|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
4-380 |
5.22e-65 |
|
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: 211.62 E-value: 5.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 4 TKTKTDYIALAHELAPR-FAERARQHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAF 82
Cdd:COG1960 6 TEEQRALRDEVREFAEEeIAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 83 AVNMHVHGLAMIARLGGAS--AEWaCRAVVDGAVISG-GFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATH 159
Cdd:COG1960 86 PVGVHNGAAEALLRFGTEEqkERY-LPRLASGEWIGAfALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 160 LFLSAATLDDRGLPQPMAFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCS 239
Cdd:COG1960 165 ILVLARTDPAAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 240 FASCFVGIARAALDHVVATQKKRIisVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAIHAeHDDVDPLAhyIDMSVMK 319
Cdd:COG1960 245 LAAQALGIAEAALELAVAYARERE--QFGRPIADFQAVQHRLADMAAELEAARALVYRAAWL-LDAGEDAA--LEAAMAK 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929020708 320 SSVTKLAHEVLTLGMQVQGGSGLSSADPLQRMYRDVVAGLLVPPATDVVQEWAGKQALGVP 380
Cdd:COG1960 320 LFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRP 380
|
|
| NcnH |
cd01159 |
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ... |
14-358 |
4.53e-35 |
|
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.
Pssm-ID: 173848 [Multi-domain] Cd Length: 370 Bit Score: 132.47 E-value: 4.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 14 AHELAPRFAERARQHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTA---FAVNMHVHG 90
Cdd:cd01159 3 AEDLAPLIRERAPEAERARRLPDEVVRALREIGFFRMFVPKRYGGLEGDFAEFAEAIATLAEACGSAAwvaSIVATHSRM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 91 LAMIARLGGASAeWAcravvDG--AVISGGFSepgvggnwwhPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAATLD 168
Cdd:cd01159 83 LAAFPPEAQEEV-WG-----DGpdTLLAGSYA----------PGGRAERVDGGYRVSGTWPFASGCDHADWILVGAIVED 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 169 DRGLPQPMAFLVPKPEqgVRVVGEWDAAGMRATGSHSLALEDLYIEDKW----SVGERGTLPMLFMMGVHWAW-----CS 239
Cdd:cd01159 147 DDGGPLPRAFVVPRAE--YEIVDTWHVVGLRGTGSNTVVVDDVFVPEHRtltaGDMMAGDGPGGSTPVYRMPLrqvfpLS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 240 FASCFVGIARAALDHVVATQKKRIISV-IGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAI-----HAEHDDVDPLAHYI 313
Cdd:cd01159 225 FAAVSLGAAEGALAEFLELAGKRVRQYgAAVKMAEAPITQLRLAEAAAELDAARAFLERATrdlwaHALAGGPIDVEERA 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 929020708 314 DMSVMKSSVTKLAHEVLTLGMQVQGGSGLSSADPLQRMYRDVVAG 358
Cdd:cd01159 305 RIRRDAAYAAKLSAEAVDRLFHAAGGSALYTASPLQRIWRDIHAA 349
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
90-355 |
1.92e-33 |
|
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: 127.01 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 90 GLAMIARLGGAS--AEWACRAVVDGAVISGGFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAATL 167
Cdd:cd00567 44 GAALLLAYGTEEqkERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLARTD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 168 DDRGLPQPM-AFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASCFVG 246
Cdd:cd00567 124 EEGPGHRGIsAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVALG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 247 IARAALDHVVATQKKRiiSVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAIHAEHDDVDPLAHYIDMSvmKSSVTKLA 326
Cdd:cd00567 204 AARAALDEAVEYAKQR--KQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMA--KLFATEAA 279
|
250 260
....*....|....*....|....*....
gi 929020708 327 HEVLTLGMQVQGGSGLSSADPLQRMYRDV 355
Cdd:cd00567 280 REVADLAMQIHGGRGYSREYPVERYLRDA 308
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
12-272 |
2.05e-29 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 117.04 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 12 ALAHELAPRFAERARQHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHvHGL 91
Cdd:cd01163 1 ARARPLAARIAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH-FGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 92 AMIARLGG--ASAEWACRAVVDGAVISGGFSEPGVGGNWWHpTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAatLDD 169
Cdd:cd01163 80 VEALLLAGpeQFRKRWFGRVLNGWIFGNAVSERGSVRPGTF-LTATVRDGGGYVLNGKKFYSTGALFSDWVTVSA--LDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 170 RGlpQPMAFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVG-----ERGTLPMLFMMGVHwawcsfASCF 244
Cdd:cd01163 157 EG--KLVFAAVPTDRPGITVVDDWDGFGQRLTASGTVTFDNVRVEPDEVLPrpnapDRGTLLTAIYQLVL------AAVL 228
|
250 260 270
....*....|....*....|....*....|
gi 929020708 245 VGIARAALDHVVA--TQKKRIISVIGKPNA 272
Cdd:cd01163 229 AGIARAALDDAVAyvRSRTRPWIHSGAESA 258
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
15-355 |
5.66e-28 |
|
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: 113.13 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 15 HELAPRFAERARQHdadsSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHVH-GLAM 93
Cdd:cd01158 16 KEIAPLAAEMDEKG----EFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSVHNSlGANP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 94 IARLGGAS--AEWACRAVVDGAVISGGFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAATLDDRG 171
Cdd:cd01158 92 IIKFGTEEqkKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSKG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 172 LPQPMAFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASCFVGIARAA 251
Cdd:cd01158 172 YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 252 LDHVVATQKKRIisVIGKPNAHLPGIQFRIaemaakvaaarAHLEAAIHAEH----------DDVDPLAHYIDMSVMKSS 321
Cdd:cd01158 252 LDAAVDYAKERK--QFGKPIADFQGIQFKL-----------ADMATEIEAARlltykaarlkDNGEPFIKEAAMAKLFAS 318
|
330 340 350
....*....|....*....|....*....|....
gi 929020708 322 vtKLAHEVLTLGMQVQGGSGLSSADPLQRMYRDV 355
Cdd:cd01158 319 --EVAMRVTTDAVQIFGGYGYTKDYPVERYYRDA 350
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
16-278 |
4.77e-21 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 93.63 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 16 ELAPRfaerARQHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHVH-GLAMI 94
Cdd:cd01156 20 EIAPL----AAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHSNlCINQI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 95 ARLGGAsaewACRAVVDGAVISG------GFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAATLD 168
Cdd:cd01156 96 YRNGSA----AQKEKYLPKLISGehigalAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVYAKTDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 169 DRGLPQPMAFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASCFVGIA 248
Cdd:cd01156 172 SAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIM 251
|
250 260 270
....*....|....*....|....*....|..
gi 929020708 249 RAALDHVV--ATQKKRiisvIGKPNAHLPGIQ 278
Cdd:cd01156 252 QAALDVAIpyAHQRKQ----FGQPIGEFQLVQ 279
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
14-355 |
2.93e-15 |
|
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: 76.33 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 14 AHELAPRFAErarqHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHVHGLAM 93
Cdd:cd01162 17 AKEMAPHAAD----WDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVSTAAYISIHNMCAWM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 94 IARLGGASA--EWACRAVVDGAVISGGFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGfPGATHLFLSAATLDDRG 171
Cdd:cd01162 93 IDSFGNDEQreRFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISG-AGDSDVYVVMARTGGEG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 172 LPQPMAFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASCFVGIARAA 251
Cdd:cd01162 172 PKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 252 LDHVVATQKKRiiSVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAIHAeHDDVDPLAhyIDMSVM-KSSVTKLAHEVL 330
Cdd:cd01162 252 LDLARAYLEER--KQFGKPLADFQALQFKLADMATELVASRLMVRRAASA-LDRGDPDA--VKLCAMaKRFATDECFDVA 326
|
330 340
....*....|....*....|....*
gi 929020708 331 TLGMQVQGGSGLSSADPLQRMYRDV 355
Cdd:cd01162 327 NQALQLHGGYGYLKDYPVEQYVRDL 351
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
22-269 |
4.38e-13 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 69.91 E-value: 4.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 22 AERARQHDADSSFPHE-NIAELVSS-GYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHVH-GLAMIARLG 98
Cdd:PLN02519 46 APHAAAIDATNSFPKDvNLWKLMGDfNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNlCINQLVRNG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 99 GAsaewACRAVVDGAVISG------GFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAATLDDRGL 172
Cdd:PLN02519 126 TP----AQKEKYLPKLISGehvgalAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 173 PQPMAFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASCFVGIARAAL 252
Cdd:PLN02519 202 KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACL 281
|
250
....*....|....*....
gi 929020708 253 DHVV--ATQKKRIISVIGK 269
Cdd:PLN02519 282 DVVLpyVRQREQFGRPIGE 300
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
18-354 |
5.60e-12 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 66.88 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 18 APRFAERARQHDADSSFPHENIAELVSSGYTAMTVPAEFGGD--NATLAELC--EAQQILAGGC----ASTAFAVNMHVH 89
Cdd:PTZ00461 53 REVVDKHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAgmDAVAAVIIhhELSKYDPGFClaylAHSMLFVNNFYY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 90 GLAMIARlggasAEWACRAVVDGAVISGGFSEPGVGGN-WWHPTTRAEEVDGGFKLNGFKGFFTGFPGAThLFLSAATLD 168
Cdd:PTZ00461 133 SASPAQR-----ARWLPKVLTGEHVGAMGMSEPGAGTDvLGMRTTAKKDSNGNYVLNGSKIWITNGTVAD-VFLIYAKVD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 169 DRglpqPMAFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASCFVGIA 248
Cdd:PTZ00461 207 GK----ITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 249 RAALDHVVATQKKRiiSVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAIHAEHDDVDplaHYIDMSVMKSSVTKLAHE 328
Cdd:PTZ00461 283 ERSVELMTSYASER--KAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNK---NRLGSDAAKLFATPIAKK 357
|
330 340
....*....|....*....|....*.
gi 929020708 329 VLTLGMQVQGGSGLSSADPLQRMYRD 354
Cdd:PTZ00461 358 VADSAIQVMGGMGYSRDMPVERLWRD 383
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
29-355 |
1.22e-09 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 59.36 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 29 DADSSFPHENIAELVSSGYTAMTVPAEFGG---DNATL----AELCEaqqilaggCASTAFavnMHVHGLAMIARLGGAS 101
Cdd:PRK12341 33 DENGTYPREFMRALADNGISMLGVPEEFGGtpaDYVTQmlvlEEVSK--------CGAPAF---LITNGQCIHSMRRFGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 102 AEwACRAVVDGAVISG------GFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAATLDDRGLPQP 175
Cdd:PRK12341 102 AE-QLRKTAESTLETGdpayalALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKDPKKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 176 MA-FLVPKPEQGVRvVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASCFVGIARAALDH 254
Cdd:PRK12341 181 FTlWWVDSSKPGIK-INPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFED 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 255 VVATQKKRIisVIGKPNAHLPGIQFRIaemaakvaaarAHLEAAIHAEHDDVDPLAHYID--MSVMKSS-VTKL-----A 326
Cdd:PRK12341 260 AARYANQRI--QFGKPIGHNQLIQEKL-----------TLMAIKIENMRNMVYKVAWQADngQSLRTSAaLAKLycartA 326
|
330 340
....*....|....*....|....*....
gi 929020708 327 HEVLTLGMQVQGGSGLSSADPLQRMYRDV 355
Cdd:PRK12341 327 MEVIDDAIQIMGGLGYTDEARVSRFWRDV 355
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
118-209 |
1.49e-09 |
|
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: 54.59 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 118 GFSEPGVGGNWWHPTTRAEEVDGG-FKLNGFKGFFTGFPGATHLFLSAATLDDRGLPQPMAFLVPKPEQGVRVVGEWDAA 196
Cdd:pfam02770 3 ALTEPGAGSDVASLKTTAADGDGGgWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKDAPGVSVRRIETKL 82
|
90
....*....|...
gi 929020708 197 GMRATGSHSLALE 209
Cdd:pfam02770 83 GVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
13-98 |
9.91e-09 |
|
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: 52.85 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 13 LAHELAPRfaerARQHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHvHGLA 92
Cdd:pfam02771 15 AEEEIAPH----AAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALSVH-SSLG 89
|
....*...
gi 929020708 93 M--IARLG 98
Cdd:pfam02771 90 AppILRFG 97
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
15-354 |
8.10e-08 |
|
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: 53.74 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 15 HELAPRFAER-----ARQHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHVH 89
Cdd:cd01157 9 QETARKFAREeiipvAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEANSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 90 GLAMIArLGGASAE---WACRAVVDGAVISGGFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAAT 166
Cdd:cd01157 89 GQMPVI-ISGNDEQkkkYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 167 LDDRGLPQPMAF---LVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASC 243
Cdd:cd01157 168 DPDPKCPASKAFtgfIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 244 FVGIARAALDHVVATQKKRiiSVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAIHaEHDDVDPLAHYidMSVMKSSVT 323
Cdd:cd01157 248 AVGLAQRALDEATKYALER--KTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAW-EVDSGRRNTYY--ASIAKAFAA 322
|
330 340 350
....*....|....*....|....*....|.
gi 929020708 324 KLAHEVLTLGMQVQGGSGLSSADPLQRMYRD 354
Cdd:cd01157 323 DIANQLATDAVQIFGGNGFNSEYPVEKLMRD 353
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
16-355 |
3.24e-07 |
|
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: 52.01 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 16 ELAPRFAERARQ----HDADSSFP---HENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHV 88
Cdd:cd01153 12 VLAPLNADGDREgpvfDDGRVVVPppfKEALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 89 HGLAMIARLGGA-SAEWACRAVVDGAVISGGFSEPGVGGNWWHPTTRAE-EVDGGFKLNGFKGFFTGFPGAT-----HLF 161
Cdd:cd01153 92 AAATLLAHGTEAqREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVyQADGSWRINGVKRFISAGEHDMsenivHLV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 162 LS---AATLDDRGLPqpmAFLVPK-----PEQGVRVVGEWDAAGMRATGSHSLALEDLYIEdkwSVGERGT-LPMLFMMg 232
Cdd:cd01153 172 LArseGAPPGVKGLS---LFLVPKflddgERNGVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMgLAQMFAM- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 233 VHWAWCSFASCFVGIARAALDHVVATQKKR------IISVIGKPNAHLPGI------QFRIAEMAAKVAAARAHLEAAIH 300
Cdd:cd01153 245 MNGARLGVGTQGTGLAEAAYLNALAYAKERkqggdlIKAAPAVTIIHHPDVrrslmtQKAYAEGSRALDLYTATVQDLAE 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 301 AEHDDVDPLAHYIDMS-----VMKSSVTKLAHEVLTLGMQVQGGSGLSSADPLQRMYRDV 355
Cdd:cd01153 325 RKATEGEDRKALSALAdlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDA 384
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
13-375 |
4.76e-07 |
|
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: 51.35 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 13 LAHELAPRfaerARQHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNAT-LAELCEAQQILAGGCASTAFAVNMHVhGL 91
Cdd:cd01160 14 FAKEVAPF----HHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDlLSAAVLWEELARAGGSGPGLSLHTDI-VS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 92 AMIARLGG-ASAEWACRAVVDGAVISG-GFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAATL-D 168
Cdd:cd01160 89 PYITRAGSpEQKERVLPQMVAGKKIGAiAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGgE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 169 DRGLPQPMAFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLPMLFMMGVHWAWCSFASCFVGIA 248
Cdd:cd01160 169 ARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 249 RAALDHVVATQKKRiiSVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAIHAEHDDVDPLAHyidMSVMKSSVTKLAHE 328
Cdd:cd01160 249 EFMLEETRNYVKQR--KAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLDVAE---ASMAKYWATELQNR 323
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 929020708 329 VLTLGMQVQGGSGLSSADPLQRMYRDVVAGLLVPPATDVVQEWAGKQ 375
Cdd:cd01160 324 VAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
239-358 |
1.56e-06 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 46.96 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 239 SFASCFVGIARAALDHVVATQKKRIISVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAIHAEHDDVD-----PLAHYI 313
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRAYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAagkpvTPALRA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 929020708 314 DMSVMKSSVTKLAHEVLTLGMQVQGGSGLSSADPLQRMYRDVVAG 358
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAA 125
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
26-355 |
1.80e-06 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 49.44 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 26 RQHDADSSFPHENIAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTaFAVNMHVHGLAMIARLGGASAEWA 105
Cdd:PRK03354 30 AECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPT-YVLYQLPGGFNTFLREGTQEQIDK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 106 CRAVVDGA--VISGGFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAATLDDRGLPQPMAFLVPKP 183
Cdd:PRK03354 109 IMAFRGTGkqMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDMS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 184 EQGVRVvGEWDAAGMRATGSHSLALEDLYIEDKWSVGERGTLpmlFMMGV----HWAWCsFASCFVGIARAALDHVVATQ 259
Cdd:PRK03354 189 KPGIKV-TKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNG---FNRVKeefdHERFL-VALTNYGTAMCAFEDAARYA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 260 KKRIisVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAI-HAEHDDVDPLahyiDMSVMKSSVTKLAHEVLTLGMQVQG 338
Cdd:PRK03354 264 NQRV--QFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAwKADNGTITSG----DAAMCKYFCANAAFEVVDSAMQVLG 337
|
330
....*....|....*..
gi 929020708 339 GSGLSSADPLQRMYRDV 355
Cdd:PRK03354 338 GVGIAGNHRISRFWRDL 354
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
245-355 |
1.36e-05 |
|
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: 44.55 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 245 VGIARAALDHVVATQKKRiiSVIGKPNAHLPGIQFRIAEMAAKVAAARAHLEAAIHAEHDDVDPLAhyiDMSVMKSSVTK 324
Cdd:pfam00441 23 LGLARRALDEALAYARRR--KAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDAGGPDGA---EASMAKLYASE 97
|
90 100 110
....*....|....*....|....*....|.
gi 929020708 325 LAHEVLTLGMQVQGGSGLSSADPLQRMYRDV 355
Cdd:pfam00441 98 AAVEVADLAMQLHGGYGYLREYPVERLYRDA 128
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
124-354 |
3.67e-04 |
|
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: 42.36 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 124 VGGNwwhpTTRAEEVDGGF-KLNGFKGFFTGFPGATHLFLSAATLDDRGLPQPMAFLVPK-----PEQGVRVVGEWDAAG 197
Cdd:cd01154 162 LGAN----ETTAERSGGGVyRLNGHKWFASAPLADAALVLARPEGAPAGARGLSLFLVPRlledgTRNGYRIRRLKDKLG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 198 MRATGSHSLALEDlyiEDKWSVGE--RGTLPMLFMMGVHWAWCSFAScfVGIARAALDHVVATQKKRiiSVIGKPNAHLP 275
Cdd:cd01154 238 TRSVATGEVEFDD---AEAYLIGDegKGIYYILEMLNISRLDNAVAA--LGIMRRALSEAYHYARHR--RAFGKPLIDHP 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 276 GIQFRIAEMAAKVAAARAHLEAAI----HAEHDDVDPlAHY--IDMSVMKSSVTKLAHEVLTLGMQVQGGSGLSSADPLQ 349
Cdd:cd01154 311 LMRRDLAEMEVDVEAATALTFRAArafdRAAADKPVE-AHMarLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVA 389
|
....*
gi 929020708 350 RMYRD 354
Cdd:cd01154 390 RLHRE 394
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
13-215 |
4.02e-03 |
|
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: 38.88 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 13 LAHELAPRFAERARqhdaDSSFPHENIAELVSSGYTAMTvPAEFGGDNATLAE---LCEAQQILAGGCASTafavnMHVH 89
Cdd:cd01151 28 CQEELAPRVLEAYR----EEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAyglIAREVERVDSGYRSF-----MSVQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 90 G-LAM--IARLGG-----------ASAEWAcravvdGAVisgGFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFP 155
Cdd:cd01151 98 SsLVMlpIYDFGSeeqkqkylpklASGELI------GCF---GLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929020708 156 GATHLFLSAATLDD---RGlpqpmaFLVPKPEQGVRVVGEWDAAGMRATGSHSLALEDLYIED 215
Cdd:cd01151 169 IADVFVVWARNDETgkiRG------FILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPE 225
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
13-223 |
9.01e-03 |
|
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: 37.71 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 13 LAHELAPRFAERARQHDADSSFPHEN-IAELVSSGYTAMTVPAEFGGDNATLAELCEAQQILAGGCASTAFAVNMHVHGL 91
Cdd:cd01152 14 LAAHLPPELREESALGYREGREDRRRwQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAAAGAPVPFNQIGIDLAG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929020708 92 AMIARLGgasAEWACRAVVDgAVISG------GFSEPGVGGNWWHPTTRAEEVDGGFKLNGFKGFFTGFPGATHLFLSAA 165
Cdd:cd01152 94 PTILAYG---TDEQKRRFLP-PILSGeeiwcqGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAHYADWAWLLVR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929020708 166 TLDD----RGLPqpmAFLVPKPEQGVRVvgewdaAGMR-ATGSHSLA---LEDLYIEDKWSVGERG 223
Cdd:cd01152 170 TDPEapkhRGIS---ILLVDMDSPGVTV------RPIRsINGGEFFNevfLDDVRVPDANRVGEVN 226
|
|
| |
