|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
41-463 |
0e+00 |
|
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: 625.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 41 MLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPesFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHIL- 119
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPP--FKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 120 GANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITS 199
Cdd:cd01153 79 GDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 200 GDsGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDvetgepGERNGVFVTNVEHKMGLKVSATCELAFGQhgvpAK 279
Cdd:cd01153 159 GE-HDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD------GERNGVTVARIEEKMGLHGSPTCELVFDN----AK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 280 GWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLTqmtdKTAPRVTITHHPDVRRSLMTQK 359
Cdd:cd01153 228 GELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 360 AYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAVKVNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRD 439
Cdd:cd01153 304 AYAEGSRALDLYTATVQDLAERKATEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRD 383
|
410 420
....*....|....*....|....
gi 889629858 440 AKIDSLYEGTTAIQAQDFFFRKIV 463
Cdd:cd01153 384 ARITTIYEGTTGIQALDLIGRKIV 407
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
3-611 |
8.25e-89 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 287.92 E-value: 8.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 3 HYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFdPKTHSVMLPESFKK 82
Cdd:PTZ00456 25 QYQPRIRDVQFLVEEVFNMYDHYEKLGKTDVTKELMDSLLEEASKLATQTLLPLYESSDSEGCVL-LKDGNVTTPKGFKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 83 SVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAG-GAGFAQILYHLGTEEQKKWAVLAAERG-WGS 160
Cdd:PTZ00456 104 AYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGlSIGAANTLMAWGSEEQKEQYLTKLVSGeWSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 161 TMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSgDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVE 240
Cdd:PTZ00456 184 TMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDH-DLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 241 TGEPGERNgVFVTNVEHKMGLKVSATCELAFGQhgvpAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNAL 320
Cdd:PTZ00456 263 GSLETAKN-VKCIGLEKKMGIKGSSTCQLSFEN----SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNAL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 321 QYAKSRVQGADLTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAevvhGVDAKLAVKVNDLM- 399
Cdd:PTZ00456 338 RYARERRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAA----AKDAATREALDHEIg 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 400 --LPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDKGVALA-----H 472
Cdd:PTZ00456 414 fyTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSLKGGNEVarfgkR 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 473 VSGQIQEFVDSGAGNGRLKTERALLAKALTdvqgmaAALTGYLMAAQQDVTSlykVGLGSVRFLMSVGDLIIGWLLQRQA 552
Cdd:PTZ00456 494 VSKLVRAHLFSRGALGQYARRLWLLQKQWR------LATTRVKMMAMSDRDA---VGAASEDFLMYTGYMVLGYYWLRMA 564
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 889629858 553 AVAVAALDAGAtgDERSFYEGKVAVASFFAKNFLPLLTSTREVIETlDNDIMELDEAAF 611
Cdd:PTZ00456 565 EVAQKKVAAGQ--DADGFYQCKVDTCQYVFQRILPRADAHFQIMQA-GPSIMASKEENW 620
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
36-456 |
9.72e-82 |
|
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: 262.08 E-value: 9.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 36 DTARDMLAEVSRLAEGPVAESFVEGDRNPPvfdpkthsvmLPESFKKsvnAMLEAGWDKVGIDEALGGMPMPKAVVWALH 115
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREGE----------FPRELWR---KLAELGLLGLTIPEEYGGLGLSLVELALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 116 EHILGANPAVWMYAG-GAGFAQILYHLGTEEQK-KWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGsWHIDGV 193
Cdd:COG1960 74 EELARADASLALPVGvHNGAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 194 KRFITSGDSGDlfeniFHLVLARPEGAgPGTKGLSLYFVPKFLFDVETGEPgerngvfvtnvEHKMGLKVSATCELAFGQ 273
Cdd:COG1960 153 KTFITNAPVAD-----VILVLARTDPA-AGHRGISLFLVPKDTPGVTVGRI-----------EDKMGLRGSDTGELFFDD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 274 HGVPAkGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGAdltqmtdktaprVTITHHPDVRR 353
Cdd:COG1960 216 VRVPA-ENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFG------------RPIADFQAVQH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 354 SLMTQKAYAEGLRALYLYTATFQDAavaevvhGVDAKLAVkvndlmlPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPI 433
Cdd:COG1960 283 RLADMAAELEAARALVYRAAWLLDA-------GEDAALEA-------AMAKLFATEAALEVADEALQIHGGYGYTREYPL 348
|
410 420
....*....|....*....|...
gi 889629858 434 EQYIRDAKIDSLYEGTTAIQAQD 456
Cdd:COG1960 349 ERLYRDARILTIYEGTNEIQRLI 371
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
475-606 |
4.34e-28 |
|
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: 109.17 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 475 GQIQEFVDSGAGNGRLKTERALLAKALTDVQGMAAALTGYLMAAQQDvtslyKVGLGSVRFLMSVGDLIIGWLLQRQAAV 554
Cdd:pfam12806 2 AEIRAFIAAAAGDPALAAEAAALAAALAALQEATAWLLARAAKGDPD-----EAGAGAVPYLMLFGDVVLGWLWLRQALA 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 889629858 555 AVAALDAGatGDERSFYEGKVAVASFFAKNFLPLLTSTREVIETLDNDIMEL 606
Cdd:pfam12806 77 AQAKLAAG--AKDAAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
161-271 |
4.50e-15 |
|
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: 70.77 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 161 TMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFenifhLVLARPEGAGpGTKGLSLYFVPKflfdve 240
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGIADLF-----LVLARTGGDD-RHGGISLFLVPK------ 68
|
90 100 110
....*....|....*....|....*....|.
gi 889629858 241 tgepgERNGVFVTNVEHKMGLKVSATCELAF 271
Cdd:pfam02770 69 -----DAPGVSVRRIETKLGVRGLPTGELVF 94
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
3-34 |
5.12e-07 |
|
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: 46.18 E-value: 5.12e-07
10 20 30
....*....|....*....|....*....|..
gi 889629858 3 HYRSNVRDQVFNLFEVLGVDKALGHGEFSDVD 34
Cdd:pfam12418 1 SYKAPLRDMRFVLYEVLGAEALAALPGFADAD 32
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
41-463 |
0e+00 |
|
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: 625.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 41 MLAEVSRLAEGPVAESFVEGDRNPPVFDPKTHSVMLPesFKKSVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHIL- 119
Cdd:cd01153 1 VLEEVARLAENVLAPLNADGDREGPVFDDGRVVVPPP--FKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 120 GANPAVWMYAGGAGFAQILYHLGTEEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITS 199
Cdd:cd01153 79 GDAPLMYASGTQGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRINGVKRFISA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 200 GDsGDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDvetgepGERNGVFVTNVEHKMGLKVSATCELAFGQhgvpAK 279
Cdd:cd01153 159 GE-HDMSENIVHLVLARSEGAPPGVKGLSLFLVPKFLDD------GERNGVTVARIEEKMGLHGSPTCELVFDN----AK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 280 GWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLTqmtdKTAPRVTITHHPDVRRSLMTQK 359
Cdd:cd01153 228 GELIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNALAYAKERKQGGDLI----KAAPAVTIIHHPDVRRSLMTQK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 360 AYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAVKVNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRD 439
Cdd:cd01153 304 AYAEGSRALDLYTATVQDLAERKATEGEDRKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRD 383
|
410 420
....*....|....*....|....
gi 889629858 440 AKIDSLYEGTTAIQAQDFFFRKIV 463
Cdd:cd01153 384 ARITTIYEGTTGIQALDLIGRKIV 407
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
3-611 |
8.25e-89 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 287.92 E-value: 8.25e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 3 HYRSNVRDQVFNLFEVLGVDKALGHGEFSDVDVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFdPKTHSVMLPESFKK 82
Cdd:PTZ00456 25 QYQPRIRDVQFLVEEVFNMYDHYEKLGKTDVTKELMDSLLEEASKLATQTLLPLYESSDSEGCVL-LKDGNVTTPKGFKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 83 SVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAG-GAGFAQILYHLGTEEQKKWAVLAAERG-WGS 160
Cdd:PTZ00456 104 AYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGlSIGAANTLMAWGSEEQKEQYLTKLVSGeWSG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 161 TMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSgDLFENIFHLVLARPEGAGPGTKGLSLYFVPKFLFDVE 240
Cdd:PTZ00456 184 TMCLTEPQCGTDLGQVKTKAEPSADGSYKITGTKIFISAGDH-DLTENIVHIVLARLPNSLPTTKGLSLFLVPRHVVKPD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 241 TGEPGERNgVFVTNVEHKMGLKVSATCELAFGQhgvpAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNAL 320
Cdd:PTZ00456 263 GSLETAKN-VKCIGLEKKMGIKGSSTCQLSFEN----SVGYLIGEPNAGMKQMFTFMNTARVGTALEGVCHAELAFQNAL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 321 QYAKSRVQGADLTQMTDKTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAevvhGVDAKLAVKVNDLM- 399
Cdd:PTZ00456 338 RYARERRSMRALSGTKEPEKPADRIICHANVRQNILFAKAVAEGGRALLLDVGRLLDIHAA----AKDAATREALDHEIg 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 400 --LPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDKGVALA-----H 472
Cdd:PTZ00456 414 fyTPIAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTGIQALDFIGRKVLSLKGGNEVarfgkR 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 473 VSGQIQEFVDSGAGNGRLKTERALLAKALTdvqgmaAALTGYLMAAQQDVTSlykVGLGSVRFLMSVGDLIIGWLLQRQA 552
Cdd:PTZ00456 494 VSKLVRAHLFSRGALGQYARRLWLLQKQWR------LATTRVKMMAMSDRDA---VGAASEDFLMYTGYMVLGYYWLRMA 564
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 889629858 553 AVAVAALDAGAtgDERSFYEGKVAVASFFAKNFLPLLTSTREVIETlDNDIMELDEAAF 611
Cdd:PTZ00456 565 EVAQKKVAAGQ--DADGFYQCKVDTCQYVFQRILPRADAHFQIMQA-GPSIMASKEENW 620
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
36-456 |
9.72e-82 |
|
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: 262.08 E-value: 9.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 36 DTARDMLAEVSRLAEGPVAESFVEGDRNPPvfdpkthsvmLPESFKKsvnAMLEAGWDKVGIDEALGGMPMPKAVVWALH 115
Cdd:COG1960 7 EEQRALRDEVREFAEEEIAPEAREWDREGE----------FPRELWR---KLAELGLLGLTIPEEYGGLGLSLVELALVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 116 EHILGANPAVWMYAG-GAGFAQILYHLGTEEQK-KWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGsWHIDGV 193
Cdd:COG1960 74 EELARADASLALPVGvHNGAAEALLRFGTEEQKeRYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDG-YVLNGQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 194 KRFITSGDSGDlfeniFHLVLARPEGAgPGTKGLSLYFVPKFLFDVETGEPgerngvfvtnvEHKMGLKVSATCELAFGQ 273
Cdd:COG1960 153 KTFITNAPVAD-----VILVLARTDPA-AGHRGISLFLVPKDTPGVTVGRI-----------EDKMGLRGSDTGELFFDD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 274 HGVPAkGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGAdltqmtdktaprVTITHHPDVRR 353
Cdd:COG1960 216 VRVPA-ENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFG------------RPIADFQAVQH 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 354 SLMTQKAYAEGLRALYLYTATFQDAavaevvhGVDAKLAVkvndlmlPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPI 433
Cdd:COG1960 283 RLADMAAELEAARALVYRAAWLLDA-------GEDAALEA-------AMAKLFATEAALEVADEALQIHGGYGYTREYPL 348
|
410 420
....*....|....*....|...
gi 889629858 434 EQYIRDAKIDSLYEGTTAIQAQD 456
Cdd:COG1960 349 ERLYRDARILTIYEGTNEIQRLI 371
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
34-457 |
3.11e-48 |
|
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: 174.10 E-value: 3.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 34 DVDTARDMLAEVSRLAEGPVAESFVEGDRNPPVFDP------KTHSVMLPESFKKSVNAMLEAGwdKVGIDEALGGMPMP 107
Cdd:cd01154 15 GDPEEEPDLSRLGELAGGELYELARLADRNPPVLEMwdrwgrRVDRVWVHPAWHALMRRLIEEG--VINIEDGPAGEGRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 108 KAVVWA---LHEHILGANPAVwmyAGGAGFAQILYHLGTEEQKKW----AVLAAERGWGSTMVLTEPDAGSDVGAARTKA 180
Cdd:cd01154 93 HVHFAAgylLSDAAAGLLCPL---TMTDAAVYALRKYGPEELKQYlpglLSDRYKTGLLGGTWMTEKQGGSDLGANETTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 181 VQQADGSWHIDGVKRFiTSGDSGDLFenifhLVLARPEGAGPGTKGLSLYFVPKFLFDvetgepGERNGVFVTNVEHKMG 260
Cdd:cd01154 170 ERSGGGVYRLNGHKWF-ASAPLADAA-----LVLARPEGAPAGARGLSLFLVPRLLED------GTRNGYRIRRLKDKLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 261 LKVSATCELAFgqhgVPAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRvqgadltqmtdkTA 340
Cdd:cd01154 238 TRSVATGEVEF----DDAEAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHR------------RA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 341 PRVTITHHPDVRRSLMTQKAYAEGLRALYLYTA-TFQDAAVAEvvhGVDAKLAvkvnDLMLPVVKGVGSEQAYAKLTESL 419
Cdd:cd01154 302 FGKPLIDHPLMRRDLAEMEVDVEAATALTFRAArAFDRAAADK---PVEAHMA----RLATPVAKLIACKRAAPVTSEAM 374
|
410 420 430
....*....|....*....|....*....|....*...
gi 889629858 420 QTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDF 457
Cdd:cd01154 375 EVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQALDV 412
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
129-454 |
2.33e-44 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 160.91 E-value: 2.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 129 AGGAGFAQILYHLGTEEQK-KWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADGsWHIDGVKRFITSGDSGDLFe 207
Cdd:cd00567 39 LGLLLGAALLLAYGTEEQKeRYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDG-YVLNGRKIFISNGGDADLF- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 208 nifhLVLARPEGAGPGTKGLSLYFVPKflfdvetgepgERNGVFVTNVEHKMGLKVSATCELAFgqHGVPA-KGWLVGEV 286
Cdd:cd00567 117 ----IVLARTDEEGPGHRGISAFLVPA-----------DTPGVTVGRIWDKMGMRGSGTGELVF--DDVRVpEDNLLGEE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 287 HNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGAdltqmtdktaprVTITHHPDVRRSL--MTQKAYAeg 364
Cdd:cd00567 180 GGGFELAMKGLNVGRLLLAAVALGAARAALDEAVEYAKQRKQFG------------KPLAEFQAVQFKLadMAAELEA-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 365 LRALYLYTATFQDAAVAEVVhgvdaklavkvndLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDS 444
Cdd:cd00567 246 ARLLLYRAAWLLDQGPDEAR-------------LEAAMAKLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAAR 312
|
330
....*....|
gi 889629858 445 LYEGTTAIQA 454
Cdd:cd00567 313 IAEGTAEIQR 322
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
36-453 |
1.78e-38 |
|
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: 145.87 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 36 DTARDMLAEVSRLAEGPVAESFVEGDRnppvfdpktHSVMLPESFKKsvnaMLEAGWDKVGIDEALGGMPMPK-AVVWAL 114
Cdd:cd01158 1 EEHQMIRKTVRDFAEKEIAPLAAEMDE---------KGEFPREVIKE----MAELGLMGIPIPEEYGGAGLDFlAYAIAI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 115 HEHILG-ANPAVWMYAGGAGFAQILYHLGTEEQK-KWAV-LAAERGWGStMVLTEPDAGSDVGAARTKAVQQADgSWHID 191
Cdd:cd01158 68 EELAKVdASVAVIVSVHNSLGANPIIKFGTEEQKkKYLPpLATGEKIGA-FALSEPGAGSDAAALKTTAKKDGD-DYVLN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 192 GVKRFITSGDSGDLFenifhLVLARPEGAgPGTKGLSLYFVPKflfdvetGEPgernGVFVTNVEHKMGLKVSATCELAF 271
Cdd:cd01158 146 GSKMWITNGGEADFY-----IVFAVTDPS-KGYRGITAFIVER-------DTP----GLSVGKKEDKLGIRGSSTTELIF 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 272 GQHGVPAKGwLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGADLtqmtdktaprvtITHHPDV 351
Cdd:cd01158 209 EDVRVPKEN-ILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKP------------IADFQGI 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 352 RRSLMTQKAYAEGLRALYLYTATFQDAAVAEVVHGVDAKLAvkvndlmlpvvkgvGSEQAYAKLTESLQTLGGSGFLQDY 431
Cdd:cd01158 276 QFKLADMATEIEAARLLTYKAARLKDNGEPFIKEAAMAKLF--------------ASEVAMRVTTDAVQIFGGYGYTKDY 341
|
410 420
....*....|....*....|..
gi 889629858 432 PIEQYIRDAKIDSLYEGTTAIQ 453
Cdd:cd01158 342 PVERYYRDAKITEIYEGTSEIQ 363
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
87-452 |
8.56e-31 |
|
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: 124.15 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 87 MLEAGWDKVGIDEALGGMPMP---KAVVWALHEHILGANPAVWMYAGGAGfaQILYHLGTEEQKKWAV--LAAERGWGSt 161
Cdd:cd01160 39 AGEQGLLGVGFPEEYGGIGGDllsAAVLWEELARAGGSGPGLSLHTDIVS--PYITRAGSPEQKERVLpqMVAGKKIGA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 162 MVLTEPDAGSDVGAARTKAVQQADgSWHIDGVKRFITSGDSGDLFenifhLVLARPEGAGPGTKGLSLyfvpkflFDVET 241
Cdd:cd01160 116 IAMTEPGAGSDLQGIRTTARKDGD-HYVLNGSKTFITNGMLADVV-----IVVARTGGEARGAGGISL-------FLVER 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 242 GEPGerngVFVTNVEHKMGLKVSATCELAFGQHGVPAKGwLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQ 321
Cdd:cd01160 183 GTPG----FSRGRKLKKMGWKAQDTAELFFDDCRVPAEN-LLGEENKGFYYLMQNLPQERLLIAAGALAAAEFMLEETRN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 322 YAKSRvqgadltqmtdkTAPRVTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDAAVAEVVHGVDAKlaVKVNDLMLP 401
Cdd:cd01160 258 YVKQR------------KAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAEASMAK--YWATELQNR 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 889629858 402 VVkgvgseqayaklTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAI 452
Cdd:cd01160 324 VA------------YECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEI 362
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
131-452 |
5.94e-30 |
|
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: 122.19 E-value: 5.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 131 GAGFAQILYHlGTEEQKKWAV--LAAERgWGSTMVLTEPDAGSDVGAARTKAVQQADGS-WHIDGVKRFITSGDSGDLFe 207
Cdd:cd01161 111 SIGFKGILLF-GTEAQKEKYLpkLASGE-WIAAFALTEPSSGSDAASIRTTAVLSEDGKhYVLNGSKIWITNGGIADIF- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 208 nifhLVLARPE---GAGPGTKGLSLYFVPKFLFDVETGEPgerngvfvtnvEHKMGLKVSATCELAFGQHGVPAKGwLVG 284
Cdd:cd01161 188 ----TVFAKTEvkdATGSVKDKITAFIVERSFGGVTNGPP-----------EKKMGIKGSNTAEVYFEDVKIPVEN-VLG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 285 EVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQG----ADLTQMTDKTAprvtithhpdvrrsLMTQKA 360
Cdd:cd01161 252 EVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFgkkiHEFGLIQEKLA--------------NMAILQ 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 361 YAEGLRAlYLYTATFQDAAVAEvvHGVDAKLavkvndlmlpvVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDA 440
Cdd:cd01161 318 YATESMA-YMTSGNMDRGLKAE--YQIEAAI-----------SKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDL 383
|
330
....*....|..
gi 889629858 441 KIDSLYEGTTAI 452
Cdd:cd01161 384 RIFRIFEGTNEI 395
|
|
| Acyl-CoA_dh_C |
pfam12806 |
Acetyl-CoA dehydrogenase C-terminal like; this domain would appear to be the very C-terminal ... |
475-606 |
4.34e-28 |
|
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: 109.17 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 475 GQIQEFVDSGAGNGRLKTERALLAKALTDVQGMAAALTGYLMAAQQDvtslyKVGLGSVRFLMSVGDLIIGWLLQRQAAV 554
Cdd:pfam12806 2 AEIRAFIAAAAGDPALAAEAAALAAALAALQEATAWLLARAAKGDPD-----EAGAGAVPYLMLFGDVVLGWLWLRQALA 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 889629858 555 AVAALDAGatGDERSFYEGKVAVASFFAKNFLPLLTSTREVIETLDNDIMEL 606
Cdd:pfam12806 77 AQAKLAAG--AKDAAFYEGKIATARFFAERVLPRTAALAAAIEAGDDSLMAL 126
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
122-452 |
2.41e-20 |
|
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: 93.28 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 122 NPAVWMyaggagfaqiLYHLGTEEQKK-WAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADgSWHIDGVKRFITSG 200
Cdd:cd01162 87 NMCAWM----------IDSFGNDEQRErFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD-HYVLNGSKAFISGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 201 DSGDLFenifhLVLARPEGAGPgtKGLSLYFVPKflfdvetGEPGERNGvfvtNVEHKMGLKVSATCELAFGQHGVPAKG 280
Cdd:cd01162 156 GDSDVY-----VVMARTGGEGP--KGISCFVVEK-------GTPGLSFG----ANEKKMGWNAQPTRAVIFEDCRVPVEN 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 281 WLVGEvhngiAQMFeVIEQARMMVGTKAIATLSTG-----YLNALQYAKSRVQGADltqmtdktaprvTITHHPDVRRSL 355
Cdd:cd01162 218 RLGGE-----GQGF-GIAMAGLNGGRLNIASCSLGaaqaaLDLARAYLEERKQFGK------------PLADFQALQFKL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 356 mtqkayAEGLRALYLYTATFQDAAVAevvhgVDAKLAVKVndLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQ 435
Cdd:cd01162 280 ------ADMATELVASRLMVRRAASA-----LDRGDPDAV--KLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQ 346
|
330
....*....|....*..
gi 889629858 436 YIRDAKIDSLYEGTTAI 452
Cdd:cd01162 347 YVRDLRVHQILEGTNEI 363
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
144-453 |
8.42e-19 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 88.80 E-value: 8.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 144 EEQKKWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAVQQADgSWHIDGVKRFITSGDSGDLFenifhLVLAR--PEGAG 221
Cdd:cd01157 100 EQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGD-EYIINGQKMWITNGGKANWY-----FLLARsdPDPKC 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 222 PGTKGLSlyfvpkfLFDVETGEPGERNGvfvtNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEvHNGIAQMFEVIEQAR 301
Cdd:cd01157 174 PASKAFT-------GFIVEADTPGIQPG----RKELNMGQRCSDTRGITFEDVRVPKENVLIGE-GAGFKIAMGAFDKTR 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 302 MMVGTKAIATLSTGYLNALQYAKSRvqgadltqmtdKTAPRVtITHHPDVRRSLMTQKAYAEGLRALYLYTATfqdaava 381
Cdd:cd01157 242 PPVAAGAVGLAQRALDEATKYALER-----------KTFGKL-IAEHQAVSFMLADMAMKVELARLAYQRAAW------- 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 889629858 382 EVVHGVDaklavkvNDLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQ 453
Cdd:cd01157 303 EVDSGRR-------NTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQ 367
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
77-453 |
5.58e-18 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 86.04 E-value: 5.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 77 PESFkksVNAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHI--LGAnPAVWMYAGGAGFAQILYHlGTEEQKKwAVLAA 154
Cdd:PRK03354 39 PERF---VKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELgrLGA-PTYVLYQLPGGFNTFLRE-GTQEQID-KIMAF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 155 eRGWGSTM---VLTEPDAGSDVGAARTkAVQQADGSWHIDGVKRFITSGdsgdlfENIFHLVLARPEGAGPGTKGLSLYF 231
Cdd:PRK03354 113 -RGTGKQMwnsAITEPGAGSDVGSLKT-TYTRRNGKVYLNGSKCFITSS------AYTPYIVVMARDGASPDKPVYTEWF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 232 vpkflfdVETGEPGERNGVFvtnveHKMGLKVSATCELAFGQHGVPAKGwLVGEVHNGIAQMFEVIEQARMMVGTKAIAT 311
Cdd:PRK03354 185 -------VDMSKPGIKVTKL-----EKLGLRMDSCCEITFDDVELDEKD-MFGREGNGFNRVKEEFDHERFLVALTNYGT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 312 LSTGYLNALQYAKSRVQGADltqmtdktaprvTITHHPDVRRSLMTQKAYAEGLRALYLYTATFQDaavaevvhgvdakl 391
Cdd:PRK03354 252 AMCAFEDAARYANQRVQFGE------------AIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKAD-------------- 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889629858 392 avkvNDLMLP----VVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQ 453
Cdd:PRK03354 306 ----NGTITSgdaaMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQ 367
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
77-452 |
8.64e-18 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 85.55 E-value: 8.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 77 PESFKKsvnAMLEAGWDKVGIDEALGGMPMPKAVVWALHEHILGANPAVWMYAGGAGFAQILyHLGTEEQKKWAVLAA-E 155
Cdd:PRK12341 39 PREFMR---ALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLITNGQCIHSMR-RFGSAEQLRKTAESTlE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 156 RGW-GSTMVLTEPDAGSDVGAARTKAVQQaDGSWHIDGVKRFITSGdsgdlFENIFHLVLAR-PEGAGPgTKGLSLYFVP 233
Cdd:PRK12341 115 TGDpAYALALTEPGAGSDNNSATTTYTRK-NGKVYLNGQKTFITGA-----KEYPYMLVLARdPQPKDP-KKAFTLWWVD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 234 KflfdvetgepgERNGVFVTNVeHKMGLKVSATCELAFGQHGVPAKGwLVGEVHNGIAQMFEVIEQARMmvgtkAIATLS 313
Cdd:PRK12341 188 S-----------SKPGIKINPL-HKIGWHMLSTCEVYLDNVEVEESD-LVGEEGMGFLNVMYNFEMERL-----INAARS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 314 TGYL-----NALQYAKSRVQgadltqmTDKtaprvTITHHPDVRRSLMTQKAYAEGLRALyLYTATFQdaavaevvhgVD 388
Cdd:PRK12341 250 LGFAecafeDAARYANQRIQ-------FGK-----PIGHNQLIQEKLTLMAIKIENMRNM-VYKVAWQ----------AD 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 889629858 389 AKLAVKVNDlmlPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAI 452
Cdd:PRK12341 307 NGQSLRTSA---ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
155-480 |
3.42e-17 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 84.80 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 155 ERGWGSTMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDlfenifHLVLARPEGagpgtkGLSLYFVPK 234
Cdd:PRK11561 175 KRGLLIGMGMTEKQGGSDVLSNTTRAERLADGSYRLVGHKWFFSVPQSDA------HLVLAQAKG------GLSCFFVPR 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 235 FLFDvetgepGERNGVFVTNVEHKMGLKVSATCELAFGQhgvpAKGWLVGEVHNGIAQMFEVIEQARMMVGTKAIATLST 314
Cdd:PRK11561 243 FLPD------GQRNAIRLERLKDKLGNRSNASSEVEFQD----AIGWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 315 GYLNALQYAKSR-VQGADLTQmtdktaprvtithHPDVRRSLMTQKAYAEGLRALYLYTATFQDaAVAEVVHGVDAKlav 393
Cdd:PRK11561 313 AFSVAIYHAHQRqVFGKPLIE-------------QPLMRQVLSRMALQLEGQTALLFRLARAWD-RRADAKEALWAR--- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 394 kvndLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQAQDfFFRKIVRDKGV----- 468
Cdd:PRK11561 376 ----LFTPAAKFVICKRGIPFVAEAMEVLGGIGYCEESELPRLYREMPVNSIWEGSGNIMCLD-VLRVLNKQPGVydlls 450
|
330
....*....|...
gi 889629858 469 -ALAHVSGQIQEF 480
Cdd:PRK11561 451 eAFVEVKGQDRHF 463
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
138-334 |
1.05e-16 |
|
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: 82.41 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 138 LYHLGTEEQK-KWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAvQQADGSWHIDGVKRFITSGDSGDLFenifhLVLAR 216
Cdd:cd01151 105 IYDFGSEEQKqKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA-RKDGGGYKLNGSKTWITNSPIADVF-----VVWAR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 217 PEGAGpGTKGlslyfvpkflFDVETGEPGERngvfVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEvhNGIAQMFEV 296
Cdd:cd01151 179 NDETG-KIRG----------FILERGMKGLS----APKIQGKFSLRASITGEIVMDNVFVPEENLLPGA--EGLRGPFKC 241
|
170 180 190
....*....|....*....|....*....|....*....
gi 889629858 297 IEQARMMVGTKAIATLSTGYLNALQYAKSRVQ-GADLTQ 334
Cdd:cd01151 242 LNNARYGIAWGALGAAEDCYHTARQYVLDRKQfGRPLAA 280
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
138-453 |
2.53e-16 |
|
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: 80.92 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 138 LYHLGTEEQKKWAVLAAERG-WGSTMVLTEPDAGSDVGAARTKAvQQADGSWHIDGVKRFITSGDSGDLFenifhLVLAR 216
Cdd:cd01156 95 IYRNGSAAQKEKYLPKLISGeHIGALAMSEPNAGSDVVSMKLRA-EKKGDRYVLNGSKMWITNGPDADTL-----VVYAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 217 pEGAGPGTKGLSlyfvpkfLFDVETGEPGerngvFVTNVE-HKMGLKVSATCELAFGQHGVPAKGwLVGEVHNGIAQMFE 295
Cdd:cd01156 169 -TDPSAGAHGIT-------AFIVEKGMPG-----FSRAQKlDKLGMRGSNTCELVFEDCEVPEEN-ILGGENKGVYVLMS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 296 VIEQARMMVGTKAIATLSTGYLNALQYAKSRVQ-G---ADLTQMTDKTAprvtithhpDVRRSLMTQKAYA-EGLRALYL 370
Cdd:cd01156 235 GLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQfGqpiGEFQLVQGKLA---------DMYTRLNASRSYLyTVAKACDR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 371 YTATFQDAAvaevvhgvdaklavkvndlmlpvvkGV---GSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKidsLYE 447
Cdd:cd01156 306 GNMDPKDAA-------------------------GVilyAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAK---LYE 357
|
....*....
gi 889629858 448 ---GTTAIQ 453
Cdd:cd01156 358 igaGTSEIR 366
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
161-271 |
4.50e-15 |
|
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: 70.77 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 161 TMVLTEPDAGSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFenifhLVLARPEGAGpGTKGLSLYFVPKflfdve 240
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGDGGGWVLNGTKWWITNAGIADLF-----LVLARTGGDD-RHGGISLFLVPK------ 68
|
90 100 110
....*....|....*....|....*....|.
gi 889629858 241 tgepgERNGVFVTNVEHKMGLKVSATCELAF 271
Cdd:pfam02770 69 -----DAPGVSVRRIETKLGVRGLPTGELVF 94
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
95-449 |
9.50e-14 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 73.43 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 95 VGIDEALGGMPMPKAVVWALHEHILGANPAVWM--YAGGAGFAQILYHLGTEEQK-KW--AVLAAERGwgSTMVLTEPDA 169
Cdd:PTZ00461 85 VTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLayLAHSMLFVNNFYYSASPAQRaRWlpKVLTGEHV--GAMGMSEPGA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 170 GSDVGAARTKAVQQADGSWHIDGVKRFITSGDSGDLFenifhLVLARPEGAGPGtkglslyfvpkflFDVETGEPGERNG 249
Cdd:PTZ00461 163 GTDVLGMRTTAKKDSNGNYVLNGSKIWITNGTVADVF-----LIYAKVDGKITA-------------FVVERGTKGFTQG 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 250 VFVTnvehKMGLKVSATCELAFGQHGVPAKGwLVGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRvqg 329
Cdd:PTZ00461 225 PKID----KCGMRASHMCQLFFEDVVVPAEN-LLGEEGKGMVGMMRNLELERVTLAAMAVGIAERSVELMTSYASER--- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 330 adltqmtdkTAPRVTITHHPDVRRSLMTQKAYAEGLRALyLYTATFQDAAVAEVVHGVDA-KLavkvndLMLPVVKGVGS 408
Cdd:PTZ00461 297 ---------KAFGKPISNFGQIQRYIAEGYADTEAAKAL-VYSVSHNVHPGNKNRLGSDAaKL------FATPIAKKVAD 360
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 889629858 409 eqayakltESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGT 449
Cdd:PTZ00461 361 --------SAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
86-453 |
5.47e-13 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 70.84 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 86 AMLEAGWDKVGIDEALGGM--PMPKAVVWALHEHILGANPAVWMYAGGAGFAQILYHlGTEEQKKW---AVLAAERGWgs 160
Cdd:cd01152 43 ALAAAGWAAPGWPKEYGGRgaSLMEQLIFREEMAAAGAPVPFNQIGIDLAGPTILAY-GTDEQKRRflpPILSGEEIW-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 161 TMVLTEPDAGSDVGAARTKAVQQADGsWHIDGVKRFITSGDSGDlfeniFHLVLARPEGAGPGTKGLSLYFVPkflFDVE 240
Cdd:cd01152 120 CQGFSEPGAGSDLAGLRTRAVRDGDD-WVVNGQKIWTSGAHYAD-----WAWLLVRTDPEAPKHRGISILLVD---MDSP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 241 tgepgernGVFVTNVEHKMGlkVSATCELAFGQHGVPAkGWLVGEVHNGIAQMFEVIEQARMMVGtkaiATLSTGYLNAL 320
Cdd:cd01152 191 --------GVTVRPIRSING--GEFFNEVFLDDVRVPD-ANRVGEVNDGWKVAMTTLNFERVSIG----GSAATFFELLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 321 QYAKSrVQGADLTQMTDktaprvtithhPDVRRSLMTQKAYAEGLRALYLYTATFQDAAvaevvhgvdaklavKVNDLML 400
Cdd:cd01152 256 ARLLL-LTRDGRPLIDD-----------PLVRQRLARLEAEAEALRLLVFRLASALAAG--------------KPPGAEA 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 889629858 401 PVVKGVGSE--QAYAKLteSLQTLGGSGFLQDYP--------IEQYIRDAKIDSLYEGTTAIQ 453
Cdd:cd01152 310 SIAKLFGSElaQELAEL--ALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQ 370
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
162-453 |
2.51e-12 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 69.14 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 162 MVLTEPDAGSDVGAARTKAvQQADGSWHIDGVKRFITSGDSGDLFenifhLVLARPEGAGpGTKGLSLyfvpkflFDVET 241
Cdd:PLN02519 146 LAMSEPNSGSDVVSMKCKA-ERVDGGYVLNGNKMWCTNGPVAQTL-----VVYAKTDVAA-GSKGITA-------FIIEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 242 GEPGerngvFVTNVE-HKMGLKVSATCELAFGQHGVPAKGWLvGEVHNGIAQMFEVIEQARMMVGTKAIATLSTGYLNAL 320
Cdd:PLN02519 212 GMPG-----FSTAQKlDKLGMRGSDTCELVFENCFVPEENVL-GQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVL 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 321 QYAKSRVQG----ADLTQMTDKTAprvtithhpDVRRSLMTQKAYaeglralylytatfqdaaVAEVVHGVDAKlavKVN 396
Cdd:PLN02519 286 PYVRQREQFgrpiGEFQFIQGKLA---------DMYTSLQSSRSY------------------VYSVARDCDNG---KVD 335
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 889629858 397 DLMLPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQ 453
Cdd:PLN02519 336 RKDCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIR 392
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
287-453 |
5.11e-12 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 63.81 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 287 HNGIAQMFEVIEQARMMVGTKAIATLSTGYLNALQYAKSRVQGAdltqmtdktaprVTITHHPDVRRSLMTQKAYAEGLR 366
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFG------------RPLIDFQLVRHKLAEMAAEIEAAR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 367 ALYLYTATFQDAavaevvhGVDAKLAVkvndlmlPVVKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLY 446
Cdd:pfam00441 69 LLVYRAAEALDA-------GGPDGAEA-------SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIG 134
|
....*..
gi 889629858 447 EGTTAIQ 453
Cdd:pfam00441 135 EGTSEIQ 141
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
141-454 |
9.01e-12 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 67.19 E-value: 9.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 141 LGTEEQK-KWAVLAAERGWGSTMVLTEPDAGSDVGAARTKAvQQADGSWHIDGVKRFITSGDSGDLFenifhLVLARpeg 219
Cdd:PLN02526 124 CGSEAQKqKYLPSLAQLDTVACWALTEPDYGSDASSLNTTA-TKVEGGWILNGQKRWIGNSTFADVL-----VIFAR--- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 220 aGPGTKGLSLYFVPKflfdvetGEPGERngvfVTNVEHKMGLKVSATCELAFGQHGVPAKGWLVGEvhNGIAQMFEVIEQ 299
Cdd:PLN02526 195 -NTTTNQINGFIVKK-------GAPGLK----ATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV--NSFQDTNKVLAV 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 889629858 300 ARMMVGTKAIATLSTGYLNALQYAKSRVQ-GADLTQMtdktaprvTITHHPDVRRSLMTQKAYAEGLRALYLYTAtfqda 378
Cdd:PLN02526 261 SRVMVAWQPIGISMGVYDMCHRYLKERKQfGAPLAAF--------QINQEKLVRMLGNIQAMFLVGWRLCKLYES----- 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 889629858 379 avAEVVHGvDAKLAvkvndlmlpvvKGVGSEQAYAKLTESLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQA 454
Cdd:PLN02526 328 --GKMTPG-HASLG-----------KAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINA 389
|
|
| AcylCoA_DH_N |
pfam12418 |
Acyl-CoA dehydrogenase N terminal; This domain family is found in bacteria and eukaryotes, and ... |
3-34 |
5.12e-07 |
|
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: 46.18 E-value: 5.12e-07
10 20 30
....*....|....*....|....*....|..
gi 889629858 3 HYRSNVRDQVFNLFEVLGVDKALGHGEFSDVD 34
Cdd:pfam12418 1 SYKAPLRDMRFVLYEVLGAEALAALPGFADAD 32
|
|
| |
