|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
3-598 |
0e+00 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 700.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 3 QYKAPLRDMQFVLHELLNAEEHYAKLPdfQGNVSRELVDQYLEAAADFCENELSPLNQVGDREGCTW-NDGVVTTPTGFK 81
Cdd:PTZ00456 25 QYQPRIRDVQFLVEEVFNMYDHYEKLG--KTDVTKELMDSLLEEASKLATQTLLPLYESSDSEGCVLlKDGNVTTPKGFK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 82 EAYQKYIELGFPSLSAEEQYGGQALPNSLGIAISEMVGSSNWAWGMYPGLSHGAVRTLEHHGSDEQKNTYLPNLVSGVWT 161
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 162 GTMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGEHDMAENIIHIVLARLPGAPKGTKGISLFIVPKFNVNAD 241
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 242 GTIGERNAVRCGSIEHKMGIHGNATCVINFDQAKGYLIGPENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKE 321
Cdd:PTZ00456 263 GSLETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 322 RLAMRSLSGPKAPEKEADPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQYADIVEKGETEEERKFADNILSLLTPIAKAF 401
Cdd:PTZ00456 343 RRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAKGC 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 402 LTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTEIQALDLLGRKVLQTQGA-MLRDFTKIIHKFVEANK 480
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSLKGGnEVARFGKRVSKLVRAHL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 481 -DNAAMKEFVEPLAALNKEWGDLTMQIGMRAMQNPDEVGAAAVDYLYFAGYITLAYLWARMALVAQEKLAEGTTDVDFYN 559
Cdd:PTZ00456 503 fSRGALGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWLRMAEVAQKKVAAGQDADGFYQ 582
|
570 580 590
....*....|....*....|....*....|....*....
gi 820954271 560 AKVTTARFYFKKILPRVRSHVDVIAGGlDPLMSLDAEHF 598
Cdd:PTZ00456 583 CKVDTCQYVFQRILPRADAHFQIMQAG-PSIMASKEENW 620
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
44-457 |
5.42e-177 |
|
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: 506.93 E-value: 5.42e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 44 LEAAADFCENELSPLNQVGDREGCTWNDGVVTTPTGFKEAYQKYIELGFPSLSAEEQYGGQALPNSLGIAISEMVgSSNW 123
Cdd:cd01153 2 LEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIF-SRGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 124 AWGMYPGLSHGAVRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGE 203
Cdd:cd01153 81 APLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 204 HDMAENIIHIVLARLPGAPKGTKGISLFIVPKFNVNadgtiGERNAVRCGSIEHKMGIHGNATCVINFDQAKGYLIGPEN 283
Cdd:cd01153 161 HDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 284 RGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERLAMRSLSgpkaPEKEADPIIVHPAVRNMLLTQKAFAEGGRA 363
Cdd:cd01153 236 MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQKAYAEGSRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 364 LVYLLAQYADIVEKGETEEE-RKFADNILSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYE 442
Cdd:cd01153 312 LDLYTATVQDLAERKATEGEdRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYE 391
|
410
....*....|....*
gi 820954271 443 GTTEIQALDLLGRKV 457
Cdd:cd01153 392 GTTGIQALDLIGRKI 406
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
38-462 |
4.45e-114 |
|
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: 345.29 E-value: 4.45e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 38 ELVDQYLEAAADFCENELSPLNQVGDREGctwndgvvTTPtgfKEAYQKYIELGFPSLSAEEQYGGQALPNSLGIAISEM 117
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREG--------EFP---RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 118 VGSSNWAWGMYPGLSHGAVRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGsYAISGEKI 197
Cdd:COG1960 76 LARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 198 FIS-AGEHDmaeniIHIVLARLPGAPkGTKGISLFIVPKFnvnADGtigernaVRCGSIEHKMGIHGNATCVINFDQ--- 273
Cdd:COG1960 155 FITnAPVAD-----VILVLARTDPAA-GHRGISLFLVPKD---TPG-------VTVGRIEDKMGLRGSDTGELFFDDvrv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 274 AKGYLIGPENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERLAMrslsgpkapekeADPIIVHPAVRNMLLT 353
Cdd:COG1960 219 PAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQF------------GRPIADFQAVQHRLAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 354 QKAFAEGGRALVYLLAQYADIVEKgeteeerkfadniLSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVR 433
Cdd:COG1960 287 MAAELEAARALVYRAAWLLDAGED-------------AALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR 353
|
410 420
....*....|....*....|....*....
gi 820954271 434 DTRIACLYEGTTEIQALDlLGRKVLQTQG 462
Cdd:COG1960 354 DARILTIYEGTNEIQRLI-IARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
134-453 |
1.17e-63 |
|
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: 212.53 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 134 GAVRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGsYAISGEKIFISAGehDMAEniIHI 213
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNG--GDAD--LFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 214 VLARLPGAPKGTKGISLFIVPKfnvnadGTIGernaVRCGSIEHKMGIHGNATCVINFDQAK---GYLIGPENRGLNCMF 290
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPA------DTPG----VTVGRIWDKMGMRGSGTGELVFDDVRvpeDNLLGEEGGGFELAM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 291 TFMNTARIGTAVQGLAASESSFQGALTYAKERlamrslsgpKAPEKeadPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQ 370
Cdd:cd00567 188 KGLNVGRLLLAAVALGAARAALDEAVEYAKQR---------KQFGK---PLAEFQAVQFKLADMAAELEAARLLLYRAAW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 371 YADiveKGETEeerkfadniLSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTEIQAL 450
Cdd:cd00567 256 LLD---QGPDE---------ARLEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRL 323
|
...
gi 820954271 451 DLL 453
Cdd:cd00567 324 IIA 326
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
134-453 |
5.14e-53 |
|
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: 186.81 E-value: 5.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 134 GAVRTLEHHGSDEQKNTYLPNLVSGV---WTGTMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGEHDmaeni 210
Cdd:cd01154 118 AAVYALRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLAD----- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 211 IHIVLARLPGAPKGTKGISLFIVPKFNvnADGTigeRNAVRCGSIEHKMGIHGNATCVINFDQAKGYLIGPENRGLNCMF 290
Cdd:cd01154 193 AALVLARPEGAPAGARGLSLFLVPRLL--EDGT---RNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 291 TFMNTARIGTAVQGLAASESSFQGALTYAKERLAMRSlsgpkapekeadPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQ 370
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGK------------PLIDHPLMRRDLAEMEVDVEAATALTFRAAR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 371 YADIVEKGEtEEERKFAdnilSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTEIQAL 450
Cdd:cd01154 336 AFDRAAADK-PVEAHMA----RLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
...
gi 820954271 451 DLL 453
Cdd:cd01154 411 DVL 413
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
41-450 |
4.32e-52 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 182.85 E-value: 4.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 41 DQYLEAAADFCENELSPLNQVGDREGctwndgvvTTPtgfKEAYQKYIELGFPSLSAEEQYGGQALPN-SLGIAISEMV- 118
Cdd:cd01158 4 QMIRKTVRDFAEKEIAPLAAEMDEKG--------EFP---REVIKEMAELGLMGIPIPEEYGGAGLDFlAYAIAIEELAk 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 119 GSSNWAWGMYPGLSHGAvRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADgSYAISGEKIF 198
Cdd:cd01158 73 VDASVAVIVSVHNSLGA-NPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD-DYVLNGSKMW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 199 ISAGEHdmAEniIHIVLARLpGAPKGTKGISLFIVPKfnvNADG-TIGERnavrcgsiEHKMGIHGNATCVINFDQA--- 274
Cdd:cd01158 151 ITNGGE--AD--FYIVFAVT-DPSKGYRGITAFIVER---DTPGlSVGKK--------EDKLGIRGSSTTELIFEDVrvp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 275 KGYLIGPENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERLAMrslsgpkapekeADPIIVHPAVRNMLLTQ 354
Cdd:cd01158 215 KENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQF------------GKPIADFQGIQFKLADM 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 355 KAFAEGGRALVYllaQYADIVEKGETeeerkfadniLSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRD 434
Cdd:cd01158 283 ATEIEAARLLTY---KAARLKDNGEP----------FIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRD 349
|
410
....*....|....*.
gi 820954271 435 TRIACLYEGTTEIQAL 450
Cdd:cd01158 350 AKITEIYEGTSEIQRL 365
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
469-593 |
2.98e-46 |
|
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal region of many bacterial acetyl-CoA dehydrogenases.
Pssm-ID: 463716 Cd Length: 126 Bit Score: 158.86 E-value: 2.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 469 TKIIHKFVEANKDNAAMKEFVEPLAALNKEWGDLTMQIGMRAMQ-NPDEVGAAAVDYLYFAGYITLAYLWARMALVAQEK 547
Cdd:pfam12806 1 LAEIRAFIAAAAGDPALAAEAAALAAALAALQEATAWLLARAAKgDPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 820954271 548 LAEGTTDVDFYNAKVTTARFYFKKILPRVRSHVDVIAGGLDPLMSL 593
Cdd:pfam12806 81 LAAGAKDAAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
50-458 |
1.19e-44 |
|
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: 162.67 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 50 FCENELSPLNQVGDRegctwnDGVVTtptgfKEAYQKYIELGFPSLSAEEQYGGQALPNSLGIAISEMVGSSNwawGMYP 129
Cdd:cd01160 13 FFAKEVAPFHHEWEK------AGEVP-----REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAG---GSGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 130 GLS-HGAVRT--LEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADgSYAISGEKIFISAGEHdm 206
Cdd:cd01160 79 GLSlHTDIVSpyITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGD-HYVLNGSKTFITNGML-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 207 aeNIIHIVLARLPGAPKGTKGISLFIVPKfnvNADGTIGERNAvrcgsieHKMGIHGNATCVINFDQA---KGYLIGPEN 283
Cdd:cd01160 156 --ADVVIVVARTGGEARGAGGISLFLVER---GTPGFSRGRKL-------KKMGWKAQDTAELFFDDCrvpAENLLGEEN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 284 RGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERLAMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAEGGRA 363
Cdd:cd01160 224 KGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAF------------GKTLAQLQVVRHKIAELATKVAVTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 364 LVYLLAQyadIVEKGETEeerkfadnilSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEG 443
Cdd:cd01160 292 FLDNCAW---RHEQGRLD----------VAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGG 358
|
410
....*....|....*
gi 820954271 444 TTEIQaLDLLGRKVL 458
Cdd:cd01160 359 TTEIM-KELISRQMV 372
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
44-459 |
9.87e-42 |
|
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: 154.91 E-value: 9.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 44 LEAAADFCENELSPLNQVGDREGctwndgvvTTPTgfkEAYQKYIELGFPSLSAEEQYGGQALPNSLGIAISEMVGSSNW 123
Cdd:cd01162 9 QEVARAFAAKEMAPHAADWDQKK--------HFPV---DVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 124 AWGMYPGLSHGAVRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADgSYAISGEKIFIS-AG 202
Cdd:cd01162 78 STAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFISgAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 203 EHDmaeniIHIVLARLPGapKGTKGISLFIVPKfnvnadGTIGernaVRCGSIEHKMGIHGNATCVINFDQAK---GYLI 279
Cdd:cd01162 157 DSD-----VYVVMARTGG--EGPKGISCFVVEK------GTPG----LSFGANEKKMGWNAQPTRAVIFEDCRvpvENRL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 280 GPENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERLAMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAE 359
Cdd:cd01162 220 GGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQF------------GKPLADFQALQFKLADMATELV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 360 GGRALVYLLAQYADivekgeteeeRKFADNILslLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIAC 439
Cdd:cd01162 288 ASRLMVRRAASALD----------RGDPDAVK--LCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQ 355
|
410 420
....*....|....*....|
gi 820954271 440 LYEGTTEIQALdLLGRKVLQ 459
Cdd:cd01162 356 ILEGTNEIMRL-IIARALLT 374
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
81-450 |
9.20e-38 |
|
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: 144.53 E-value: 9.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 81 KEAYQKYIELGFPSLSAEEQYGGQALPNSLGIAISEMVGssnwawgMYPGLS-----HGAVRTLE--HHGSDEQKNTYLP 153
Cdd:cd01161 59 RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVG-------MDLGFSvtlgaHQSIGFKGilLFGTEAQKEKYLP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 154 NLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGS-YAISGEKIFISAGehDMAEniIHIVLARLP-----GAPKgtKG 227
Cdd:cd01161 132 KLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNG--GIAD--IFTVFAKTEvkdatGSVK--DK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 228 ISLFIVpkfnvnadgtigERN--AVRCGSIEHKMGIHGNATCVINFDQAK---GYLIGPENRGLNCMFTFMNTARIGTAV 302
Cdd:cd01161 206 ITAFIV------------ERSfgGVTNGPPEKKMGIKGSNTAEVYFEDVKipvENVLGEVGDGFKVAMNILNNGRFGMGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 303 QGLAASESSFQGALTYAKERLAMRslsgpkapEKEADPIIVHPAVRNMLLTQKAfAEggrALVYLLAQYADivekgetee 382
Cdd:cd01161 274 ALIGTMKRCIEKAVDYANNRKQFG--------KKIHEFGLIQEKLANMAILQYA-TE---SMAYMTSGNMD--------- 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820954271 383 ERKFADniLSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTEIQAL 450
Cdd:cd01161 333 RGLKAE--YQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
38-455 |
1.51e-33 |
|
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: 131.76 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 38 ELVDQYLEAAADFCENELSPLNQVGDREgctwndgvvttpTGF-KEAYQKYIELGFPSLSAEEQYGGQALPN-SLGIAIS 115
Cdd:cd01156 4 DEIEMLRQSVREFAQKEIAPLAAKIDRD------------NEFpRDLWRKMGKLGLLGITAPEEYGGSGMGYlAHVIIME 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 116 EMVGSSNWAwgmypGLSHGA-----VRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEpNADGSY 190
Cdd:cd01156 72 EISRASGSV-----ALSYGAhsnlcINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAE-KKGDRY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 191 AISGEKIFISAGEHdmAEniIHIVLARlPGAPKGTKGISLFIVPKfnvnadgtiGERNAVRCGSIEhKMGIHGNATCVIN 270
Cdd:cd01156 146 VLNGSKMWITNGPD--AD--TLVVYAK-TDPSAGAHGITAFIVEK---------GMPGFSRAQKLD-KLGMRGSNTCELV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 271 FDQAK---GYLIGPENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERLAMrslsGPKAPEKEadpiIVHPAV 347
Cdd:cd01156 211 FEDCEvpeENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQF----GQPIGEFQ----LVQGKL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 348 RNMLLTQKAfaegGRALVYLLAQYADiveKGETeEERKFADNILslltpiakaFLTETGSESAKHGVQVFGGHGFISEHG 427
Cdd:cd01156 283 ADMYTRLNA----SRSYLYTVAKACD---RGNM-DPKDAAGVIL---------YAAEKATQVALDAIQILGGNGYINDYP 345
|
410 420 430
....*....|....*....|....*....|.
gi 820954271 428 MEQIVRDtriACLYE---GTTEIQALdLLGR 455
Cdd:cd01156 346 TGRLLRD---AKLYEigaGTSEIRRM-VIGR 372
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
164-465 |
3.27e-26 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 112.92 E-value: 3.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 164 MCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGEHDMaeniiHIVLARLPGapkgtkGISLFIVPKFNVNadgt 243
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDA-----HLVLAQAKG------GLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 244 iGERNAVRCGSIEHKMGIHGNATCVINFDQAKGYLIGPENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERL 323
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 324 AMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQYADiveKGETEEERKFAdnilSLLTPIAKAFLT 403
Cdd:PRK11561 326 VF------------GKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD---RRADAKEALWA----RLFTPAAKFVIC 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820954271 404 ETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTEIQALDLLgrKVLQTQGAML 465
Cdd:PRK11561 387 KRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL--RVLNKQPGVY 446
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
143-458 |
1.21e-25 |
|
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: 108.83 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 143 GSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADgSYAISGEKIFISAGEHDMAeniiHIVLARLPGAP 222
Cdd:cd01157 97 GNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGGKANW----YFLLARSDPDP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 223 K--GTKGISLFIVPkfnvnadgtiGERNAVRCGSIEHKMGIHGNATCVINFDQ----AKGYLIGPENRGLNCMFTFMNTa 296
Cdd:cd01157 172 KcpASKAFTGFIVE----------ADTPGIQPGRKELNMGQRCSDTRGITFEDvrvpKENVLIGEGAGFKIAMGAFDKT- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 297 RIGTAVQGLAASESSFQGALTYAKERLAMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAEGGRaLVYLLAQYadive 376
Cdd:cd01157 241 RPPVAAGAVGLAQRALDEATKYALERKTF------------GKLIAEHQAVSFMLADMAMKVELAR-LAYQRAAW----- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 377 kgETEEERKFadnilSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTEIQALdLLGRK 456
Cdd:cd01157 303 --EVDSGRRN-----TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRL-IISRE 374
|
..
gi 820954271 457 VL 458
Cdd:cd01157 375 HL 376
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
45-457 |
1.64e-24 |
|
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: 105.90 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 45 EAAADFCENELSPLNQVGDREGCTwndgvvttptgFKEAYQKYIELGFPSLSAEEqYGGQALPN-SLGIAISEMVGSSNW 123
Cdd:cd01151 22 DTAREFCQEELAPRVLEAYREEKF-----------DRKIIEEMGELGLLGATIKG-YGCAGLSSvAYGLIAREVERVDSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 124 AWGMYPGLSHGAVRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGsYAISGEKIFIsaGE 203
Cdd:cd01151 90 YRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKTWI--TN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 204 HDMAEniIHIVLARLpgapKGTKGISLFIVPKfnvNADGTIGERnavrcgsIEHKMGIHGNATCVINFDQ---AKGYLIg 280
Cdd:cd01151 167 SPIAD--VFVVWARN----DETGKIRGFILER---GMKGLSAPK-------IQGKFSLRASITGEIVMDNvfvPEENLL- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 281 PENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERlamRSLSGPKApekeadpiivhpavRNMLLTQK-AFAE 359
Cdd:cd01151 230 PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDR---KQFGRPLA--------------AFQLVQKKlADML 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 360 GGRALVYLLAqyadiVEKGETEEERKFADNILSLLtpiaKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIAC 439
Cdd:cd01151 293 TEIALGLLAC-----LRVGRLKDQGKATPEQISLL----KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVN 363
|
410
....*....|....*...
gi 820954271 440 LYEGTTEIQALdLLGRKV 457
Cdd:cd01151 364 TYEGTHDIHAL-ILGRAI 380
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
89-461 |
6.71e-22 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 98.41 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 89 ELGFPSLSAEEQYGGQALPNSLG-IAISEMVGSSNWAwgmypGLSHGA-----VRTLEHHGSDEQKNTYLPNLVSGVWTG 162
Cdd:PLN02519 70 DFNLHGITAPEEYGGLGLGYLYHcIAMEEISRASGSV-----GLSYGAhsnlcINQLVRNGTPAQKEKYLPKLISGEHVG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 163 TMCLTESHAGSDLGIIRTKAEpNADGSYAISGEKIFISAGEhdMAENIihIVLARLPGApKGTKGISLFIVPKfnvnadG 242
Cdd:PLN02519 145 ALAMSEPNSGSDVVSMKCKAE-RVDGGYVLNGNKMWCTNGP--VAQTL--VVYAKTDVA-AGSKGITAFIIEK------G 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 243 TIGERNAVRCgsieHKMGIHGNATCVINFDQA---KGYLIGPENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYA 319
Cdd:PLN02519 213 MPGFSTAQKL----DKLGMRGSDTCELVFENCfvpEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 320 KERlamrslsgpkapEKEADPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQYADivekGETEEERKFADNILslltpiak 399
Cdd:PLN02519 289 RQR------------EQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCD----NGKVDRKDCAGVIL-------- 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820954271 400 aFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTEIQALdLLGRKVLQTQ 461
Cdd:PLN02519 345 -CAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGRELFKEE 404
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
283-455 |
6.48e-19 |
|
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: 83.84 E-value: 6.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 283 NRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERLAMRSlsgpkapekeadPIIVHPAVRNMLLTQKAFAEGGR 362
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGR------------PLIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 363 ALVYLLAQYADivekgeteeerkfADNILSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYE 442
Cdd:pfam00441 69 LLVYRAAEALD-------------AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
170
....*....|...
gi 820954271 443 GTTEIQaLDLLGR 455
Cdd:pfam00441 136 GTSEIQ-RNIIAR 147
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
163-272 |
6.21e-17 |
|
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: 76.16 E-value: 6.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 163 TMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFIS-AGEHDmaeniIHIVLARlPGAPKGTKGISLFIVPKfnvNAD 241
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIAD-----LFLVLAR-TGGDDRHGGISLFLVPK---DAP 71
|
90 100 110
....*....|....*....|....*....|.
gi 820954271 242 GtigernaVRCGSIEHKMGIHGNATCVINFD 272
Cdd:pfam02770 72 G-------VSVRRIETKLGVRGLPTGELVFD 95
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
136-446 |
6.75e-17 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 83.06 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 136 VRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGEhdMAEniIHIVL 215
Cdd:PTZ00461 127 VNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNGT--VAD--VFLIY 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 216 ARLPGApkgtkgISLFIVPKfnvnadGTIGernaVRCGSIEHKMGIHGNATCVINFDQA---KGYLIGPENRGLNCMFTF 292
Cdd:PTZ00461 203 AKVDGK------ITAFVVER------GTKG----FTQGPKIDKCGMRASHMCQLFFEDVvvpAENLLGEEGKGMVGMMRN 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 293 MNTARIGTAVQGLAASESSFQGALTYAKERLAMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQYA 372
Cdd:PTZ00461 267 LELERVTLAAMAVGIAERSVELMTSYASERKAF------------GKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV 334
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820954271 373 divekGETEEERKFADNILSLLTPIAKafltetgsESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTE 446
Cdd:PTZ00461 335 -----HPGNKNRLGSDAAKLFATPIAK--------KVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
138-459 |
7.12e-16 |
|
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: 79.70 E-value: 7.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 138 TLEHHGSDEQKNTYLPNLVSG--VWtgtmCL--TESHAGSDLGIIRTKAEPNADGsYAISGEKIFISAGEhdmaENIIHI 213
Cdd:cd01152 95 TILAYGTDEQKRRFLPPILSGeeIW----CQgfSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAH----YADWAW 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 214 VLARLPGAPKGTKGISLFIVPkfnVNADGtigernaVRCGSIEHKMGIHGnaTCVINFDQAK---GYLIGPENRGLN-CM 289
Cdd:cd01152 166 LLVRTDPEAPKHRGISILLVD---MDSPG-------VTVRPIRSINGGEF--FNEVFLDDVRvpdANRVGEVNDGWKvAM 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 290 FTFMNtarigtavqglaasESSFQGAlTYAK--ERLAMRSLSGPKAPEKEADpiivHPAVRNMLLTQKAFAEGGRALVYL 367
Cdd:cd01152 234 TTLNF--------------ERVSIGG-SAATffELLLARLLLLTRDGRPLID----DPLVRQRLARLEAEAEALRLLVFR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 368 LAQYADivekgetEEERKFADNilslltPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIV--------RDTRIAC 439
Cdd:cd01152 295 LASALA-------AGKPPGAEA------SIAKLFGSELAQELAELALELLGTAALLRDPAPGAELagrweadyLRSRATT 361
|
330 340
....*....|....*....|
gi 820954271 440 LYEGTTEIQaLDLLGRKVLQ 459
Cdd:cd01152 362 IYGGTSEIQ-RNIIAERLLG 380
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
45-158 |
2.52e-11 |
|
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: 60.94 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 45 EAAADFCENELSPLNQVGDREGctwndgvvttpTGFKEAYQKYIELGFPSLSAEEQYGGQALPNSLGIAISEMVGSSNWA 124
Cdd:pfam02771 9 DTVREFAEEEIAPHAAEWDEEG-----------EFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADAS 77
|
90 100 110
....*....|....*....|....*....|....*
gi 820954271 125 WGMYPGLSHG-AVRTLEHHGSDEQKNTYLPNLVSG 158
Cdd:pfam02771 78 VALALSVHSSlGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
89-459 |
5.57e-11 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 64.47 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 89 ELGFPSLSAEEQYGGQALPNSLGIAISEMVGSSNWAWGMYPGLSHGaVRTLEHHGSDEQKNTYLPNLVSG--VWTGTMcl 166
Cdd:PRK03354 48 DMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGG-FNTFLREGTQEQIDKIMAFRGTGkqMWNSAI-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 167 TESHAGSDLGIIRTKAEpNADGSYAISGEKIFISAGehdmAENIIHIVLARLPGAPKGTKGISLFIvpkfNVNADGTIGE 246
Cdd:PRK03354 125 TEPGAGSDVGSLKTTYT-RRNGKVYLNGSKCFITSS----AYTPYIVVMARDGASPDKPVYTEWFV----DMSKPGIKVT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 247 RnavrcgsiEHKMGIHGNATCVINFDQA---KGYLIGPENRGLNCMFTFMNTARIGTAVQGLAASESSFQGALTYAKERL 323
Cdd:PRK03354 196 K--------LEKLGLRMDSCCEITFDDVeldEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 324 AMRSLSGPKA--PEKEADPIIVHPAVRNMLltqkafaeggralvYLLAQYADivekgeteeerkfADNILSLLTPIAKAF 401
Cdd:PRK03354 268 QFGEAIGRFQliQEKFAHMAIKLNSMKNML--------------YEAAWKAD-------------NGTITSGDAAMCKYF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 820954271 402 LTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTEIQALDlLGRKVLQ 459
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILT-LGRAVLK 377
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
135-457 |
3.07e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 62.56 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 135 AVRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEpNADGSYAISGEKIFIsaGEHDMAEniIHIV 214
Cdd:PLN02526 117 AMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT-KVEGGWILNGQKRWI--GNSTFAD--VLVI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 215 LARlpgaPKGTKGISLFIVPKfnvnadGTIGernaVRCGSIEHKMGIHGNATCVINFDQAkgyLIGPENR--GLNcmfTF 292
Cdd:PLN02526 192 FAR----NTTTNQINGFIVKK------GAPG----LKATKIENKIGLRMVQNGDIVLKDV---FVPDEDRlpGVN---SF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 293 MNT------ARIGTAVQGLAASESSFQGALTYAKERlamRSLSGPKAPEKEADPIIVHpavrnMLLTQKAFAEGGRALVY 366
Cdd:PLN02526 252 QDTnkvlavSRVMVAWQPIGISMGVYDMCHRYLKER---KQFGAPLAAFQINQEKLVR-----MLGNIQAMFLVGWRLCK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 367 LLaqyadivEKGEteeerkfadnilslLTP----IAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYE 442
Cdd:PLN02526 324 LY-------ESGK--------------MTPghasLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYE 382
|
330
....*....|....*
gi 820954271 443 GTTEIQALdLLGRKV 457
Cdd:PLN02526 383 GTYDINAL-VTGREI 396
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
3-32 |
5.94e-10 |
|
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam02770, pfam00441, pfam02771. This family is one of the enzymes involved in AcylCoA interaction in beta-oxidation.
Pssm-ID: 463571 Cd Length: 32 Bit Score: 54.27 E-value: 5.94e-10
10 20 30
....*....|....*....|....*....|
gi 820954271 3 QYKAPLRDMQFVLHELLNAEEhYAKLPDFQ 32
Cdd:pfam12418 1 SYKAPLRDMRFVLYEVLGAEA-LAALPGFA 29
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
113-443 |
1.46e-09 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 60.81 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 113 AISEMVGSSNWAWGMYPGLSHG-AVRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKA--EPNAD-- 187
Cdd:cd01150 86 ALTNSLGGYDLSLGAKLGLHLGlFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQef 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 188 --GSYAISGEKIFISagehDMAENIIH-IVLARL--PGAPKGTKGislFIVPkfnVNADGTIGERNAVRCGSIEHKMGIH 262
Cdd:cd01150 166 viNTPDFTATKWWPG----NLGKTATHaVVFAQLitPGKNHGLHA---FIVP---IRDPKTHQPLPGVTVGDIGPKMGLN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 263 GnatcVIN-FDQAKGYLIgPENRGLNCM-------------------FTFMNTARIGTAVQGLAASESSFQGALTYAKER 322
Cdd:cd01150 236 G----VDNgFLQFRNVRI-PRENLLNRFgdvspdgtyvspfkdpnkrYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRY 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 323 LAMRSLSGPKAPEKEAdPIIVHPAVRNMLLTQKAFAEGGR-ALVYLLAQYADIVEKGETEEERKFADniLSLLTPIAKAF 401
Cdd:cd01150 311 SAVRRQFGPKPSDPEV-QILDYQLQQYRLFPQLAAAYAFHfAAKSLVEMYHEIIKELLQGNSELLAE--LHALSAGLKAV 387
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 820954271 402 LTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEG 443
Cdd:cd01150 388 ATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEG 429
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
81-178 |
1.23e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 44.95 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 81 KEAYQKYIELGFPSLSAEEQYGGQ---ALPNS----------LGIAISEMVGSSnwawgMYPGlshgavRTLEHHGSDEQ 147
Cdd:PRK13026 111 PEVWDYLKKEGFFALIIPKEYGGKgfsAYANStivskiatrsVSAAVTVMVPNS-----LGPG------ELLTHYGTQEQ 179
|
90 100 110
....*....|....*....|....*....|.
gi 820954271 148 KNTYLPNLVSGVWTGTMCLTESHAGSDLGII 178
Cdd:PRK13026 180 KDYWLPRLADGTEIPCFALTGPEAGSDAGAI 210
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
107-178 |
7.49e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 42.50 E-value: 7.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820954271 107 PNSLGiaisemvgssnwawgmyPGlshgavRTLEHHGSDEQKNTYLPNLVSGVWTGTMCLTESHAGSDLGII 178
Cdd:PRK09463 163 PNSLG-----------------PG------ELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
100-252 |
1.92e-03 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 41.02 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 100 QYGGQALPNSLGIAISEMVGSSNWAwGMYPGLSHGAVRT--LEHHGSDEQKNTYLpnlvSGVWTGTMCL---TESHAGSD 174
Cdd:PTZ00457 73 EYGGLGLGHTAHALIYEEVGTNCDS-KLLSTIQHSGFCTylLSTVGSKELKGKYL----TAMSDGTIMMgwaTEEGCGSD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 175 LGIIRTKAEPNADGSYAISGEK--IFISAGEH--DMAENIIHIVLARlpgAPKGTKGISLFIVPK----FNVNADGTIGE 246
Cdd:PTZ00457 148 ISMNTTKASLTDDGSYVLTGQKrcEFAASATHflVLAKTLTQTAAEE---GATEVSRNSFFICAKdakgVSVNGDSVVFE 224
|
....*.
gi 820954271 247 RNAVRC 252
Cdd:PTZ00457 225 NTPAAD 230
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
301-446 |
1.95e-03 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 38.87 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820954271 301 AVQGLAASESSFQGALTYAKERLAMRSlsgpkapekeADPIIVHPAVRNMLLTQKAFAEGGRALVYllAQYADIVEKGET 380
Cdd:pfam08028 3 AAAALGAARAALAEFTERARGRVRAYF----------GVPLAEDPATQLALAEAAARIDAARLLLE--RAAARIEAAAAA 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820954271 381 EEERKFADnilSLLTPIAKAFLTETGSESAKHGVQVFGGHGFISEHGMEQIVRDTRIACLYEGTTE 446
Cdd:pfam08028 71 GKPVTPAL---RAEARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| |
