|
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: 705.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 3 QYKAPLRDMQFVLHELLNAEEHYAKLpAFSgNVSRELVDQYLEAAADFCENELSPLNQVGDREGCTW-NDGVVTTPTGFK 81
Cdd:PTZ00456 25 QYQPRIRDVQFLVEEVFNMYDHYEKL-GKT-DVTKELMDSLLEEASKLATQTLLPLYESSDSEGCVLlKDGNVTTPKGFK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 82 EAYQKYIELGFPSLSAEEQYGGQGLPNSLGITISEMVGTANWAWGMYPGLSHGAVRTLEHHGSQEQKDTYLPNLVSGVWT 161
Cdd:PTZ00456 103 EAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLVSGEWS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 162 GTMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGEHDMAENIIHIVLARLPGAPKGTKGISLFIVPKFNLNAD 241
Cdd:PTZ00456 183 GTMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDHDLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 242 GSIGERNAVRCGSIEHKMGIHGNATCVINFDNAKGYLIGPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKD 321
Cdd:PTZ00456 263 GSLETAKNVKCIGLEKKMGIKGSSTCQLSFENSVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNALRYARE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 322 RLAMRSLSGPKAPEKEADPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQYADVVEQAAEEEDRKFADNILSLLTPIAKAF 401
Cdd:PTZ00456 343 RRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAAAKDAATREALDHEIGFYTPIAKGC 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 402 LTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTEIQALDLLGRKVLGTQGA-MLKDFTKIIHKFAEANK 480
Cdd:PTZ00456 423 LTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSLKGGnEVARFGKRVSKLVRAHL 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 481 -DNAGMKEFVEPLAALNKEWGDLTMQIGMRAMQNPEEVGAAAVDYLYFSGYVTLAYLWARMALVAQEALAAGTTDVDFYN 559
Cdd:PTZ00456 503 fSRGALGQYARRLWLLQKQWRLATTRVKMMAMSDRDAVGAASEDFLMYTGYMVLGYYWLRMAEVAQKKVAAGQDADGFYQ 582
|
570 580 590
....*....|....*....|....*....|....*....
gi 1126530072 560 AKVTTARFYFKKILPRVRSHVDVIATGlDPLMALDAEHF 598
Cdd:PTZ00456 583 CKVDTCQYVFQRILPRADAHFQIMQAG-PSIMASKEENW 620
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
44-457 |
3.10e-176 |
|
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: 505.00 E-value: 3.10e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 44 LEAAADFCENELSPLNQVGDREGCTWNDGVVTTPTGFKEAYQKYIELGFPSLSAEEQYGGQGLPNSLGITISEMVgTANW 123
Cdd:cd01153 2 LEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPPFKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIF-SRGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 124 AWGMYPGLSHGAVRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGE 203
Cdd:cd01153 81 APLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 204 HDMAENIIHIVLARLPGAPKGTKGISLFIVPKFNLNadgsiGERNAVRCGSIEHKMGIHGNATCVINFDNAKGYLIGPEN 283
Cdd:cd01153 161 HDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD-----GERNGVTVARIEEKMGLHGSPTCELVFDNAKGELIGEEG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 284 RGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRLAMRSLSgpkaPEKEADPIIVHPAVRNMLLTQKAFAEGGRA 363
Cdd:cd01153 236 MGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQKAYAEGSRA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 364 LVYLLAQYADVVEQAA-EEEDRKFADNILSLLTPIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYE 442
Cdd:cd01153 312 LDLYTATVQDLAERKAtEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYE 391
|
410
....*....|....*
gi 1126530072 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 |
1.51e-116 |
|
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: 351.45 E-value: 1.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 38 ELVDQYLEAAADFCENELSPLNQVGDREGctwndgvvTTPtgfKEAYQKYIELGFPSLSAEEQYGGQGLPNSLGITISEM 117
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREG--------EFP---RELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 118 VGTANWAWGMYPGLSHGAVRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGsYAISGEKI 197
Cdd:COG1960 76 LARADASLALPVGVHNGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQKT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 198 FIS-AGEHDmaeniIHIVLARLPGAPkGTKGISLFIVPKFnlnADGsigernaVRCGSIEHKMGIHGNATCVINFDN--- 273
Cdd:COG1960 155 FITnAPVAD-----VILVLARTDPAA-GHRGISLFLVPKD---TPG-------VTVGRIEDKMGLRGSDTGELFFDDvrv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 274 AKGYLIGPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRLAMrslsgpkapekeADPIIVHPAVRNMLLT 353
Cdd:COG1960 219 PAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQF------------GRPIADFQAVQHRLAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 354 QKAFAEGGRALVYLLAQYADVVEQAAEEedrkfadnilsllTPIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVR 433
Cdd:COG1960 287 MAAELEAARALVYRAAWLLDAGEDAALE-------------AAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYR 353
|
410 420
....*....|....*....|....*....
gi 1126530072 434 DTRISCLYEGTTEIQALDlLGRKVLGTQG 462
Cdd:COG1960 354 DARILTIYEGTNEIQRLI-IARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
134-453 |
1.54e-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: 212.14 E-value: 1.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 134 GAVRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGsYAISGEKIFISAGehDMAEniIHI 213
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNG--GDAD--LFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 214 VLARLPGAPKGTKGISLFIVPKfnlnadgsigERNAVRCGSIEHKMGIHGNATCVINFDNAK---GYLIGPENRGLNCMF 290
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPA----------DTPGVTVGRIWDKMGMRGSGTGELVFDDVRvpeDNLLGEEGGGFELAM 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 291 TFMNTARIGTAVQGLSASESSFQGALAYAKDRlamrslsgpKAPEKeadPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQ 370
Cdd:cd00567 188 KGLNVGRLLLAAVALGAARAALDEAVEYAKQR---------KQFGK---PLAEFQAVQFKLADMAAELEAARLLLYRAAW 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 371 YADvveqAAEEEDRkfadnilsLLTPIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTEIQAL 450
Cdd:cd00567 256 LLD----QGPDEAR--------LEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRL 323
|
...
gi 1126530072 451 DLL 453
Cdd:cd00567 324 IIA 326
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
41-450 |
9.50e-55 |
|
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: 190.17 E-value: 9.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 41 DQYLEAAADFCENELSPLNQVGDREGctwndgvvTTPtgfKEAYQKYIELGFPSLSAEEQYGGQGLP------------- 107
Cdd:cd01158 4 QMIRKTVRDFAEKEIAPLAAEMDEKG--------EFP---REVIKEMAELGLMGIPIPEEYGGAGLDflayaiaieelak 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 108 --NSLGITISEMVGTANWAwgmypglshgavrtLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPN 185
Cdd:cd01158 73 vdASVAVIVSVHNSLGANP--------------IIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 186 ADgSYAISGEKIFISAGEHdmAEniIHIVLARLpGAPKGTKGISLFIVPKfnlNADG-SIGERnavrcgsiEHKMGIHGN 264
Cdd:cd01158 139 GD-DYVLNGSKMWITNGGE--AD--FYIVFAVT-DPSKGYRGITAFIVER---DTPGlSVGKK--------EDKLGIRGS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 265 ATCVINFDNA---KGYLIGPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRLAMrslsgpkapekeADPI 341
Cdd:cd01158 202 STTELIFEDVrvpKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQF------------GKPI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 342 IVHPAVRNMLLTQKAFAEGGRALVYLLAQYAD----VVEQAAeeedrkfadnilslltpIAKAFLTETGSEAAKHGVQVF 417
Cdd:cd01158 270 ADFQGIQFKLADMATEIEAARLLTYKAARLKDngepFIKEAA-----------------MAKLFASEVAMRVTTDAVQIF 332
|
410 420 430
....*....|....*....|....*....|...
gi 1126530072 418 GGHGFISEHGMEQIVRDTRISCLYEGTTEIQAL 450
Cdd:cd01158 333 GGYGYTKDYPVERYYRDAKITEIYEGTSEIQRL 365
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
134-453 |
5.70e-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: 5.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 134 GAVRTLEHHGSQEQKDTYLPNLVSGV---WTGTMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGEHDmaeni 210
Cdd:cd01154 118 AAVYALRKYGPEELKQYLPGLLSDRYktgLLGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPLAD----- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 211 IHIVLARLPGAPKGTKGISLFIVPKFNlnadgSIGERNAVRCGSIEHKMGIHGNATCVINFDNAKGYLIGPENRGLNCMF 290
Cdd:cd01154 193 AALVLARPEGAPAGARGLSLFLVPRLL-----EDGTRNGYRIRRLKDKLGTRSVATGEVEFDDAEAYLIGDEGKGIYYIL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 291 TFMNTARIGTAVQGLSASESSFQGALAYAKDRLAMRSlsgpkapekeadPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQ 370
Cdd:cd01154 268 EMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGK------------PLIDHPLMRRDLAEMEVDVEAATALTFRAAR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 371 YADVvEQAAEEEDRKFAdnilSLLTPIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTEIQAL 450
Cdd:cd01154 336 AFDR-AAADKPVEAHMA----RLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
...
gi 1126530072 451 DLL 453
Cdd:cd01154 411 DVL 413
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
469-593 |
1.80e-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: 159.64 E-value: 1.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 469 TKIIHKFAEANKDNAGMKEFVEPLAALNKEWGDLTMQIGMRAMQ-NPEEVGAAAVDYLYFSGYVTLAYLWARMALVAQEA 547
Cdd:pfam12806 1 LAEIRAFIAAAAGDPALAAEAAALAAALAALQEATAWLLARAAKgDPDEAGAGAVPYLMLFGDVVLGWLWLRQALAAQAK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1126530072 548 LAAGTTDVDFYNAKVTTARFYFKKILPRVRSHVDVIATGLDPLMAL 593
Cdd:pfam12806 81 LAAGAKDAAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
44-459 |
8.45e-45 |
|
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: 163.38 E-value: 8.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 44 LEAAADFCENELSPLNQVGDREGctwndgvvTTPTgfkEAYQKYIELGFPSLSAEEQYGGQGLPNSLGITISEMVGTANW 123
Cdd:cd01162 9 QEVARAFAAKEMAPHAADWDQKK--------HFPV---DVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 124 AWGMYPGLSHGAVRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADgSYAISGEKIFIS-AG 202
Cdd:cd01162 78 STAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFISgAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 203 EHDmaeniIHIVLARLPGapKGTKGISLFIVPKfnlnadGSIGernaVRCGSIEHKMGIHGNATCVINFDNAK---GYLI 279
Cdd:cd01162 157 DSD-----VYVVMARTGG--EGPKGISCFVVEK------GTPG----LSFGANEKKMGWNAQPTRAVIFEDCRvpvENRL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 280 GPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRLAMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAE 359
Cdd:cd01162 220 GGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQF------------GKPLADFQALQFKLADMATELV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 360 GGRALVYllaqyadvveQAAEEEDRKFADNILslLTPIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISC 439
Cdd:cd01162 288 ASRLMVR----------RAASALDRGDPDAVK--LCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQ 355
|
410 420
....*....|....*....|
gi 1126530072 440 LYEGTTEIQALdLLGRKVLG 459
Cdd:cd01162 356 ILEGTNEIMRL-IIARALLT 374
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
50-458 |
9.47e-45 |
|
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: 163.05 E-value: 9.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 50 FCENELSPLNQVGDRegctwnDGVVTtptgfKEAYQKYIELGFPSLSAEEQYGGQGLPNSLGITISEMVGTANwawGMYP 129
Cdd:cd01160 13 FFAKEVAPFHHEWEK------AGEVP-----REVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAG---GSGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 130 GLS-HGAVRT--LEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADgSYAISGEKIFISAGEHdm 206
Cdd:cd01160 79 GLSlHTDIVSpyITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGD-HYVLNGSKTFITNGML-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 207 aeNIIHIVLARLPGAPKGTKGISLFIVPKfnlNADGSIGERNAvrcgsieHKMGIHGNATCVINFDNA---KGYLIGPEN 283
Cdd:cd01160 156 --ADVVIVVARTGGEARGAGGISLFLVER---GTPGFSRGRKL-------KKMGWKAQDTAELFFDDCrvpAENLLGEEN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 284 RGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRLAMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAEGGRA 363
Cdd:cd01160 224 KGFYYLMQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAF------------GKTLAQLQVVRHKIAELATKVAVTRA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 364 LVYLLAQyadvvEQAAEEEDrkfadnilSLLTPIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEG 443
Cdd:cd01160 292 FLDNCAW-----RHEQGRLD--------VAEASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGG 358
|
410
....*....|....*
gi 1126530072 444 TTEIQaLDLLGRKVL 458
Cdd:cd01160 359 TTEIM-KELISRQMV 372
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
81-450 |
1.43e-39 |
|
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: 149.54 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 81 KEAYQKYIELGFPSLSAEEQYGGQGLPNSLGITISEMVGtanwawgMYPGLS-----HGAVRTLE--HHGSQEQKDTYLP 153
Cdd:cd01161 59 RKTLTQLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVG-------MDLGFSvtlgaHQSIGFKGilLFGTEAQKEKYLP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 154 NLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGS-YAISGEKIFISAGehDMAEniIHIVLARLP-----GAPKgtKG 227
Cdd:cd01161 132 KLASGEWIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNG--GIAD--IFTVFAKTEvkdatGSVK--DK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 228 ISLFIVpkfnlnadgsigERN--AVRCGSIEHKMGIHGNATCVINFDNAK---GYLIGPENRGLNCMFTFMNTARIGTAV 302
Cdd:cd01161 206 ITAFIV------------ERSfgGVTNGPPEKKMGIKGSNTAEVYFEDVKipvENVLGEVGDGFKVAMNILNNGRFGMGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 303 QGLSASESSFQGALAYAKDRLAMRslsgpkapEKEADPIIVHPAVRNMLLTQKAfAEggrALVYLLAQYADvveqaaeee 382
Cdd:cd01161 274 ALIGTMKRCIEKAVDYANNRKQFG--------KKIHEFGLIQEKLANMAILQYA-TE---SMAYMTSGNMD--------- 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126530072 383 DRKFADniLSLLTPIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTEIQAL 450
Cdd:cd01161 333 RGLKAE--YQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
38-455 |
5.09e-36 |
|
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: 138.70 E-value: 5.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 38 ELVDQYLEAAADFCENELSPLNQVGDREgctwndgvvttpTGF-KEAYQKYIELGFPSLSAEEQYGGQGLPNSLGITISE 116
Cdd:cd01156 4 DEIEMLRQSVREFAQKEIAPLAAKIDRD------------NEFpRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIME 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 117 MVGTANWAWGmypgLSHGA-----VRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEpNADGSYA 191
Cdd:cd01156 72 EISRASGSVA----LSYGAhsnlcINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAE-KKGDRYV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 192 ISGEKIFISAGEHdmAEniIHIVLARlPGAPKGTKGISLFIVPKfnlnadgsiGERNAVRCGSIEhKMGIHGNATCVINF 271
Cdd:cd01156 147 LNGSKMWITNGPD--AD--TLVVYAK-TDPSAGAHGITAFIVEK---------GMPGFSRAQKLD-KLGMRGSNTCELVF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 272 DNAK---GYLIGPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRLAMrslsGPKAPEKEadpiIVHPAVR 348
Cdd:cd01156 212 EDCEvpeENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQF----GQPIGEFQ----LVQGKLA 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 349 NMLLTQKAfaegGRALVYLLAQYADvveqaAEEEDRK-FADNILslltpiakaFLTETGSEAAKHGVQVFGGHGFISEHG 427
Cdd:cd01156 284 DMYTRLNA----SRSYLYTVAKACD-----RGNMDPKdAAGVIL---------YAAEKATQVALDAIQILGGNGYINDYP 345
|
410 420 430
....*....|....*....|....*....|.
gi 1126530072 428 MEQIVRDTRiscLYE---GTTEIQALdLLGR 455
Cdd:cd01156 346 TGRLLRDAK---LYEigaGTSEIRRM-VIGR 372
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
164-465 |
1.05e-26 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 114.46 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 164 MCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGEHDMaeniiHIVLARLPGapkgtkGISLFIVPKFNLNadgs 243
Cdd:PRK11561 182 MGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDA-----HLVLAQAKG------GLSCFFVPRFLPD---- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 244 iGERNAVRCGSIEHKMGIHGNATCVINFDNAKGYLIGPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRL 323
Cdd:PRK11561 247 -GQRNAIRLERLKDKLGNRSNASSEVEFQDAIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 324 AMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQYADvveQAAEEEDRKFAdnilSLLTPIAKAFLT 403
Cdd:PRK11561 326 VF------------GKPLIEQPLMRQVLSRMALQLEGQTALLFRLARAWD---RRADAKEALWA----RLFTPAAKFVIC 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126530072 404 ETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTEIQALDLLgrKVLGTQGAML 465
Cdd:PRK11561 387 KRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLDVL--RVLNKQPGVY 446
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
42-459 |
2.99e-26 |
|
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: 110.75 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 42 QYLEAAADFCENELSPLNQVGDREG-CTWndgvvttptgfkEAYQKYIELGFPSLSAEEQYGGQGLPnslgiTISEMVGT 120
Cdd:cd01157 7 EFQETARKFAREEIIPVAAEYDKSGeYPW------------PLIKRAWELGLMNTHIPEDCGGLGLG-----TFDTCLIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 121 ANWAWG--------MYPGLSHGAVRTlehHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADgSYAI 192
Cdd:cd01157 70 EELAYGctgvqtaiEANSLGQMPVII---SGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYII 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 193 SGEKIFISAGEHDMAeniiHIVLARLPGAPK--GTKGISLFIVPkfnlnadgsiGERNAVRCGSIEHKMGIHGNATCVIN 270
Cdd:cd01157 146 NGQKMWITNGGKANW----YFLLARSDPDPKcpASKAFTGFIVE----------ADTPGIQPGRKELNMGQRCSDTRGIT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 271 FDN----AKGYLIGPENRGLNCMFTFMNTaRIGTAVQGLSASESSFQGALAYAKDRLAMrslsgpkapekeADPIIVHPA 346
Cdd:cd01157 212 FEDvrvpKENVLIGEGAGFKIAMGAFDKT-RPPVAAGAVGLAQRALDEATKYALERKTF------------GKLIAEHQA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 347 VRNMLLTQKAFAEGGRALVYLlaqyadvveqAAEEEDRKFADnilSLLTPIAKAFLTETGSEAAKHGVQVFGGHGFISEH 426
Cdd:cd01157 279 VSFMLADMAMKVELARLAYQR----------AAWEVDSGRRN---TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEY 345
|
410 420 430
....*....|....*....|....*....|...
gi 1126530072 427 GMEQIVRDTRISCLYEGTTEIQALdLLGRKVLG 459
Cdd:cd01157 346 PVEKLMRDAKIYQIYEGTSQIQRL-IISREHLG 377
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
45-462 |
1.92e-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: 105.52 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 45 EAAADFCENELSPLNQVGDREGCTwndgvvttptgFKEAYQKYIELGFPSLSAEEqYGGQGLPN-SLGITISEMVGTANW 123
Cdd:cd01151 22 DTAREFCQEELAPRVLEAYREEKF-----------DRKIIEEMGELGLLGATIKG-YGCAGLSSvAYGLIAREVERVDSG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 124 AWGMYPGLSHGAVRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEPNADGsYAISGEKIFIsaGE 203
Cdd:cd01151 90 YRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGG-YKLNGSKTWI--TN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 204 HDMAEniIHIVLARLpgapKGTKGISLFIVPKfnlNADGsigernaVRCGSIEHKMGIHGNATCVINFDN---AKGYLIg 280
Cdd:cd01151 167 SPIAD--VFVVWARN----DETGKIRGFILER---GMKG-------LSAPKIQGKFSLRASITGEIVMDNvfvPEENLL- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 281 PENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRlamRSLSGPKApekeadpiivhpavRNMLLTQK-AFAE 359
Cdd:cd01151 230 PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDR---KQFGRPLA--------------AFQLVQKKlADML 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 360 GGRALVYLLA-QYADVVEQAaeeedrKFADNILSLLtpiaKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRIS 438
Cdd:cd01151 293 TEIALGLLAClRVGRLKDQG------KATPEQISLL----KRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESV 362
|
410 420
....*....|....*....|....
gi 1126530072 439 CLYEGTTEIQALdLLGRKVLGTQG 462
Cdd:cd01151 363 NTYEGTHDIHAL-ILGRAITGIQA 385
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
89-457 |
1.12e-23 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 103.42 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 89 ELGFPSLSAEEQYGGQGLPNSLGITISEMVGTANWAwgmyPGLSHGA-----VRTLEHHGSQEQKDTYLPNLVSGVWTGT 163
Cdd:PLN02519 70 DFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGS----VGLSYGAhsnlcINQLVRNGTPAQKEKYLPKLISGEHVGA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 164 MCLTESHAGSDLGIIRTKAEpNADGSYAISGEKIFISAGEhdMAENIihIVLARLPGApKGTKGISLFIVPKfnlnadGS 243
Cdd:PLN02519 146 LAMSEPNSGSDVVSMKCKAE-RVDGGYVLNGNKMWCTNGP--VAQTL--VVYAKTDVA-AGSKGITAFIIEK------GM 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 244 IGERNAVRCgsieHKMGIHGNATCVINFDNA---KGYLIGPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAK 320
Cdd:PLN02519 214 PGFSTAQKL----DKLGMRGSDTCELVFENCfvpEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 321 DRlamrslsgpkapEKEADPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQYADvveqaAEEEDRK-FADNILslltpiak 399
Cdd:PLN02519 290 QR------------EQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCD-----NGKVDRKdCAGVIL-------- 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1126530072 400 aFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTEIQALdLLGRKV 457
Cdd:PLN02519 345 -CAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRM-LIGREL 400
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
283-455 |
1.09e-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: 85.77 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 283 NRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRLAMRSlsgpkapekeadPIIVHPAVRNMLLTQKAFAEGGR 362
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGR------------PLIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 363 ALVYLLAQYADvveqaaeeedrkfADNILSLLTPIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYE 442
Cdd:pfam00441 69 LLVYRAAEALD-------------AGGPDGAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGE 135
|
170
....*....|...
gi 1126530072 443 GTTEIQaLDLLGR 455
Cdd:pfam00441 136 GTSEIQ-RNIIAR 147
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
77-458 |
1.28e-19 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 90.94 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 77 PTGFKEAYqkyIELGFPSLSAEEQYGGQGLPNSLGITISEMVGTANwawGMYPGLSHG-AVRTLEHHGSQEQ-KDTYLPN 154
Cdd:PRK12341 39 PREFMRAL---ADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCG---APAFLITNGqCIHSMRRFGSAEQlRKTAEST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 155 LVSGVWTGTMCLTESHAGSDLGIIRTKAEpNADGSYAISGEKIFIS-AGEHDMAeniihIVLARLPGAPKGTKGISLFIV 233
Cdd:PRK12341 113 LETGDPAYALALTEPGAGSDNNSATTTYT-RKNGKVYLNGQKTFITgAKEYPYM-----LVLARDPQPKDPKKAFTLWWV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 234 PkfnLNADGSigERNAVrcgsieHKMGIHGNATCVINFDNA---KGYLIGPENRG-LNCMFTFmNTARIGTAVQGLSASE 309
Cdd:PRK12341 187 D---SSKPGI--KINPL------HKIGWHMLSTCEVYLDNVeveESDLVGEEGMGfLNVMYNF-EMERLINAARSLGFAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 310 SSFQGALAYAKDRLAMRSLSGPKA--PEKEADPIIvhpAVRNMlltqkafaeggRALVYllaqyadvveQAAEEedrkfA 387
Cdd:PRK12341 255 CAFEDAARYANQRIQFGKPIGHNQliQEKLTLMAI---KIENM-----------RNMVY----------KVAWQ-----A 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126530072 388 DNILSLLT--PIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTEIQaLDLLGRKVL 458
Cdd:PRK12341 306 DNGQSLRTsaALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIAGRQIL 377
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
89-446 |
1.22e-17 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 85.37 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 89 ELGFPSLSAEEQYGGQGLPNSLGITISEMVGTANwawgmyPG-----LSHGA--VRTLEHHGSQEQKDTYLPNLVSGVWT 161
Cdd:PTZ00461 79 DLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYD------PGfclayLAHSMlfVNNFYYSASPAQRARWLPKVLTGEHV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 162 GTMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFISAGEhdMAEniIHIVLARLPGApkgtkgISLFIVPKfnlnad 241
Cdd:PTZ00461 153 GAMGMSEPGAGTDVLGMRTTAKKDSNGNYVLNGSKIWITNGT--VAD--VFLIYAKVDGK------ITAFVVER------ 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 242 GSIGernaVRCGSIEHKMGIHGNATCVINFDNA---KGYLIGPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAY 318
Cdd:PTZ00461 217 GTKG----FTQGPKIDKCGMRASHMCQLFFEDVvvpAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 319 AKDRLAMrslsgpkapekeADPIIVHPAVRNMLLTQKAFAEGGRALVYLLAQYAdvveqAAEEEDRKFADNILSLLTPIA 398
Cdd:PTZ00461 293 ASERKAF------------GKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-----HPGNKNRLGSDAAKLFATPIA 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1126530072 399 KafltetgsEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTE 446
Cdd:PTZ00461 356 K--------KVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
99-459 |
1.58e-17 |
|
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: 84.71 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 99 EQYGGQGLPNSLGITISEMVGTAnwawGM-YPGLSHG---AVRTLEHHGSQEQKDTYLPNLVSG--VWtgtmCL--TESH 170
Cdd:cd01152 56 KEYGGRGASLMEQLIFREEMAAA----GApVPFNQIGidlAGPTILAYGTDEQKRRFLPPILSGeeIW----CQgfSEPG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 171 AGSDLGIIRTKAEPNADGsYAISGEKIFISAGEhdmaENIIHIVLARLPGAPKGTKGISLFIVPkfnLNADGsigernaV 250
Cdd:cd01152 128 AGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAH----YADWAWLLVRTDPEAPKHRGISILLVD---MDSPG-------V 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 251 RCGSIEHKMGIHGnaTCVINFDNAK---GYLIGPENRGLN-CMFTFMNtarigtavqglsasESSFQGAL-AYAKDRLAM 325
Cdd:cd01152 193 TVRPIRSINGGEF--FNEVFLDDVRvpdANRVGEVNDGWKvAMTTLNF--------------ERVSIGGSaATFFELLLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 326 RSLSGPKAPEKEADpiivHPAVRNMLLTQKAFAEGGRALVYLLAqyadvveQAAEEEDRKFADNilslltPIAKAFLTET 405
Cdd:cd01152 257 RLLLLTRDGRPLID----DPLVRQRLARLEAEAEALRLLVFRLA-------SALAAGKPPGAEA------SIAKLFGSEL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1126530072 406 GSEAAKHGVQVFGGHGFISEHGMEQIV--------RDTRISCLYEGTTEIQaLDLLGRKVLG 459
Cdd:cd01152 320 AQELAELALELLGTAALLRDPAPGAELagrweadyLRSRATTIYGGTSEIQ-RNIIAERLLG 380
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
163-272 |
8.90e-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: 75.78 E-value: 8.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 163 TMCLTESHAGSDLGIIRTKAEPNADGSYAISGEKIFIS-AGEHDmaeniIHIVLARlPGAPKGTKGISLFIVPKfnlNAD 241
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITnAGIAD-----LFLVLAR-TGGDDRHGGISLFLVPK---DAP 71
|
90 100 110
....*....|....*....|....*....|.
gi 1126530072 242 GsigernaVRCGSIEHKMGIHGNATCVINFD 272
Cdd:pfam02770 72 G-------VSVRRIETKLGVRGLPTGELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
89-458 |
2.13e-14 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 75.25 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 89 ELGFPSLSAEEQYGGQGLPNSLGITISEMVGTANWAWGMYPGLSHGaVRTLEHHGSQEQKDTYLPNLVSG--VWTGTMcl 166
Cdd:PRK03354 48 DMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGG-FNTFLREGTQEQIDKIMAFRGTGkqMWNSAI-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 167 TESHAGSDLGIIRTKAEpNADGSYAISGEKIFISAGehdmAENIIHIVLARLPGAPKGTKGISLFIvpkfnlnaDGSige 246
Cdd:PRK03354 125 TEPGAGSDVGSLKTTYT-RRNGKVYLNGSKCFITSS----AYTPYIVVMARDGASPDKPVYTEWFV--------DMS--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 247 RNAVRCGSIeHKMGIHGNATCVINFDNA---KGYLIGPENRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAYAKDRL 323
Cdd:PRK03354 189 KPGIKVTKL-EKLGLRMDSCCEITFDDVeldEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 324 AMRSLSGPKA--PEKEADPIIVHPAVRNMLLtqkafaeggralvyllaqyadvveQAAEEEDRkfaDNILSLLTPIAKAF 401
Cdd:PRK03354 268 QFGEAIGRFQliQEKFAHMAIKLNSMKNMLY------------------------EAAWKADN---GTITSGDAAMCKYF 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1126530072 402 LTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTEIQALDlLGRKVL 458
Cdd:PRK03354 321 CANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILT-LGRAVL 376
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
45-158 |
2.10e-12 |
|
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: 64.02 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 45 EAAADFCENELSPLNQVGDREGctwndgvvttpTGFKEAYQKYIELGFPSLSAEEQYGGQGLPNSLGITISEMVGTANWA 124
Cdd:pfam02771 9 DTVREFAEEEIAPHAAEWDEEG-----------EFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADAS 77
|
90 100 110
....*....|....*....|....*....|....*
gi 1126530072 125 WGMYPGLSHG-AVRTLEHHGSQEQKDTYLPNLVSG 158
Cdd:pfam02771 78 VALALSVHSSlGAPPILRFGTEEQKERYLPKLASG 112
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
3-32 |
2.72e-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: 55.42 E-value: 2.72e-10
10 20 30
....*....|....*....|....*....|
gi 1126530072 3 QYKAPLRDMQFVLHELLNAEEhYAKLPAFS 32
Cdd:pfam12418 1 SYKAPLRDMRFVLYEVLGAEA-LAALPGFA 29
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
135-459 |
1.87e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 59.87 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 135 AVRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKAEpNADGSYAISGEKIFIsaGEHDMAEniIHIV 214
Cdd:PLN02526 117 AMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTAT-KVEGGWILNGQKRWI--GNSTFAD--VLVI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 215 LARlpgaPKGTKGISLFIVPKfnlnadGSIGernaVRCGSIEHKMGIHGNATCVINFDNAkgyLIGPENR--GLNcmfTF 292
Cdd:PLN02526 192 FAR----NTTTNQINGFIVKK------GAPG----LKATKIENKIGLRMVQNGDIVLKDV---FVPDEDRlpGVN---SF 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 293 MNT------ARIGTAVQGLSASESSFQGALAYAKDRlamRSLSGPKAPEKEADPIIVHpavrnMLLTQKAFAEGGRALVY 366
Cdd:PLN02526 252 QDTnkvlavSRVMVAWQPIGISMGVYDMCHRYLKER---KQFGAPLAAFQINQEKLVR-----MLGNIQAMFLVGWRLCK 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 367 LLAQYADVVEQAAeeedrkfadnilslltpIAKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEGTTE 446
Cdd:PLN02526 324 LYESGKMTPGHAS-----------------LGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYD 386
|
330
....*....|...
gi 1126530072 447 IQALdLLGRKVLG 459
Cdd:PLN02526 387 INAL-VTGREITG 398
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
114-443 |
1.06e-08 |
|
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: 58.11 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 114 ISEMVGTANWAWGMYPGLSHG-AVRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGIIRTKA--EPNAD--- 187
Cdd:cd01150 87 LTNSLGGYDLSLGAKLGLHLGlFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTAtyDPLTQefv 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 188 -GSYAISGEKIFISagehDMAENIIH-IVLARL--PGAPKGTKGislFIVPkfnlnadgsIGERN------AVRCGSIEH 257
Cdd:cd01150 167 iNTPDFTATKWWPG----NLGKTATHaVVFAQLitPGKNHGLHA---FIVP---------IRDPKthqplpGVTVGDIGP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 258 KMGIHGNATCVINFDN---------AKGYLIGPE----------NRGLNCMFTFMNTARIGTAVQGLSASESSFQGALAY 318
Cdd:cd01150 231 KMGLNGVDNGFLQFRNvriprenllNRFGDVSPDgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRY 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 319 AkdrlAMRSLSGPKAPEKEAdPIIVHPAVRNMLLTQKAFAEGGR-ALVYLLAQYADVVEQAAEEEDRKFADniLSLLTPI 397
Cdd:cd01150 311 S----AVRRQFGPKPSDPEV-QILDYQLQQYRLFPQLAAAYAFHfAAKSLVEMYHEIIKELLQGNSELLAE--LHALSAG 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1126530072 398 AKAFLTETGSEAAKHGVQVFGGHGFISEHGMEQIVRDTRISCLYEG 443
Cdd:cd01150 384 LKAVATWTAAQGIQECREACGGHGYLAMNRLPTLRDDNDPFCTYEG 429
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
81-178 |
1.18e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 45.33 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 81 KEAYQKYIELGFPSLSAEEQYGGQG---LPNSlgiTISEMVGTANWAWG---MYPGlSHGAVRTLEHHGSQEQKDTYLPN 154
Cdd:PRK13026 111 PEVWDYLKKEGFFALIIPKEYGGKGfsaYANS---TIVSKIATRSVSAAvtvMVPN-SLGPGELLTHYGTQEQKDYWLPR 186
|
90 100
....*....|....*....|....
gi 1126530072 155 LVSGVWTGTMCLTESHAGSDLGII 178
Cdd:PRK13026 187 LADGTEIPCFALTGPEAGSDAGAI 210
|
|
| Rhamnogalacturan_acetylesterase_like |
cd01821 |
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ... |
332-411 |
2.54e-04 |
|
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.
Pssm-ID: 238859 Cd Length: 198 Bit Score: 42.59 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 332 KAPEKEADPIIVHPAVRNmlltqkAFAEGGRaLVYLLAQYADVVEQAAEEEDRKFADnilslLTPIAKAFLTETGSEAAK 411
Cdd:cd01821 102 EARAKGATPILVTPVTRR------TFDEGGK-VEDTLGDYPAAMRELAAEEGVPLID-----LNAASRALYEAIGPEKSK 169
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
100-196 |
3.48e-04 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 43.33 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126530072 100 QYGGQGLPNSLGITISEMVGTANWAwGMYPGLSHGAVRT--LEHHGSQEQKDTYLpnlvSGVWTGTMCL---TESHAGSD 174
Cdd:PTZ00457 73 EYGGLGLGHTAHALIYEEVGTNCDS-KLLSTIQHSGFCTylLSTVGSKELKGKYL----TAMSDGTIMMgwaTEEGCGSD 147
|
90 100
....*....|....*....|..
gi 1126530072 175 LGIIRTKAEPNADGSYAISGEK 196
Cdd:PTZ00457 148 ISMNTTKASLTDDGSYVLTGQK 169
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
105-178 |
1.12e-03 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 42.11 E-value: 1.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1126530072 105 GLPNSLGitisemvgtanwawgmyPGlshgavRTLEHHGSQEQKDTYLPNLVSGVWTGTMCLTESHAGSDLGII 178
Cdd:PRK09463 161 MVPNSLG-----------------PG------ELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211
|
|
| |
