|
Name |
Accession |
Description |
Interval |
E-value |
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
38-445 |
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: 747.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 38 AFAKELFLGKIKKKEVFPFPEVSQDELNE-INQFLGPVEKFFTEEVDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYG 116
Cdd:cd01161 1 SFALNMFLGDIVTKQVFPYPSVLTEEQTEeLNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKELGLFGLQVPEEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 117 GLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRA 196
Cdd:cd01161 81 GLGLNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGILLFGTEAQKEKYLPKLASGEWIAAFALTEPSSGSDAASIRTTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 197 TLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFE 276
Cdd:cd01161 161 VLSEDGKHYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVKDKITAFIVERSFGGVTNGPPEKKMGIKGSNTAEVYFE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 277 NTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVM 356
Cdd:cd01161 241 DVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 357 ESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:cd01161 321 ESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEILRLFI 400
|
....*....
gi 119599702 437 ALTGLQHAG 445
Cdd:cd01161 401 ALTGLQHAG 409
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
66-437 |
7.92e-149 |
|
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: 435.04 E-value: 7.92e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 66 EINQFLGPVEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTL 142
Cdd:COG1960 8 EQRALRDEVREFAEEEIApeAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARaDASLALPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 143 AAHqAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANI 222
Cdd:COG1960 88 GVH-NGAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGD--GYVLNGQKTFITNAPVADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 223 FTVFAKTEvvDSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNS 302
Cdd:COG1960 165 ILVLARTD--PAAGH--RGISLFLVPKDTPGVTVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 303 GRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGfpDCSIEAAMV 382
Cdd:COG1960 241 GRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDAGE--DAALEAAMA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 119599702 383 KVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:COG1960 319 KLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIA 373
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
69-437 |
5.49e-135 |
|
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: 399.34 E-value: 5.49e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 69 QFLGPVEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSR-LGEIISMDGSITVTLAAH 145
Cdd:cd01158 5 MIRKTVRDFAEKEIAplAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIaIEELAKVDASVAVIVSVH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 146 QAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTV 225
Cdd:cd01158 85 NSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGD--DYVLNGSKMWITNGGEADFYIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 226 FAKTevvdsDGSVKDK-ITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGR 304
Cdd:cd01158 163 FAVT-----DPSKGYRgITAFIVERDTPGLSVGKKEDKLGIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 305 FSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYlTAGMLDQPGFPdCSIEAAMVKV 384
Cdd:cd01158 238 IGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTY-KAARLKDNGEP-FIKEAAMAKL 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 119599702 385 FSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01158 316 FASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIA 368
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
148-437 |
7.02e-121 |
|
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: 361.22 E-value: 7.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 148 IGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFA 227
Cdd:cd00567 43 LGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTARKDGD--GYVLNGRKIFISNGGDADLFIVLA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 228 KTevvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSM 307
Cdd:cd00567 121 RT---DEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 308 GSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPDCSIEAAMVKVFSS 387
Cdd:cd00567 198 AAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAKLFAT 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 119599702 388 EAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd00567 277 EAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
66-437 |
8.43e-106 |
|
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: 324.36 E-value: 8.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 66 EINQFLGPVEKFFTEEVDSR--KIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSntmYsrLGEIISMD------GS 137
Cdd:cd01156 5 EIEMLRQSVREFAQKEIAPLaaKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMG---Y--LAHVIIMEeisrasGS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 138 ITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlsEDKKHYILNGSKVWITNG 217
Cdd:cd01156 80 VALSYGAHSNLCINQIYRNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAE--KKGDRYVLNGSKMWITNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 218 GLANIFTVFAKTEVvdsdGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAM 297
Cdd:cd01156 158 PDADTLVVYAKTDP----SAGAHGITAFIVEKGMPGFSRAQKLDKLGMRGSNTCELVFEDCEVPEENILGGENKGVYVLM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 298 NILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTAGMLDqpgf 372
Cdd:cd01156 234 SGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLAdmytrLNASRSYLYTVAKACDRGNMD---- 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119599702 373 pdcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01156 310 ---PKDAAGVILYAAEKATQVALDAIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEIRRMVIG 371
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
74-437 |
1.69e-87 |
|
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: 277.07 E-value: 1.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 74 VEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQAIGLK 151
Cdd:cd01160 10 VRRFFAKEVApfHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPGLSLHTDIVSP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 152 GIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLseDKKHYILNGSKVWITNGGLANIFTVFAKTev 231
Cdd:cd01160 90 YITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARK--DGDHYVLNGSKTFITNGMLADVVIVVART-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 232 vDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVV 311
Cdd:cd01160 166 -GGEARGAGGISLFLVERGTPGFSRGRKLKKMGWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 312 AGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAW 391
Cdd:cd01160 245 LAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAFLDNCAWRHEQGRLD--VAEASMAKYWATELQN 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 119599702 392 QCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01160 323 RVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELIS 368
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
88-437 |
9.14e-87 |
|
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: 275.09 E-value: 9.14e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 88 DQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIGLKgIILAGTEEQKAKYL 166
Cdd:cd01162 28 DQKKHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTgCVSTAAYISIHNMCAWM-IDSFGNDEQRERFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 167 PKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFAKTevvdsDGSVKDKITAFI 246
Cdd:cd01162 107 PDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGD--HYVLNGSKAFISGAGDSDVYVVMART-----GGEGPKGISCFV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 247 VERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYA 326
Cdd:cd01162 180 VEKGTPGLSFGANEKKMGWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 327 CTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGY 406
Cdd:cd01162 260 EERKQFGKPLADFQALQFKLADMATELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGY 338
|
330 340 350
....*....|....*....|....*....|.
gi 119599702 407 TRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:cd01162 339 LKDYPVEQYVRDLRVHQILEGTNEIMRLIIA 369
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
57-436 |
3.65e-80 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 259.04 E-value: 3.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 57 PEVSQDELNEinQFLGPVEKFFTEEV--DSRKIDQEGKIPDE-TLEKLK-SLGLFGLQVPEEYGGLGFSNTMYS-RLGEI 131
Cdd:PLN02519 22 SSLLFDDTQL--QFKESVQQFAQENIapHAAAIDATNSFPKDvNLWKLMgDFNLHGITAPEEYGGLGLGYLYHCiAMEEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 132 ISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEdkKHYILNGSK 211
Cdd:PLN02519 100 SRASGSVGLSYGAHSNLCINQLVRNGTPAQKEKYLPKLISGEHVGALAMSEPNSGSDVVSMKCKAERVD--GGYVLNGNK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 212 VWITNGGLANIFTVFAKTEVvdSDGSvkDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGD 291
Cdd:PLN02519 178 MWCTNGPVAQTLVVYAKTDV--AAGS--KGITAFIIEKGMPGFSTAQKLDKLGMRGSDTCELVFENCFVPEENVLGQEGK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 292 GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA-----LMAQKAYVMESMTYLTAGM 366
Cdd:PLN02519 254 GVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLAdmytsLQSSRSYVYSVARDCDNGK 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 367 LDQpgfPDCsieaAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYI 436
Cdd:PLN02519 334 VDR---KDC----AGVILCAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEIRRMLI 396
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
69-443 |
1.67e-74 |
|
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: 243.26 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 69 QFLGPVEKFFTEEV--DSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLAAHQ 146
Cdd:cd01157 7 EFQETARKFAREEIipVAAEYDKSGEYPWPLIKRAWELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEAN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 147 AIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKkhYILNGSKVWITNGGLANIFTVF 226
Cdd:cd01157 87 SLGQMPVIISGNDEQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDE--YIINGQKMWITNGGKANWYFLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 227 AKTEVvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFS 306
Cdd:cd01157 165 ARSDP-DPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 307 MGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPgfPDCSIEAAMVKVFS 386
Cdd:cd01157 244 VAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSG--RRNTYYASIAKAFA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 119599702 387 SEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQH 443
Cdd:cd01157 322 ADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHLGK 378
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
74-430 |
2.18e-68 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 228.28 E-value: 2.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 74 VEKFFTEEVD--SRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLG-EIISMDGSITVTLAAHQAIGL 150
Cdd:PTZ00461 48 VAKFSREVVDkhAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHhELSKYDPGFCLAYLAHSMLFV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKVWITNGGLANIFTVFAKte 230
Cdd:PTZ00461 128 NNFYYSASPAQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGN-YVLNGSKIWITNGTVADVFLIYAK-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 231 vvdsdgsVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSV 310
Cdd:PTZ00461 205 -------VDGKITAFVVERGTKGFTQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 311 VAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLdQPGFPDcSIEAAMVKVFSSEAA 390
Cdd:PTZ00461 278 AVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-HPGNKN-RLGSDAAKLFATPIA 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 119599702 391 WQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:PTZ00461 356 KKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIE 395
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
74-442 |
2.56e-68 |
|
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: 227.24 E-value: 2.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 74 VEKFFTEEVDSRKID--QEGKIPDETLEKLKSLGLFGLQvPEEYGGLGFSNTMYSRLG-EIISMDGSITVTLAAHQAIGL 150
Cdd:cd01151 24 AREFCQEELAPRVLEayREEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLIArEVERVDSGYRSFMSVQSSLVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlsEDKKHYILNGSKVWITNGGLANIFTVFAKTE 230
Cdd:cd01151 103 LPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRAR--KDGGGYKLNGSKTWITNSPIADVFVVWARND 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 231 vvdsdgsVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVgDGFKVAMNILNSGRFSMGSV 310
Cdd:cd01151 181 -------ETGKIRGFILERGMKGLSAPKIQGKFSLRASITGEIVMDNVFVPEENLLPGA-EGLRGPFKCLNNARYGIAWG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 311 VAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGF-PDcsiEAAMVKVFSSEA 389
Cdd:cd01151 253 ALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIALGLLACLRVGRLKDQGKAtPE---QISLLKRNNCGK 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 119599702 390 AWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI--LRMYIALTGLQ 442
Cdd:cd01151 330 ALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIhaLILGRAITGIQ 384
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
85-431 |
1.23e-63 |
|
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: 215.33 E-value: 1.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 85 RKIDQEG--------KIPDETLEKLKSL---GLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIglKG 152
Cdd:cd01153 18 ADGDREGpvfddgrvVVPPPFKEALDAFaeaGWMALGVPEEYGGQGLPITVYSALAEIFSRgDAPLMYASGTQGAA--AT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 153 IILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYIlNGSKVWITNG---GLANIF-TVFAK 228
Cdd:cd01153 96 LLAHGTEAQREKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVYQADGSWRI-NGVKRFISAGehdMSENIVhLVLAR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 229 TEVVDSDgsVKDkITAFIV-ERDFGGVTNG----KPEDKLGIRGSNTCEVHFENTKIPvenILGEVGDGFKVAMNILNSG 303
Cdd:cd01153 175 SEGAPPG--VKG-LSLFLVpKFLDDGERNGvtvaRIEEKMGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 304 RFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQE------KFALMAQKAYVMES--MTYLTAGMLDQPGFPDC 375
Cdd:cd01153 249 RLGVGTQGTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIihhpdvRRSLMTQKAYAEGSraLDLYTATVQDLAERKAT 328
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119599702 376 SIEAA------------MVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEI 431
Cdd:cd01153 329 EGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEGTTGI 396
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
74-437 |
1.77e-53 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 187.24 E-value: 1.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 74 VEKFFTEEvDSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSN-TMYSRLGEIISMDGSITVTlaaHQAIGLKG 152
Cdd:PRK12341 20 ITRNFPEE-YFRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYvTQMLVLEEVSKCGAPAFLI---TNGQCIHS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 153 IILAGTEEQKAK-YLPKLASGEhiAAFCL--TEPASGSDAASIRSRATlSEDKKHYiLNGSKVWITNGGLANIFTVFAKt 229
Cdd:PRK12341 96 MRRFGSAEQLRKtAESTLETGD--PAYALalTEPGAGSDNNSATTTYT-RKNGKVY-LNGQKTFITGAKEYPYMLVLAR- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 230 evvDSDGSVKDK-ITAFIVERDFGGVTNgKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMG 308
Cdd:PRK12341 171 ---DPQPKDPKKaFTLWWVDSSKPGIKI-NPLHKIGWHMLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 309 SVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQpGFPdCSIEAAMVKVFSSE 388
Cdd:PRK12341 247 ARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADN-GQS-LRTSAALAKLYCAR 324
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 119599702 389 AAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILrMYIA 437
Cdd:PRK12341 325 TAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIM-IYIA 372
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
100-442 |
2.03e-50 |
|
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: 179.08 E-value: 2.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 100 KLKSLGLFGLQVPEEYGGLGFS-------NTMYSRLGEIISMdGSITVTLAAHqaiglkgIILA-GTEEQKAKYLPKLAS 171
Cdd:cd01152 43 ALAAAGWAAPGWPKEYGGRGASlmeqlifREEMAAAGAPVPF-NQIGIDLAGP-------TILAyGTDEQKRRFLPPILS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 172 GEHIaaFCL--TEPASGSDAASIRSRATLSEDkkHYILNGSKVWITNGGLANIFTVFAKTevvdsDGSVK--DKITAFIV 247
Cdd:cd01152 115 GEEI--WCQgfSEPGAGSDLAGLRTRAVRDGD--DWVVNGQKIWTSGAHYADWAWLLVRT-----DPEAPkhRGISILLV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 248 ERDFGGVT-------NGKPEdklgirgsnTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIe 320
Cdd:cd01152 186 DMDSPGVTvrpirsiNGGEF---------FNEVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLL- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 321 mtaEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPDcsIEAAMVKVFSSEAAwQCVSE-ALQ 399
Cdd:cd01152 256 ---ARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPG--AEASIAKLFGSELA-QELAElALE 329
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 119599702 400 ILGGLGYTRDYP--------YERILRDTRILLIFEGTNEILRMYIALTGLQ 442
Cdd:cd01152 330 LLGTAALLRDPApgaelagrWEADYLRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
75-442 |
1.27e-49 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 176.95 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 75 EKFFTEevdsrkIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMDGSITVTLaaHQ-AIGLKGI 153
Cdd:PRK03354 26 EAYFAE------CDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVL--YQlPGGFNTF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 154 ILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATlSEDKKHYiLNGSKVWITNGGLANIFTVFAKtevvD 233
Cdd:PRK03354 98 LREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYT-RRNGKVY-LNGSKCFITSSAYTPYIVVMAR----D 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 234 SDGSVKDKITAFIVERDFGGVTNGKPEdKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAG 313
Cdd:PRK03354 172 GASPDKPVYTEWFVDMSKPGIKVTKLE-KLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 314 LLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAWQC 393
Cdd:PRK03354 251 TAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTIT--SGDAAMCKYFCANAAFEV 328
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 119599702 394 VSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEilrMYIALTGLQ 442
Cdd:PRK03354 329 VDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDE---MQILTLGRA 374
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
73-442 |
6.85e-46 |
|
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: 167.18 E-value: 6.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 73 PVEKFFTEEVdsRKIDQEGKIPDETLEKLK----SLGLFGLQVPEEYGGLGFSNTMYSRLGEII--SMDGSITVTLAAHQ 146
Cdd:cd01155 20 PAEQEFLEYY--AEGGDRWWTPPPIIEKLKakakAEGLWNLFLPEVSGLSGLTNLEYAYLAEETgrSFFAPEVFNCQAPD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 147 AIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPA-SGSDAASIRsrATLSEDKKHYILNGSKVWITNGG--LANIF 223
Cdd:cd01155 98 TGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIE--CSIERDGDDYVINGRKWWSSGAGdpRCKIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 224 TVFAKTevvDSDGSVKDKITAFI-VERDFGGVTNGKPedkLGIRGSNT-----CEVHFENTKIPVENILGEVGDGFKVAM 297
Cdd:cd01155 176 IVMGRT---DPDGAPRHRQQSMIlVPMDTPGVTIIRP---LSVFGYDDaphghAEITFDNVRVPASNLILGEGRGFEIAQ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 298 NILNSGRF--SMGSVvaGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFAlmaqKAYVMESMTYL----TAGMLDQPG 371
Cdd:cd01155 250 GRLGPGRIhhCMRLI--GAAERALELMCQRAVSREAFGKKLAQHGVVAHWIA----KSRIEIEQARLlvlkAAHMIDTVG 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119599702 372 FPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQ 442
Cdd:cd01155 324 NKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
290-437 |
5.13e-44 |
|
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: 153.95 E-value: 5.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 290 GDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQ 369
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119599702 370 pGFPDcSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:pfam00441 81 -GGPD-GAEASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
41-405 |
2.56e-43 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 166.15 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 41 KELFLGK--IKKKEVFPFPEVSQDElneinQ-FL-GPVEKFfTEEVDSRKIDQE-GKIPDETLEKLKSLGLFGLQVPEEY 115
Cdd:PRK09463 59 GELFSGKpdWKKLLNYPKPTLTAEE-----QaFLdGPVEEL-CRMVNDWQITHElADLPPEVWQFIKEHGFFGMIIPKEY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 116 GGLGFSNTMYSR-LGEIISMDGSITVTLAAHQAIGlKGIILA--GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASI 192
Cdd:PRK09463 133 GGLEFSAYAHSRvLQKLASRSGTLAVTVMVPNSLG-PGELLLhyGTDEQKDHYLPRLARGEEIPCFALTSPEAGSDAGSI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 193 RS-----RATLSEDKKHYI-LNGSKVWITnggLANIFTVFA---KteVVDSDGSVKDK----ITAFIVERDFGGVTNGKP 259
Cdd:PRK09463 212 PDtgvvcKGEWQGEEVLGMrLTWNKRYIT---LAPIATVLGlafK--LYDPDGLLGDKedlgITCALIPTDTPGVEIGRR 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 260 EDKLGirgsntceVHFEN--TK-----IPVENILGE---VGDGFKVAMNILNSGR-FSMGSVVAGLLKRLIEMTAEYACT 328
Cdd:PRK09463 287 HFPLN--------VPFQNgpTRgkdvfIPLDYIIGGpkmAGQGWRMLMECLSVGRgISLPSNSTGGAKLAALATGAYARI 358
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119599702 329 RKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPdcSIEAAMVKVFSSEAAWQCVSEALQILGGLG 405
Cdd:PRK09463 359 RRQFKLPIGKFEGIEEPLARIAGNAYLMDAARTLTTAAVDLGEKP--SVLSAIAKYHLTERGRQVINDAMDIHGGKG 433
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
20-405 |
1.70e-39 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 154.73 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 20 LVVSTANRRLLRTSPPVRAFAK-----------------------ELFLGK--IKKKEVFPFPEVSQDElneiNQFL-GP 73
Cdd:PRK13026 14 LVFAVKPLRRQFITRPVFKFFKkvlpplsdtereameagdvwwegELFSGKpdWQKLHSYPKPTLTAEE----QAFIdNE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 74 VEKFFTEeVDSRKIDQEGK-IPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRL-GEIISMDGSITVTLAAHQAIGlK 151
Cdd:PRK13026 90 VETLLTM-LDDWDIVQNRKdLPPEVWDYLKKEGFFALIIPKEYGGKGFSAYANSTIvSKIATRSVSAAVTVMVPNSLG-P 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 152 GIILA--GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSE---DKKHYI---LNGSKVWITnggLANIF 223
Cdd:PRK13026 168 GELLThyGTQEQKDYWLPRLADGTEIPCFALTGPEAGSDAGAIPDTGIVCRgefEGEEVLglrLTWDKRYIT---LAPVA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 224 TV----FaktEVVDSDGSVKDK----ITAFIVERDFGGVTNGKPEDKLGIR---GSNTCEVHFentkIPVENILG---EV 289
Cdd:PRK13026 245 TVlglaF---KLRDPDGLLGDKkelgITCALIPTDHPGVEIGRRHNPLGMAfmnGTTRGKDVF----IPLDWIIGgpdYA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 290 GDGFKVAMNILNSGR-FSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLD 368
Cdd:PRK13026 318 GRGWRMLVECLSAGRgISLPALGTASGHMATRTTGAYAYVRRQFGMPIGQFEGVQEALARIAGNTYLLEAARRLTTTGLD 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 119599702 369 QPGFPdcSIEAAMVKVFSSEAAWQCVSEALQILGGLG 405
Cdd:PRK13026 398 LGVKP--SVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
89-431 |
2.71e-37 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 143.45 E-value: 2.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 89 QEGKIPDETLEKLKSLGLFGLQVpEEYGGLGFSNTMYS-RLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLP 167
Cdd:PLN02526 57 EKAEFPFHIIPKLGSLGIAGGTI-KGYGCPGLSITASAiATAEVARVDASCSTFILVHSSLAMLTIALCGSEAQKQKYLP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 168 KLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKkhYILNGSKVWITNGGLANIFTVFAKTevvdsdgSVKDKITAFIV 247
Cdd:PLN02526 136 SLAQLDTVACWALTEPDYGSDASSLNTTATKVEGG--WILNGQKRWIGNSTFADVLVIFARN-------TTTNQINGFIV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 248 ERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVgDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYAC 327
Cdd:PLN02526 207 KKGAPGLKATKIENKIGLRMVQNGDIVLKDVFVPDEDRLPGV-NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCHRYLK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 328 TRKQFNKRLSEFGLIQEKFALMAQKAYVMESM------TYLTAGMldQPGfpdcsiEAAMVKVFSSEAAWQCVSEALQIL 401
Cdd:PLN02526 286 ERKQFGAPLAAFQINQEKLVRMLGNIQAMFLVgwrlckLYESGKM--TPG------HASLGKAWITKKARETVALGRELL 357
|
330 340 350
....*....|....*....|....*....|
gi 119599702 402 GGLGYTRDYPYERILRDTRILLIFEGTNEI 431
Cdd:PLN02526 358 GGNGILADFLVAKAFCDLEPIYTYEGTYDI 387
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
138-432 |
1.00e-33 |
|
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: 133.65 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 138 ITVTLAAhqaigLKGIILAGTEEQKaKYLPKLASGEH----IAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKvW 213
Cdd:cd01154 113 LTMTDAA-----VYALRKYGPEELK-QYLPGLLSDRYktglLGGTWMTEKQGGSDLGANETTAERSGGGV-YRLNGHK-W 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 214 ITNGGLANIFTVFAKTEvvDSDGSVKDkITAFIVER-DFGGVTNG----KPEDKLGIRGSNTCEVHFENTkipVENILGE 288
Cdd:cd01154 185 FASAPLADAALVLARPE--GAPAGARG-LSLFLVPRlLEDGTRNGyrirRLKDKLGTRSVATGEVEFDDA---EAYLIGD 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 289 VGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLD 368
Cdd:cd01154 259 EGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFD 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119599702 369 QPGfPDCSIEAAMVKVFS-------SEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEIL 432
Cdd:cd01154 339 RAA-ADKPVEAHMARLATpvakliaCKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNIQ 408
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
8-431 |
2.05e-31 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 129.60 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 8 LRTTAAARACRGLVVSTANRRLLRTSPPVR--AFAKELFLGKIKKKEVFPFPEVSQDELNEInqfLGPVEKFFTE----- 80
Cdd:PTZ00456 2 FRRVCSSAAASHAAAVSASARSLQYQPRIRdvQFLVEEVFNMYDHYEKLGKTDVTKELMDSL---LEEASKLATQtllpl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 81 ----EVDSRKIDQEGKIP-----DETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISMdGSITVTLAAHQAIG-L 150
Cdd:PTZ00456 79 yessDSEGCVLLKDGNVTtpkgfKEAYQALKAGGWTGISEPEEYGGQALPLSVGFITRELMAT-ANWGFSMYPGLSIGaA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 151 KGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKhYILNGSKVWITNGG---LANI-FTVF 226
Cdd:PTZ00456 158 NTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGS-YKITGTKIFISAGDhdlTENIvHIVL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 227 AKTEvvDSDGSVKDkITAFIVER----DFGGVTNGKP------EDKLGIRGSNTCEVHFENTkipVENILGEVGDGFKVA 296
Cdd:PTZ00456 237 ARLP--NSLPTTKG-LSLFLVPRhvvkPDGSLETAKNvkciglEKKMGIKGSSTCQLSFENS---VGYLIGEPNAGMKQM 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 297 MNILNSGRfsMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFA------------LMAQKAyVME---SMTY 361
Cdd:PTZ00456 311 FTFMNTAR--VGTALEGVCHAELAFQNALRYARERRSMRALSGTKEPEKPAdriichanvrqnILFAKA-VAEggrALLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 362 LTAGMLD-QPGFPDCSIEAAM----------VKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:PTZ00456 388 DVGRLLDiHAAAKDAATREALdheigfytpiAKGCLTEWGVEAASRCLQVWGGHGYIKGNGMEQILRDARIGTLYEGTTG 467
|
.
gi 119599702 431 I 431
Cdd:PTZ00456 468 I 468
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
74-173 |
3.68e-29 |
|
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: 111.79 E-value: 3.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 74 VEKFFTEEV--DSRKIDQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFSNTMYSRLGEIISM-DGSITVTLAAHQAIGL 150
Cdd:pfam02771 11 VREFAEEEIapHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARaDASVALALSVHSSLGA 90
|
90 100
....*....|....*....|...
gi 119599702 151 KGIILAGTEEQKAKYLPKLASGE 173
Cdd:pfam02771 91 PPILRFGTEEQKERYLPKLASGE 113
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
177-276 |
5.10e-28 |
|
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: 107.75 E-value: 5.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 177 AFCLTEPASGSDAASIRSRAtLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEvvdsDGSVKDKITAFIVERDFGGVTN 256
Cdd:pfam02770 1 AFALTEPGAGSDVASLKTTA-ADGDGGGWVLNGTKWWITNAGIADLFLVLARTG----GDDRHGGISLFLVPKDAPGVSV 75
|
90 100
....*....|....*....|
gi 119599702 257 GKPEDKLGIRGSNTCEVHFE 276
Cdd:pfam02770 76 RRIETKLGVRGLPTGELVFD 95
|
|
| PTZ00457 |
PTZ00457 |
acyl-CoA dehydrogenase; Provisional |
27-571 |
2.17e-27 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185636 [Multi-domain] Cd Length: 520 Bit Score: 116.52 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 27 RRLLRTSP--PVR--AFAKELFLGKIKKKEVFPFPevsqdelneinqflgpvekffteevdSRKID-QEGKIPDETLEKL 101
Cdd:PTZ00457 2 RRRFSSAPrqYVRhaSYAAGLFNFKIVPEEMFPYP--------------------------CRKLDgDEAENLQSLLEQI 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 102 KSLG-----LFGLQVPEEYGGLGFSNTMYSRLGEIISMDGsITVTLAAHQAIGLKGIILA--GTEEQKAKYLPKLASGEH 174
Cdd:PTZ00457 56 RSNDkilgnLYGARIATEYGGLGLGHTAHALIYEEVGTNC-DSKLLSTIQHSGFCTYLLStvGSKELKGKYLTAMSDGTI 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 175 IAAFClTEPASGSDAASIRSRATLSEDKKhYILNGSKvWITNGGLANIFTVFAKT---EVVDSDGSVKDKITAFIVERDF 251
Cdd:PTZ00457 135 MMGWA-TEEGCGSDISMNTTKASLTDDGS-YVLTGQK-RCEFAASATHFLVLAKTltqTAAEEGATEVSRNSFFICAKDA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 252 GGVTngkpedklgIRGSNtceVHFENTkiPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEmtaeyactrkQ 331
Cdd:PTZ00457 212 KGVS---------VNGDS---VVFENT--PAADVVGVVGEGFKDAMITLFTEQYLYAASLLGIMKRVVQ----------E 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 332 FNKRLSEFGlIQEKFALMAQKAYVMESMTYLTAGMLDQPGfPDCSIEAAMVKVFSSEAawqcVSEALQILgGLGYTRDYP 411
Cdd:PTZ00457 268 LRGSNAEEG-ATDTVASFACAMYAMESTLYALTANLDLPT-EDSLLECTLVSAFVQST----TNQLLSIL-ETATPPSTT 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 412 YERILRDTRILLIFEGTNEILRMYIALTGLQHAG----RILTTRIHELKQAKVSTVMDTVG-RRLRDSlgrtvdlgltgn 486
Cdd:PTZ00457 341 LEKCFANARLFLSMMESRDFLYSSAVCCGVEDYGlffqRASTLQMMQARTLRSLGVRDRVPiKNLPDC------------ 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 487 hgvvhpSLADSAnkfeenTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVL 566
Cdd:PTZ00457 409 ------SLIDEA------VVAFGNAVEATFVRSGSQVPYQQLLLNRLGEAASLLYAASAVASRASMCVSKGLPSAKVEGE 476
|
....*
gi 119599702 567 LANTF 571
Cdd:PTZ00457 477 LASAF 481
|
|
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
117-444 |
2.87e-20 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 95.25 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 117 GLGFSNTMYSRLGEII--SMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEP-ASGSDAASIR 193
Cdd:PLN02876 491 GAGLSNLEYGYLCEIMgrSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPqVASSDATNIE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 194 srATLSEDKKHYILNGSKvWITNGGL---ANIFTVFAKTevvDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGS-- 268
Cdd:PLN02876 571 --CSIRRQGDSYVINGTK-WWTSGAMdprCRVLIVMGKT---DFNAPKHKQQSMILVDIQTPGVQIKRPLLVFGFDDAph 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 269 NTCEVHFENTKIPVENI-LGEvGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGliqeKFA 347
Cdd:PLN02876 645 GHAEISFENVRVPAKNIlLGE-GRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHG----SFL 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 348 LMAQKAYVMESMTYL----TAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILL 423
Cdd:PLN02876 720 SDLAKCRVELEQTRLlvleAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATARTLR 799
|
330 340
....*....|....*....|.
gi 119599702 424 IFEGTNEILRMYIALTGLQHA 444
Cdd:PLN02876 800 IADGPDEVHLGTIAKLELQRA 820
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
99-462 |
1.67e-16 |
|
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: 83.15 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 99 EKLKSLGLFGLQVPEEYGGLGFSNTMYsrlgeiismDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAF 178
Cdd:cd01150 68 TDVERMGELMADDPEKMLALTNSLGGY---------DLSLGAKLGLHLGLFGNAIKNLGTDEHQDYWLQGANNLEIIGCF 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 179 CLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWItnGGL---ANIFTVFAKTEVVDSDGSVKdkitAFIVE-R 249
Cdd:cd01150 139 AQTELGHGSNLQGLETTATYDPLTQEFVINtpdftATKWWP--GNLgktATHAVVFAQLITPGKNHGLH----AFIVPiR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 250 DFG------GVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGD----------------GFKVAMNILNSGRFSM 307
Cdd:cd01150 213 DPKthqplpGVTVGDIGPKMGLNGVDNGFLQFRNVRIPRENLLNRFGDvspdgtyvspfkdpnkRYGAMLGTRSGGRVGL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 308 GSVVAGLLKRLIEMTAEYACTRKQFNKRLS-------EFGLIQEKFALMAQKAYV------------MESMTYLTAGMLD 368
Cdd:cd01150 293 IYDAAMSLKKAATIAIRYSAVRRQFGPKPSdpevqilDYQLQQYRLFPQLAAAYAfhfaakslvemyHEIIKELLQGNSE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 369 QpgFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTrDYPYERILR-DTRILLIFEGTNEILrmyialtgLQHAGRI 447
Cdd:cd01150 373 L--LAELHALSAGLKAVATWTAAQGIQECREACGGHGYL-AMNRLPTLRdDNDPFCTYEGDNTVL--------LQQTANY 441
|
410
....*....|....*
gi 119599702 448 LTTRIHELKQAKVST 462
Cdd:cd01150 442 LLKKYAQAFSLADYL 456
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
88-287 |
5.50e-15 |
|
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: 76.98 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 88 DQEGKIPDETLEKLKSLGLFGLQVPEEYGGLGFS-NTMYSRLGEIISMDGSITVTLAAHQAIgLKGIILAGTEEQKAKYL 166
Cdd:cd01163 18 DRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASlPDLYEVVRELAAADSNIAQALRAHFGF-VEALLLAGPEQFRKRWF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 167 PKLASGeHIAAFCLTEpaSGSDAASIRSRATLSEDkKHYILNGSKvWITNGGLaniFTVFAKTEVVDSDGsvkdKITAFI 246
Cdd:cd01163 97 GRVLNG-WIFGNAVSE--RGSVRPGTFLTATVRDG-GGYVLNGKK-FYSTGAL---FSDWVTVSALDEEG----KLVFAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 119599702 247 VERDFGGVTNGKPEDKLGIR--GSNTceVHFENTKIPVENILG 287
Cdd:cd01163 165 VPTDRPGITVVDDWDGFGQRltASGT--VTFDNVRVEPDEVLP 205
|
|
| PLN02636 |
PLN02636 |
acyl-coenzyme A oxidase |
133-437 |
1.47e-11 |
|
acyl-coenzyme A oxidase
Pssm-ID: 215342 [Multi-domain] Cd Length: 686 Bit Score: 67.58 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 133 SMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN---- 208
Cdd:PLN02636 132 SVDMSLGIKLGVQYSLWGGSVINLGTKKHRDKYFDGIDNLDYPGCFAMTELHHGSNVQGLQTTATFDPLTDEFVINtpnd 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 209 -GSKVWITNGGLANIF-TVFAKTEVV--DSDGSVKDKITAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFEN 277
Cdd:PLN02636 212 gAIKWWIGNAAVHGKFaTVFARLKLPthDSKGVSDMGVHAFIVPiRDMKthqvlpGVEIRDCGHKVGLNGVDNGALRFRS 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 278 TKIPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFN-KRLSEFG 340
Cdd:PLN02636 292 VRIPRDNLLNRFGDvsrdgkytsslptinkRFAATLGELVGGRVGLAYGSVGVLKASNTIAIRYSLLRQQFGpPKQPEIS 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 341 LI-----QEKFALMAQKAYVMESMT-YLT---AGML---DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTR 408
Cdd:PLN02636 372 ILdyqsqQHKLMPMLASTYAFHFATeYLVerySEMKkthDDQLVADVHALSAGLKAYITSYTAKALSTCREACGGHGYAA 451
|
330 340
....*....|....*....|....*....
gi 119599702 409 DYPYERILRDTRILLIFEGTNEILRMYIA 437
Cdd:PLN02636 452 VNRFGSLRNDHDIFQTFEGDNTVLLQQVA 480
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
180-432 |
1.80e-11 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 66.70 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 180 LTEPASGSDAASIRSRATLSEDKKhYILNGSKvWITNGGLANIFTVFAKTevvdsdgsvKDKITAFIVERDF-GGVTNG- 257
Cdd:PRK11561 184 MTEKQGGSDVLSNTTRAERLADGS-YRLVGHK-WFFSVPQSDAHLVLAQA---------KGGLSCFFVPRFLpDGQRNAi 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 258 ---KPEDKLGIRGSNTCEVHFENTkipVENILGEVGDGFKvamNILNSG---RF--SMGSvvAGLLKRLIEMTAEYACTR 329
Cdd:PRK11561 253 rleRLKDKLGNRSNASSEVEFQDA---IGWLLGEEGEGIR---LILKMGgmtRFdcALGS--HGLMRRAFSVAIYHAHQR 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 330 KQFNKRLSEFGLIQEkfaLMAQKAYVMESMTYLT---AGMLDQPGFPDcsiEAAMVKVFSSEAAWQ-C------VSEALQ 399
Cdd:PRK11561 325 QVFGKPLIEQPLMRQ---VLSRMALQLEGQTALLfrlARAWDRRADAK---EALWARLFTPAAKFViCkrgipfVAEAME 398
|
250 260 270
....*....|....*....|....*....|...
gi 119599702 400 ILGGLGYTRDYPYERILRDTRILLIFEGTNEIL 432
Cdd:PRK11561 399 VLGGIGYCEESELPRLYREMPVNSIWEGSGNIM 431
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
306-430 |
4.42e-09 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 55.04 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 306 SMGSVVAGLLKRLIEMTAEYACTRKQ--FNKRLSEFGLIQEKFALMA----QKAYVMESMTYLTAGMLDQ--PGFPDCSI 377
Cdd:pfam08028 1 GIAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAaridAARLLLERAAARIEAAAAAgkPVTPALRA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 119599702 378 EAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNE 430
Cdd:pfam08028 81 EARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQHAAVNP 133
|
|
| PTZ00460 |
PTZ00460 |
acyl-CoA dehydrogenase; Provisional |
143-547 |
3.67e-07 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185639 [Multi-domain] Cd Length: 646 Bit Score: 53.31 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 143 AAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWITN- 216
Cdd:PTZ00460 96 TVHFAMVIPAFQVLGTDEQINLWMPSLLNFEIVGCYAQTELGHGSDVQNLETTATYDKQTNEFVIHtpsveAVKFWPGEl 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 217 GGLANIFTVFAKTEVvdsDGSVKDkITAFIVE-RDFG------GVTNGKPEDKLGIRGSNTCEVHFENTKIPVENIL--- 286
Cdd:PTZ00460 176 GFLCNFALVYAKLIV---NGKNKG-VHPFMVRiRDKEthkplqGVEVGDIGPKMGYAVKDNGFLSFDHYRIPLDSLLary 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 287 ------GEV---GDGfKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNK------RLSEFGLIQEK-FALMA 350
Cdd:PTZ00460 252 ikvsedGQVerqGNP-KVSYASMMYMRNLIIDQYPRFAAQALTVAIRYSIYRQQFTNdnkqenSVLEYQTQQQKlLPLLA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 351 QkAYVMeSMTYLTAGMLDQPGF-----PDCSIEAAMVKVFSSEAAW--QCVSEALQ----ILGGLGYTRDYPYERILRDT 419
Cdd:PTZ00460 331 E-FYAC-IFGGLKIKELVDDNFnrvqkNDFSLLQLTHAILSAAKANytYFVSNCAEwcrlSCGGHGYAHYSGLPAIYFDM 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 420 RILLIFEGTNEILRMYIA---LTGLQHA-----------GRILT-----------TRIHELKQAKVSTVMDTVGRRLRDS 474
Cdd:PTZ00460 409 SPNITLEGENQIMYLQLArylLKQLQHAvqkpekvpeyfNFLSHitekladqttiESLGQLLGLNCTILTIYAAKKIMDH 488
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119599702 475 LGRTVDLGLTGNHgVVHPSLADSANKFEEN-TYcfgrtvetllLRFGKTIMEEQLVLKRVANILINLYGMTAVL 547
Cdd:PTZ00460 489 INTGKDFQQSWDT-KSGIALASAASRFIEYfNY----------LCFLDTINNANKSTKEILTQLADLYGITMLL 551
|
|
| PLN02443 |
PLN02443 |
acyl-coenzyme A oxidase |
157-406 |
9.33e-06 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178062 [Multi-domain] Cd Length: 664 Bit Score: 48.68 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 157 GTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILN-----GSKVWitNGGLANIFT---VFAK 228
Cdd:PLN02443 114 GTEEQQKKWLPLAYKMQIIGCYAQTELGHGSNVQGLETTATFDPKTDEFVIHsptltSSKWW--PGGLGKVSThavVYAR 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 229 tevVDSDGsvKDK-ITAFIVE-------RDFGGVTNGKPEDKLGIRGSNTCE---VHFENTKIPVENILGEVG----DGF 293
Cdd:PLN02443 192 ---LITNG--KDHgIHGFIVQlrslddhSPLPGVTVGDIGMKFGNGAYNTMDngfLRFDHVRIPRDQMLMRLSkvtrEGK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 294 KVAMNI---LNSGR--FSMGSVVAG---LLKRLIEMTAEYACTRKQFNKRLS--EFGLIQEK------FALMAQkAY--- 354
Cdd:PLN02443 267 YVQSDVprqLVYGTmvYVRQTIVADastALSRAVCIATRYSAVRRQFGSQDGgpETQVIDYKtqqsrlFPLLAS-AYafr 345
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 119599702 355 -VMESMTYLTAGML------DQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGY 406
Cdd:PLN02443 346 fVGEWLKWLYTDVTqrleanDFSTLPEAHACTAGLKSLTTSATADGIEECRKLCGGHGY 404
|
|
| PLN02312 |
PLN02312 |
acyl-CoA oxidase |
128-332 |
2.98e-05 |
|
acyl-CoA oxidase
Pssm-ID: 215178 [Multi-domain] Cd Length: 680 Bit Score: 47.07 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 128 LGEIISM-DGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYI 206
Cdd:PLN02312 138 LLEVIGIyDHSLAIKLGVHFFLWGGAIKFLGTKRHHDKWLKDTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFV 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119599702 207 LN-----GSKVWItnGGLANIFT---VFAKTEVvdsDGsVKDKITAFIVE-RDFGGVT--NGKPED---KLGIRGSNTCE 272
Cdd:PLN02312 218 INtpcesAQKYWI--GGAANHAThtiVFSQLHI---NG-KNEGVHAFIAQiRDQDGNIcpNIRIADcghKIGLNGVDNGR 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119599702 273 VHFENTKIPVENILGEVGD----------------GFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQF 332
Cdd:PLN02312 292 IWFDNLRIPRENLLNSVADvspdgkyvsaikdpdqRFGAFLAPLTSGRVTIAVSAIYSSKVGLAIAIRYSLSRRAF 367
|
|
|