNRHFPL-NVPFQNGptrgqnifvpIDFIIG 355
Cdd:cd01154 193 A---ALVLARPEGAPAGAR--GLSLFLVPRlledgTRNGYRIrrlkdklGTRSVATgEVEFDDA----------EAYLIG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516400656 356 GQkmaGQGWRMLVECLSVGRgITLPSNSTGGIKSAALATGAYSRIRRQFKQPIGHLEGVEEALARL-----GGNAYVMDA 430
Cdd:cd01154 258 DE---GKGIYYILEMLNISR-LDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMevdveAATALTFRA 333
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516400656 431 ASNLTVAGIDLGEK---PSVISAIVKYHCTHRGQRSIIDAMDIVGGKGIClgPSNFLARGYQGSPIAVTVEG-ANIL 503
Cdd:cd01154 334 ARAFDRAAADKPVEahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYL--EEWPVARLHREAQVTPIWEGtGNIQ 408
|
|
| |
