|
Name |
Accession |
Description |
Interval |
E-value |
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
72-481 |
0e+00 |
|
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: 745.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 72 SFAVAMFKGQLATDQVFPYPSVLNQEQTEFLKELVEPVSRFFEEVNDPAKNDTLEMVEETTLQGLKELGAFGLQVPSELG 151
Cdd:cd01161 1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 152 GVGLCNTQYARLVEIVGMhDLAVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTS 231
Cdd:cd01161 81 GLGLNNTQYARLAEIVGM-DLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 232 AVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPaTGAVKEKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVF 311
Cdd:cd01161 160 AVLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDA-TGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 312 FDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQY 391
Cdd:cd01161 239 FEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 392 VTESMAYMVSANMDQGST-DFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01161 319 ATESMAYMTSGNMDRGLKaEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRL 398
|
410
....*....|.
gi 966994270 471 FVALQGCMDKG 481
Cdd:cd01161 399 FIALTGLQHAG 409
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
94-473 |
3.33e-135 |
|
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: 401.14 E-value: 3.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 94 LNQEQTEFLKElvepVSRFFEEVNDP--AKNDTLEMVEETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHD 171
Cdd:COG1960 5 LTEEQRALRDE----VREFAEEEIAPeaREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 172 LAVGITLGAHQSIGfKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 251
Cdd:COG1960 81 ASLALPVGVHNGAA-EALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRD--GDGYVLNGQKTFIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 252 NGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:COG1960 158 NAPVADVILVLART---DPAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 332 VAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGsTDF 411
Cdd:COG1960 233 IAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAG-EDA 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966994270 412 QIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:COG1960 312 ALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
103-473 |
3.26e-122 |
|
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: 367.75 E-value: 3.26e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 103 KELVEPVSRFFEEVNDP--AKNDTLEMVEETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLAVGITLGA 180
Cdd:cd01158 4 QMIRKTVRDFAEKEIAPlaAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVIVSV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 181 HQSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFT 260
Cdd:cd01158 84 HNSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKD--GDDYVLNGSKMWITNGGEADFYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 261 VFAktpVTDPATGavKEKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNG 340
Cdd:cd01158 162 VFA---VTDPSKG--YRGITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 341 RFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGStDFQIEAAISKI 420
Cdd:cd01158 237 RIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGE-PFIKEAAMAKL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 966994270 421 FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01158 316 FASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
189-473 |
7.49e-104 |
|
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: 318.84 E-value: 7.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 189 ILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTPVT 268
Cdd:cd00567 48 LLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKD--GDGYVLNGRKIFISNGGDADLFIVLARTDEE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 269 DPATGAvkekITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAAL 348
Cdd:cd00567 126 GPGHRG----ISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLAAVA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 349 AGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDFQIEAAISKIFGSEAAWK 428
Cdd:cd00567 202 LGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEAARE 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 966994270 429 VTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd00567 282 VADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
105-473 |
7.01e-88 |
|
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: 278.91 E-value: 7.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 105 LVEPVSRFFEEVNDP--AKNDTLEMVEETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLAVGITLGAHQ 182
Cdd:cd01156 9 LRQSVREFAQKEIAPlaAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALSYGAHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 183 SIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAvpSPCGKYYTLNGSKLWISNGGLADIFTVF 262
Cdd:cd01156 89 NLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRA--EKKGDRYVLNGSKMWITNGPDADTLVVY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 263 AKTpvtDPATGAvkEKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRF 342
Cdd:cd01156 167 AKT---DPSAGA--HGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 343 GMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDfQIEAAISKIFG 422
Cdd:cd01156 242 VLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNMD-PKDAAGVILYA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 966994270 423 SEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01156 321 AEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
94-473 |
2.04e-78 |
|
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: 254.29 E-value: 2.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 94 LNQEQTEFLKelvepVSRFF---EEVNDPAKNDTLEMVEETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMH 170
Cdd:cd01162 1 LNEEQRAIQE-----VARAFaakEMAPHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 171 DLAVGITLGAHQSIGFKgILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWI 250
Cdd:cd01162 76 CVSTAAYISIHNMCAWM-IDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVRE--GDHYVLNGSKAFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 251 SNGGLADIFTVFAKTpvtdpaTGAVKEKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGF 330
Cdd:cd01162 153 SGAGDSDVYVVMART------GGEGPKGISCFVVEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 331 KVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTD 410
Cdd:cd01162 227 GIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDRGDPD 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966994270 411 FQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01162 307 AVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIA 369
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
109-475 |
1.67e-72 |
|
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: 238.55 E-value: 1.67e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 109 VSRFFEEVNDP--AKNDTLEMVEETTLQGLKELGAFGLQVPSELGGVGLcNTQYARLVEIVGMHDLAVGITLGAHQSIGF 186
Cdd:cd01160 10 VRRFFAKEVAPfhHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGG-DLLSAAVLWEELARAGGSGPGLSLHTDIVS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 187 KGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISNGGLADIFTVFAKTp 266
Cdd:cd01160 89 PYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKD--GDHYVLNGSKTFITNGMLADVVIVVART- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 267 vTDPATGAvkEKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAA 346
Cdd:cd01160 166 -GGEARGA--GGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 347 ALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDfQIEAAISKIFGSEAA 426
Cdd:cd01160 243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD-VAEASMAKYWATELQ 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 966994270 427 WKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQ 475
Cdd:cd01160 322 NRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISRQ 370
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
137-472 |
1.66e-65 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 220.90 E-value: 1.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 137 KELGAF---GLQVPSELGGVGLCNTQYARLVEIVGMHDLAVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETLAA 213
Cdd:PLN02519 66 KLMGDFnlhGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 214 FCLTEPSSGSDAASIRTSAVPSPCGkyYTLNGSKLWISNGGLADIFTVFAKTpvtDPATGAvkEKITAFVVERGFGGVTH 293
Cdd:PLN02519 146 LAMSEPNSGSDVVSMKCKAERVDGG--YVLNGNKMWCTNGPVAQTLVVYAKT---DVAAGS--KGITAFIIEKGMPGFST 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 294 GPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKI 373
Cdd:PLN02519 219 AQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 374 HNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDFQiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLR 453
Cdd:PLN02519 299 GEFQFIQGKLADMYTSLQSSRSYVYSVARDCDNGKVDRK-DCAGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLR 377
|
330
....*....|....*....
gi 966994270 454 DLRIFRIFEGTNDILRLFV 472
Cdd:PLN02519 378 DAKLYEIGAGTSEIRRMLI 396
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
99-473 |
3.11e-63 |
|
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: 214.37 E-value: 3.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 99 TEFLKELVEPVSRFFEEVNDP--AKNDTLEMVEETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVEivgmhDLAVGI 176
Cdd:cd01157 2 TEQQKEFQETARKFAREEIIPvaAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITE-----ELAYGC 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 177 TlGAH-----QSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWIS 251
Cdd:cd01157 77 T-GVQtaieaNSLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKK--GDEYIINGQKMWIT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 252 NGGLADIFTVFAKTPvTDPATGAVKeKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:cd01157 154 NGGKANWYFLLARSD-PDPKCPASK-AFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 332 VAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMlQYVTESMAYMVSAN-MDQGSTD 410
Cdd:cd01157 232 IAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAM-KVELARLAYQRAAWeVDSGRRN 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966994270 411 fQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01157 311 -TYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIIS 372
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
103-464 |
3.65e-63 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 215.19 E-value: 3.65e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 103 KELVEPVSRFFEEVNDP-AKNDTLEMVEETTL-QGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLAVGITLGA 180
Cdd:PTZ00461 42 AALRETVAKFSREVVDKhAREDDINMHFNRDLfKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCLAYLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 181 HQSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSPCGKYyTLNGSKLWISNGGLADIFT 260
Cdd:PTZ00461 122 HSMLFVNNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGNY-VLNGSKIWITNGTVADVFL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 261 VFAKtpvtdpatgaVKEKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNG 340
Cdd:PTZ00461 201 IYAK----------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 341 RFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDfQIEAAISKI 420
Cdd:PTZ00461 271 RVTLAAMAVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKN-RLGSDAAKL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 966994270 421 FGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGT 464
Cdd:PTZ00461 350 FATPIAKKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGT 393
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
78-487 |
3.35e-62 |
|
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: 211.83 E-value: 3.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 78 FKGQLATDQVfpypsVLNQEQTEFLKELVEP--VSRFFEEVNDPakndtlEMVEEttlqgLKELGAFGLQvPSELGGVGL 155
Cdd:cd01151 9 LDDLLTEEER-----AIRDTAREFCQEELAPrvLEAYREEKFDR------KIIEE-----MGELGLLGAT-IKGYGCAGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 156 CNTQY---ARLVEIVgmhDLAVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSA 232
Cdd:cd01151 72 SSVAYgliAREVERV---DSGYRSFMSVQSSLVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 233 vpSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFF 312
Cdd:cd01151 149 --RKDGGGYKLNGSKTWITNSPIADVFVVWARNDETG--------KIRGFILERGMKGLSAPKIQGKFSLRASITGEIVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 313 DGVRVPSENVLGEVgSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARM-VMLQY 391
Cdd:cd01151 219 DNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMlTEIAL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 392 VTEsMAYMVSANMDQGS-TDFQIeaAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01151 298 GLL-ACLRVGRLKDQGKaTPEQI--SLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIHAL 374
|
410
....*....|....*..
gi 966994270 471 FValqgcmdkGKELSGL 487
Cdd:cd01151 375 IL--------GRAITGI 383
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
131-467 |
1.73e-54 |
|
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: 191.45 E-value: 1.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 131 TTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLAVGITLGAHQsiGFKGILLFGTKAQKEKYLPKLASGET 210
Cdd:cd01153 40 EALDAFAEAGWMALGVPEEYGGQGLPITVYSALAEIFSRGDAPLMYASGTQG--AAATLLAHGTEAQREKWIPRLAEGEW 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 211 LAAFCLTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKLWISNG--GLAD--IFTVFAKTPvtDPATGAvkEKITAFVV-- 284
Cdd:cd01153 118 TGTMCLTEPDAGSDLGALRTKAVYQADGSWR-INGVKRFISAGehDMSEniVHLVLARSE--GAPPGV--KGLSLFLVpk 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 285 -----ERGfgGVTHGPPEKKMGIKASNTAEVFFDGVRVPsenVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIITKA 359
Cdd:cd01153 193 flddgERN--GVTVARIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQGTGLAEAAYLNA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 360 VDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDFQIEA---------------------AIS 418
Cdd:cd01153 268 LAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDLYTATVQDLAerkategedrkalsaladlltPVV 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 966994270 419 KIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDI 467
Cdd:cd01153 348 KGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
94-468 |
2.20e-49 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 176.84 E-value: 2.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 94 LNQEQTEFLKELVEPVSRFFEEvNDPAKNDTLEMVEETTLQGLKELGAFGLQVPSELGGVGLCN-TQYARLVEIVGMHDL 172
Cdd:PRK12341 5 LTEEQELLLASIRELITRNFPE-EYFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYvTQMLVLEEVSKCGAP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 173 AVGITlgahQSIGFKGILLFGTKAQKEKYLpKLASGETLAAFCL--TEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWI 250
Cdd:PRK12341 84 AFLIT----NGQCIHSMRRFGSAEQLRKTA-ESTLETGDPAYALalTEPGAGSDNNSATTTYTRKN-GKVY-LNGQKTFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 251 SNGGLADIFTVFAKtpvtDPATGAVKEKITAFVVERGFGGVTHGPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGF 330
Cdd:PRK12341 157 TGAKEYPYMLVLAR----DPQPKDPKKAFTLWWVDSSKPGIKINPLHK-IGWHMLSTCEVYLDNVEVEESDLVGEEGMGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 331 KVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTd 410
Cdd:PRK12341 232 LNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADNGQS- 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 966994270 411 FQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDIL 468
Cdd:PRK12341 311 LRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM 368
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
130-470 |
4.10e-43 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 159.61 E-value: 4.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 130 ETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGmhdlavgiTLGAHQSI------GFKGILLFGTKAQKEKYLP 203
Cdd:PRK03354 40 ERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELG--------RLGAPTYVlyqlpgGFNTFLREGTQEQIDKIMA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 204 KLASGETLAAFCLTEPSSGSDAASIRTSAVPSPcGKYYtLNGSKLWISNGGLADIFTVFAKTPVTDPatgavKEKITAFV 283
Cdd:PRK03354 112 FRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRN-GKVY-LNGSKCFITSSAYTPYIVVMARDGASPD-----KPVYTEWF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 284 VERGFGGVTHGPPEKkMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYA 363
Cdd:PRK03354 185 VDMSKPGIKVTKLEK-LGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 364 TNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFM 443
Cdd:PRK03354 264 NQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT-SGDAAMCKYFCANAAFEVVDSAMQVLGGVGIA 342
|
330 340
....*....|....*....|....*..
gi 966994270 444 KEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:PRK03354 343 GNHRISRFWRDLRVDRVSGGSDEMQIL 369
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
327-473 |
1.28e-39 |
|
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: 142.39 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 327 GSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQ 406
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966994270 407 GSTDfQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:pfam00441 81 GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
100-473 |
1.04e-37 |
|
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: 144.41 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 100 EFLKELVEPVSRffEEVNDPAKNDtlEMVEETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVE---IVGM--HDLAV 174
Cdd:cd01152 12 AWLAAHLPPELR--EESALGYREG--REDRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREemaAAGApvPFNQI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 175 GITLGAHQsigfkgILLFGTKAQKEKYLPKLASGETLaaFCL--TEPSSGSDAASIRTSAVPSpcGKYYTLNGSKLWISN 252
Cdd:cd01152 88 GIDLAGPT------ILAYGTDEQKRRFLPPILSGEEI--WCQgfSEPGAGSDLAGLRTRAVRD--GDDWVVNGQKIWTSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 253 GGLADIFTVFAKTpvtDPAtgAVKEK-ITAFVVERGFGGVTHGPPEKKMGikASNTAEVFFDGVRVPSENVLGEVGSGFK 331
Cdd:cd01152 158 AHYADWAWLLVRT---DPE--APKHRgISILLVDMDSPGVTVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 332 VAMHILNNGR---FGMAAALAGTMRGiitkAVDYATNRiqfGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGS 408
Cdd:cd01152 231 VAMTTLNFERvsiGGSAATFFELLLA----RLLLLTRD---GRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGK 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966994270 409 tDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPG--------VERVLRDLRIFRIFEGTNDILRLFVA 473
Cdd:cd01152 304 -PPGAEASIAKLFGSELAQELAELALELLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIA 375
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
102-463 |
2.32e-35 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 137.91 E-value: 2.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 102 LKELVEPVSRFFEEVNDPAKNDTLEMVEET---------TLQGLKE----LGAFGLQVPSELGGVGLCNTQYARLVEIVG 168
Cdd:cd01155 3 AQELRARVKAFMEEHVYPAEQEFLEYYAEGgdrwwtpppIIEKLKAkakaEGLWNLFLPEVSGLSGLTNLEYAYLAEETG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 169 MHDLAVGITLGAHQSIGFKGIL-LFGTKAQKEKYLPKLASGETLAAFCLTEPS-SGSDAASIRTSAVPSpcGKYYTLNGS 246
Cdd:cd01155 83 RSFFAPEVFNCQAPDTGNMEVLhRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERD--GDDYVINGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 247 KLWISNGGLAD--IFTVFAKTpvtDPATGAVKEKITAFVVERGFGGVTHGPPEKKMGIKAS--NTAEVFFDGVRVPSENV 322
Cdd:cd01155 161 KWWSSGAGDPRckIAIVMGRT---DPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDAphGHAEITFDNVRVPASNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 323 LGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLA--RMV--MLQYVTESMAY 398
Cdd:cd01155 238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAksRIEieQARLLVLKAAH 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966994270 399 MvsanMDQ-GSTDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEG 463
Cdd:cd01155 318 M----IDTvGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADG 379
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
151-489 |
4.25e-34 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 134.59 E-value: 4.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 151 GGVGLCNTQYARLVEIVGMHDLAVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRT 230
Cdd:PLN02526 83 GCPGLSITASAIATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNT 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 231 SAVPSPCGkyYTLNGSKLWISNGGLADIFTVFAKTPVTDpatgavkeKITAFVVERGFGGVTHGPPEKKMGIKASNTAEV 310
Cdd:PLN02526 163 TATKVEGG--WILNGQKRWIGNSTFADVLVIFARNTTTN--------QINGFIVKKGAPGLKATKIENKIGLRMVQNGDI 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 311 FFDGVRVPSENVLGEVGSgFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARmvMLQ 390
Cdd:PLN02526 233 VLKDVFVPDEDRLPGVNS-FQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLKERKQFGAPLAAFQINQEKLVR--MLG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 391 YVtESMAYM--------VSANMDQGstdfqiEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFE 462
Cdd:PLN02526 310 NI-QAMFLVgwrlcklyESGKMTPG------HASLGKAWITKKARETVALGRELLGGNGILADFLVAKAFCDLEPIYTYE 382
|
330 340
....*....|....*....|....*..
gi 966994270 463 GTNDILRLFValqgcmdkGKELSGLGS 489
Cdd:PLN02526 383 GTYDINALVT--------GREITGIAS 401
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
199-470 |
3.12e-31 |
|
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: 126.33 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 199 EKYLPKLASGET----LAAFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTPVTDPATGA 274
Cdd:cd01154 132 KQYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSG-GGVYRLNGHK-WFASAPLADAALVLARPEGAPAGARG 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 275 vkekITAFVVERGFGGVTHGPPE-----KKMGIKASNTAEVFFDGvrvpSEN-VLGEVGSGFKVAMHILNNGRFGMAAAL 348
Cdd:cd01154 210 ----LSLFLVPRLLEDGTRNGYRirrlkDKLGTRSVATGEVEFDD----AEAyLIGDEGKGIYYILEMLNISRLDNAVAA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 349 AGTMRGIITKAVDYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDFQIEA-------AISKIF 421
Cdd:cd01154 282 LGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEAhmarlatPVAKLI 361
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 966994270 422 GSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRL 470
Cdd:cd01154 362 ACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQAL 410
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
100-467 |
1.82e-28 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 120.74 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 100 EFLKELVEPVSRFFEEVNDP------------AKNDTLEMVE--ETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVE 165
Cdd:PTZ00456 58 ELMDSLLEEASKLATQTLLPlyessdsegcvlLKDGNVTTPKgfKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 166 IVGMHDLAVGITLGahQSIG-FKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSPCGKyYTLN 244
Cdd:PTZ00456 138 LMATANWGFSMYPG--LSIGaANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKIT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 245 GSKLWISNG--GLAD--IFTVFAKTPVTDPATgavkEKITAFVVERGF----------GGVTHGPPEKKMGIKASNTAEV 310
Cdd:PTZ00456 215 GTKIFISAGdhDLTEniVHIVLARLPNSLPTT----KGLSLFLVPRHVvkpdgsletaKNVKCIGLEKKMGIKGSSTCQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 311 FFDGvrvPSENVLGEVGSGFKVAMHILNNGRFGMA------AALA-----------GTMRGII-TKAVDYATNRIqfgek 372
Cdd:PTZ00456 291 SFEN---SVGYLIGEPNAGMKQMFTFMNTARVGTAlegvchAELAfqnalryarerRSMRALSgTKEPEKPADRI----- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 373 IHNFGLIQEKL--------ARMVMLQyVTESMAYMVSAN--MDQGSTDFQIE--AAISKIFGSEAAWKVTDECIQIMGGM 440
Cdd:PTZ00456 363 ICHANVRQNILfakavaegGRALLLD-VGRLLDIHAAAKdaATREALDHEIGfyTPIAKGCLTEWGVEAASRCLQVWGGH 441
|
410 420
....*....|....*....|....*..
gi 966994270 441 GFMKEPGVERVLRDLRIFRIFEGTNDI 467
Cdd:PTZ00456 442 GYIKGNGMEQILRDARIGTLYEGTTGI 468
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
213-313 |
3.57e-27 |
|
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: 105.44 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 213 AFCLTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGavkekITAFVVERGFGGVT 292
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTAADGD-GGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGG-----ISLFLVPKDAPGVS 74
|
90 100
....*....|....*....|.
gi 966994270 293 HGPPEKKMGIKASNTAEVFFD 313
Cdd:pfam02770 75 VRRIETKLGVRGLPTGELVFD 95
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
99-209 |
1.83e-22 |
|
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: 92.53 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 99 TEFLKELVEPVSRFFEEVNDP--AKNDTLEMVEETTLQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLAVGI 176
Cdd:pfam02771 1 TEEQEALRDTVREFAEEEIAPhaAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVAL 80
|
90 100 110
....*....|....*....|....*....|...
gi 966994270 177 TLGAHQSIGFKGILLFGTKAQKEKYLPKLASGE 209
Cdd:pfam02771 81 ALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
72-615 |
9.16e-21 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 96.10 E-value: 9.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 72 SFAVAMFKGQLATDQVFPYPS-VLNQEQTEFLKELVEPVSrffeevndpaKNDTlemveetTLQGLkelgaFGLQVPSEL 150
Cdd:PTZ00457 17 SYAAGLFNFKIVPEEMFPYPCrKLDGDEAENLQSLLEQIR----------SNDK-------ILGNL-----YGARIATEY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 151 GGVGLCNTQYARLVEIVGMHDLAVGITLGAHQsiGFKGILL--FGTKAQKEKYLPKLASGETLAAFClTEPSSGSDAASI 228
Cdd:PTZ00457 75 GGLGLGHTAHALIYEEVGTNCDSKLLSTIQHS--GFCTYLLstVGSKELKGKYLTAMSDGTIMMGWA-TEEGCGSDISMN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 229 RTSAVPSPCGKYyTLNGSKLWIsNGGLADIFTVFAKTpVTDPATGA---VKEKITAFVVERGFGGVThgppekkmgikaS 305
Cdd:PTZ00457 152 TTKASLTDDGSY-VLTGQKRCE-FAASATHFLVLAKT-LTQTAAEEgatEVSRNSFFICAKDAKGVS------------V 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 306 NTAEVFFDgvRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIITkavdyatnriQFGEKIHNFGlIQEKLAR 385
Cdd:PTZ00457 217 NGDSVVFE--NTPAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQ----------ELRGSNAEEG-ATDTVAS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 386 MVMLQYVTESMAYMVSANMDQGSTDFQIEAAISKIFGSEAawkvTDECIQIMGGMGFMKEPgVERVLRDLRIFRIFEGTN 465
Cdd:PTZ00457 284 FACAMYAMESTLYALTANLDLPTEDSLLECTLVSAFVQST----TNQLLSILETATPPSTT-LEKCFANARLFLSMMESR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 466 DIlrLFVALQGCmdkGKELSGLgsalknPFGNAGLLlgeagkQLRRRAGLGSGLSLSGIVHPELsRSGELAVQALEQFAT 545
Cdd:PTZ00457 359 DF--LYSSAVCC---GVEDYGL------FFQRASTL------QMMQARTLRSLGVRDRVPIKNL-PDCSLIDEAVVAFGN 420
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 546 VVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHHTAQHEKMLCDTWCIEAAARIR 615
Cdd:PTZ00457 421 AVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGELASAFIAMAVSRAR 490
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
136-441 |
1.14e-20 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 96.95 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 136 LKELGAFGLQVPSELGGVGLcnTQYA--RLVEIVGMHDLAVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETL 211
Cdd:PRK13026 117 LKKEGFFALIIPKEYGGKGF--SAYAnsTIVSKIATRSVSAAVTVMVPNSLG-PGELLthYGTQEQKDYWLPRLADGTEI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 212 AAFCLTEPSSGSDAASIRTSAVpsPC-GKY-------YTLNGSKLWISnggLADIFTVF-----AKTPvtDPATGAVKE- 277
Cdd:PRK13026 194 PCFALTGPEAGSDAGAIPDTGI--VCrGEFegeevlgLRLTWDKRYIT---LAPVATVLglafkLRDP--DGLLGDKKEl 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 278 KITAFVVERGFGGVTHGPPEKKMGIkasntaeVFFDG------VRVPSENVLG---EVGSGFKVAMHILNNGRF----GM 344
Cdd:PRK13026 267 GITCALIPTDHPGVEIGRRHNPLGM-------AFMNGttrgkdVFIPLDWIIGgpdYAGRGWRMLVECLSAGRGislpAL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 345 AAAlAGTMRGIITKAvdYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDfQIEAAISKIFGSE 424
Cdd:PRK13026 340 GTA-SGHMATRTTGA--YAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLDLGVKP-SVVTAIAKYHMTE 415
|
330
....*....|....*..
gi 966994270 425 AAWKVTDECIQIMGGMG 441
Cdd:PRK13026 416 LARDVVNDAMDIHAGKG 432
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
136-446 |
2.65e-19 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 92.57 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 136 LKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLAVGITLGAHQSIGfKGILL--FGTKAQKEKYLPKLASGETLAA 213
Cdd:PRK09463 118 IKEHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAVTVMVPNSLG-PGELLlhYGTDEQKDHYLPRLARGEEIPC 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 214 FCLTEPSSGSDAASIRTSAVpsPC-----GK---YYTLNGSKLWISnggLADIFTVFA---KtpVTDPaTGAVKEK---- 278
Cdd:PRK09463 197 FALTSPEAGSDAGSIPDTGV--VCkgewqGEevlGMRLTWNKRYIT---LAPIATVLGlafK--LYDP-DGLLGDKedlg 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 279 ITAFVVERGFGGVTHGPPEKKMGIkasntaeVFFDG------VRVPSENVLGE---VGSGFKVAMHILNNGR-------- 341
Cdd:PRK09463 269 ITCALIPTDTPGVEIGRRHFPLNV-------PFQNGptrgkdVFIPLDYIIGGpkmAGQGWRMLMECLSVGRgislpsns 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 342 FGMAAALAGTmrgiiTKAvdYATNRIQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGSTDFQIeAAISKIF 421
Cdd:PRK09463 342 TGGAKLAALA-----TGA--YARIRRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKPSVL-SAIAKYH 413
|
330 340
....*....|....*....|....*
gi 966994270 422 GSEAAWKVTDECIQIMGGMGFMKEP 446
Cdd:PRK09463 414 LTERGRQVINDAMDIHGGKGICLGP 438
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
159-473 |
4.21e-19 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 91.46 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 159 QYARLVEIVGMHDLAVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSPCG 238
Cdd:PLN02636 122 KYFAITEAVGSVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLT 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 239 KYYTLN-----GSKLWISNGGLADIF-TVFAKTPVTDPATGAVKEK-ITAFVV-------ERGFGGVTHGPPEKKMGIKA 304
Cdd:PLN02636 202 DEFVINtpndgAIKWWIGNAAVHGKFaTVFARLKLPTHDSKGVSDMgVHAFIVpirdmktHQVLPGVEIRDCGHKVGLNG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 305 SNTAEVFFDGVRVPSENVLGEVG----------------SGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQ 368
Cdd:PLN02636 282 VDNGALRFRSVRIPRDNLLNRFGdvsrdgkytsslptinKRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQ 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 369 FGE------KIHNFGLIQEKLarMVML----------QYVTESMAYMVSANMDQGSTDFQIEAAISKIFGSEAAWKVTDE 432
Cdd:PLN02636 362 FGPpkqpeiSILDYQSQQHKL--MPMLastyafhfatEYLVERYSEMKKTHDDQLVADVHALSAGLKAYITSYTAKALST 439
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 966994270 433 CIQIMGGMGFmkePGVER--VLR-DLRIFRIFEGTNDILRLFVA 473
Cdd:PLN02636 440 CREACGGHGY---AAVNRfgSLRnDHDIFQTFEGDNTVLLQQVA 480
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
163-578 |
5.36e-19 |
|
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: 91.24 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 163 LVEIVGMHDLAVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSPCGKYYT 242
Cdd:cd01150 87 LTNSLGGYDLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCFAQTELGHGSNLQGLETTATYDPLTQEFV 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 243 LN-----GSKLWIsnGGLADIFT---VFAKTpvtdpATGAVKEKITAFVVE-------RGFGGVTHGPPEKKMGIKASNT 307
Cdd:cd01150 167 INtpdftATKWWP--GNLGKTAThavVFAQL-----ITPGKNHGLHAFIVPirdpkthQPLPGVTVGDIGPKMGLNGVDN 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 308 AEVFFDGVRVPSENVL---GEV-------------GSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQFGE 371
Cdd:cd01150 240 GFLQFRNVRIPRENLLnrfGDVspdgtyvspfkdpNKRYGAMLGTRSGGRVGLIYDAAMSLKKAATIAIRYSAVRRQFGP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 372 K-------IHNFGLIQEK----LARMVMLQYVTESMAYM---VSANMDQGSTDFQIE----AAISKIFGSEAAWKVTDEC 433
Cdd:cd01150 320 KpsdpevqILDYQLQQYRlfpqLAAAYAFHFAAKSLVEMyheIIKELLQGNSELLAElhalSAGLKAVATWTAAQGIQEC 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 434 IQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVAlQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRA 513
Cdd:cd01150 400 REACGGHGYLAMNRLPTLRDDNDPFCTYEGDNTVLLQQTA-NYLLKKYAQAFSLADYLEAYEWLAAHLLRHAAAQLEKLK 478
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966994270 514 GLGSGLSLSGivhpelSRSGELAVQALEQFA-TVVEAKLIKHKKGIVNE--QFLLQRLAdgaiDLYAM 578
Cdd:cd01150 479 KSGSGSFEAR------NNSQVHLRCAAKAHTeYTVLQRFHESVEEIVDPsvRAVLKRLC----DLYAL 536
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
148-467 |
1.71e-18 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 89.85 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 148 SELGGVGLCNTQYARLVEIVGMHDLAVGI-TLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETLAAFCLTEPS-SGSDA 225
Cdd:PLN02876 487 DQLLGAGLSNLEYGYLCEIMGRSVWAPQVfNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDA 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 226 ASIRTSAVPSpcGKYYTLNGSKLWISngGLAD----IFTVFAKTPVTDPA------------TGAVKEKITAFVVerGFG 289
Cdd:PLN02876 567 TNIECSIRRQ--GDSYVINGTKWWTS--GAMDprcrVLIVMGKTDFNAPKhkqqsmilvdiqTPGVQIKRPLLVF--GFD 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 290 GVTHGppekkmgikasnTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQF 369
Cdd:PLN02876 641 DAPHG------------HAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAF 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 370 GEKIHNFGLIQEKLARmvmLQYVTESMAYMVSANMDQ----GSTDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKE 445
Cdd:PLN02876 709 GKLIAQHGSFLSDLAK---CRVELEQTRLLVLEAADQldrlGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSD 785
|
330 340
....*....|....*....|..
gi 966994270 446 PGVERVLRDLRIFRIFEGTNDI 467
Cdd:PLN02876 786 TVLAHLWATARTLRIADGPDEV 807
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
136-366 |
5.54e-11 |
|
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: 64.65 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 136 LKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLAVGITLGAHqsIGF-KGILLFGTKAQKEKYLPKLASGETLAAf 214
Cdd:cd01163 31 LRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAH--FGFvEALLLAGPEQFRKRWFGRVLNGWIFGN- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 215 clTEPSSGSDAASIRTSAVPSPCGKYYtLNGSKlWISNGGL-ADIFTVFAktpvTDPAtgavkEKITAFVVERGFGGVTH 293
Cdd:cd01163 108 --AVSERGSVRPGTFLTATVRDGGGYV-LNGKK-FYSTGALfSDWVTVSA----LDEE-----GKLVFAAVPTDRPGITV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966994270 294 GPPEKKMGIK--ASNTAEvfFDGVRVPSENVLGEvGSGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNR 366
Cdd:cd01163 175 VDDWDGFGQRltASGTVT--FDNVRVEPDEVLPR-PNAPDRGTLLTAIYQLVLAAVLAGIARAALDDAVAYVRSR 246
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
119-488 |
1.90e-08 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 57.48 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 119 PAKNDTLEMVEETTL---QGLKELGAF-----GLQVPSELggvglcntQYARLVEIVGMHDLAVGITLGAHQSIGFKGIL 190
Cdd:PLN02312 94 PDYNQTMEQQREITMkriLYLLERGVFrgwltETGPEAEL--------RKLALLEVIGIYDHSLAIKLGVHFFLWGGAIK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 191 LFGTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLN-----GSKLWIsnGGLADIFT---VF 262
Cdd:PLN02312 166 FLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINtpcesAQKYWI--GGAANHAThtiVF 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 263 AKTPVTdpatgAVKEKITAFVVE------RGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVG--------- 327
Cdd:PLN02312 244 SQLHIN-----GKNEGVHAFIAQirdqdgNICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNSVAdvspdgkyv 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 328 -------SGFKVAMHILNNGRFGMAAALAGTMRGIITKAVDYATNRIQF-----GEKI-------HNFGLIqEKLARMVM 388
Cdd:PLN02312 319 saikdpdQRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAFsvtpnGPEVllldypsHQRRLL-PLLAKTYA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 389 LQYVTESMAYMVSANMDQGSTDFQIeaaISKIFGSEAAW---KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 465
Cdd:PLN02312 398 MSFAANDLKMIYVKRTPESNKAIHV---VSSGFKAVLTWhnmRTLQECREACGGQGLKTENRVGQLKAEYDVQSTFEGDN 474
|
410 420
....*....|....*....|....*....
gi 966994270 466 DILR------LFVALQGCMDKGKELSGLG 488
Cdd:PLN02312 475 NVLMqqvskaLLAEYVSAKKRNKPFKGLG 503
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
193-473 |
3.12e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 53.70 E-value: 3.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 193 GTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLN-----GSKLWISN-GGLADIFTVFAKTP 266
Cdd:PTZ00460 110 GTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGElGFLCNFALVYAKLI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 267 VTDPATG--AVKEKITAFVVERGFGGVTHGPPEKKMGIKASNTAEVFFDGVRVPSENVLG---EVGSGFKVAMHilNNGR 341
Cdd:PTZ00460 190 VNGKNKGvhPFMVRIRDKETHKPLQGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLAryiKVSEDGQVERQ--GNPK 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 342 FGMAAALagTMRGII------------TKAVDYATNRIQFGE------KIHNFGLIQEK----LARMVMLQYVTESMAYM 399
Cdd:PTZ00460 268 VSYASMM--YMRNLIidqyprfaaqalTVAIRYSIYRQQFTNdnkqenSVLEYQTQQQKllplLAEFYACIFGGLKIKEL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 400 VSANMDQ-GSTDFQIEAAISKIFGSEAAW------KVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFV 472
Cdd:PTZ00460 346 VDDNFNRvQKNDFSLLQLTHAILSAAKANytyfvsNCAEWCRLSCGGHGYAHYSGLPAIYFDMSPNITLEGENQIMYLQL 425
|
.
gi 966994270 473 A 473
Cdd:PTZ00460 426 A 426
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
216-479 |
5.91e-07 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 52.45 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 216 LTEPSSGSDAASIRTSAVPSPcGKYYTLNGSKlWISNGGLADIFTVFAKTpvtdpatgavKEKITAFVVERGFGGVTHGP 295
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLA-DGSYRLVGHK-WFFSVPQSDAHLVLAQA----------KGGLSCFFVPRFLPDGQRNA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 296 P-----EKKMGIKASNTAEVFFDGVrvpSENVLGEVGSGFKvamHILNNG---RFGMAAALAGTMRGIITKAVDYATNRI 367
Cdd:PRK11561 252 IrlerlKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFDCALGSHGLMRRAFSVAIYHAHQRQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 368 QFGEKIHNFGLIQEKLARMVM-LQYVTESMAYMVSANMDQGSTDfqiEAAISKIFGSEAAWKVTD-------ECIQIMGG 439
Cdd:PRK11561 326 VFGKPLIEQPLMRQVLSRMALqLEGQTALLFRLARAWDRRADAK---EALWARLFTPAAKFVICKrgipfvaEAMEVLGG 402
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 966994270 440 MGFMKEPGVERVLRDLRIFRIFEGTN-----DILRLFVALQGCMD 479
Cdd:PRK11561 403 IGYCEESELPRLYREMPVNSIWEGSGnimclDVLRVLNKQPGVYD 447
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
343-465 |
2.09e-06 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 47.34 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 343 GMAAALAGTMRGIITKAVDYATNRIQ--FGEKIHNFGLIQEKLARMV-------MLQYVTESMAYMVSANMDQGSTDFQI 413
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridaarLLLERAAARIEAAAAAGKPVTPALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 966994270 414 EAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTN 465
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVN 132
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
193-501 |
1.46e-05 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 48.29 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 193 GTKAQKEKYLPKLASGETLAAFCLTEPSSGSDAASIRTSAVPSPCGKYY-----TLNGSKLWisNGGLADIFT---VFAK 264
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFvihspTLTSSKWW--PGGLGKVSThavVYAR 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 265 TpvtdpATGAVKEKITAFVVE-------RGFGGVTHGPPEKKMGIKASNTAE---VFFDGVRVPSENVLGEVGSGFKVAM 334
Cdd:PLN02443 192 L-----ITNGKDHGIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSKVTREGK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 335 HILNNG------------RFGMAAALAGTMRGIITKAVDYATNRIQFGEK-------IHNFGLIQEK----LARMVMLQY 391
Cdd:PLN02443 267 YVQSDVprqlvygtmvyvRQTIVADASTALSRAVCIATRYSAVRRQFGSQdggpetqVIDYKTQQSRlfplLASAYAFRF 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966994270 392 VTESMAYMVSANMDQ-GSTDF----QIEAAIS--KIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGT 464
Cdd:PLN02443 347 VGEWLKWLYTDVTQRlEANDFstlpEAHACTAglKSLTTSATADGIEECRKLCGGHGYLCSSGLPELFAVYVPACTYEGD 426
|
330 340 350
....*....|....*....|....*....|....*..
gi 966994270 465 NDILRLFVAlQGCMdkgKELSGLGSAlKNPFGNAGLL 501
Cdd:PLN02443 427 NVVLLLQVA-RFLM---KTVSQLGSG-KKPVGTTAYM 458
|
|
| |
