|
Name |
Accession |
Description |
Interval |
E-value |
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
36-400 |
1.05e-57 |
|
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: 198.53 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 36 FAARMRELDAAEAFPTEAVARLDALGLPAQYVPARHGGTLDSYEDLLQLVRVVARRDLTVAIAHTKTYLGAVSTWVGGTA 115
Cdd:COG1960 24 IAPEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADASLALPVGVHNGAAEALLRFGTE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 116 EQAQELGARIASGA-VVSWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTRGYSLL 194
Cdd:COG1960 104 EQKERYLPRLASGEwIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFITNAPVADVILVLARTDPAAGHRGISLF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 195 LVDKAllADGShTCLPAAKTHGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHALRIA 274
Cdd:COG1960 184 LVPKD--TPGV-TVGRIEDKMGLRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 275 TRFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVTLLASRGVHTlTEEMSVSSAAVKYLVPTTADELITGMGQFLGA 354
Cdd:COG1960 261 VAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLDA-GEDAALEAAMAKLFATEAALEVADEALQIHGG 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2020605850 355 RSFLSEefaHGLfAKLERDHRIVGIFDGNTLVNLNALINQFAALAR 400
Cdd:COG1960 340 YGYTRE---YPL-ERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
103-391 |
5.79e-52 |
|
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: 181.33 E-value: 5.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 103 YLGAVSTWVGGTAEQAQELGARIASG-AVVSWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLAR 181
Cdd:cd00567 42 LLGAALLLAYGTEEQKERYLPPLASGeAIAAFALTEPGAGSDLAGIRTTARKDGDGYVLNGRKIFISNGGDADLFIVLAR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 182 TSLAG-GTRGYSLLLVDKAllADGShTCLPAAKTHGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICA 260
Cdd:cd00567 122 TDEEGpGHRGISAFLVPAD--TPGV-TVGRIWDKMGMRGSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRLLLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 261 SLSLGAGDHALRIATRFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVTLLASRGVHTLTEEMSVSSAAVKYLVPTT 340
Cdd:cd00567 199 AVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQGPDEARLEAAMAKLFATEA 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2020605850 341 ADELITGMGQFLGARSFLSEefahGLFAKLERDHRIVGIFDGNTLVNLNAL 391
Cdd:cd00567 279 AREVADLAMQIHGGRGYSRE----YPVERYLRDARAARIAEGTAEIQRLII 325
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
37-389 |
5.31e-34 |
|
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: 133.16 E-value: 5.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 37 AARMRELDAAEAFPTEAVARLDALGLPAQYVPARHGGTLDSYEDLLQLVRVVARRDLTVAI---AHTKTYLGAVSTWvgG 113
Cdd:cd01158 19 APLAAEMDEKGEFPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELAKVDASVAVivsVHNSLGANPIIKF--G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 114 TAEQAQELGARIASG-AVVSWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTRGYS 192
Cdd:cd01158 97 TEEQKKKYLPPLATGeKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGEADFYIVFAVTDPSKGYRGIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 193 LLLVDKAllADGSHTCLPAAKThGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHALR 272
Cdd:cd01158 177 AFIVERD--TPGLSVGKKEDKL-GIRGSSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 273 IATRFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVTLLASRgvhtLTEE---MSVSSAAVKYLVPTTADELITGMG 349
Cdd:cd01158 254 AAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAAR----LKDNgepFIKEAAMAKLFASEVAMRVTTDAV 329
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2020605850 350 QFLGARSFlSEEFAhglFAKLERDHRIVGIFDGNTLVNLN 389
Cdd:cd01158 330 QIFGGYGY-TKDYP---VERYYRDAKITEIYEGTSEIQRL 365
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
41-387 |
6.44e-23 |
|
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: 101.39 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 41 RELDAAEAFPTEAVARLDALGLPAQYVPARHGG---TLDSYEDLLQLVRVVARRDLTVAIAHTKTYLGAVstwVGGTAEQ 117
Cdd:cd01161 49 AKNDQLEKIPRKTLTQLKELGLFGLQVPEEYGGlglNNTQYARLAEIVGMDLGFSVTLGAHQSIGFKGIL---LFGTEAQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 118 AQELGARIASGAVV-SWGLTERAHGSDLLSGELTATPVAGG--YRLDGEKWLINNATRSDLVCVLARTSLAGGT----RG 190
Cdd:cd01161 126 KEKYLPKLASGEWIaAFALTEPSSGSDAASIRTTAVLSEDGkhYVLNGSKIWITNGGIADIFTVFAKTEVKDATgsvkDK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 191 YSLLLVDKALladGSHTCLPAAKTHGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHA 270
Cdd:cd01161 206 ITAFIVERSF---GGVTNGPPEKKMGIKGSNTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRC 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 271 LRIATRFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVT-LLASRGVHTLTEEMSVSSAAVKYLVPTTADELITGMG 349
Cdd:cd01161 283 IEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAyMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAI 362
|
330 340 350
....*....|....*....|....*....|....*...
gi 2020605850 350 QFLGARSFLSEefaHGLfAKLERDHRIVGIFDGNTLVN 387
Cdd:cd01161 363 QIHGGMGFMRE---YGV-ERVLRDLRIFRIFEGTNEIL 396
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
41-349 |
3.67e-21 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 96.16 E-value: 3.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 41 RELDAAEAFPTEAVARLDALGLPAQYVPARHGGT-LDSyedllqLVRVVARRDLT--------VAIAHTKTYLGavSTWV 111
Cdd:PTZ00461 61 REDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAgMDA------VAAVIIHHELSkydpgfclAYLAHSMLFVN--NFYY 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 112 GGTAEQAQELGARIASGAVV-SWGLTERAHGSDLLSGELTATPVA-GGYRLDGEKWLINNATRSDLVCVLARTS------ 183
Cdd:PTZ00461 133 SASPAQRARWLPKVLTGEHVgAMGMSEPGAGTDVLGMRTTAKKDSnGNYVLNGSKIWITNGTVADVFLIYAKVDgkitaf 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 184 -LAGGTRGYslllvdkalladgshTCLPAAKTHGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASL 262
Cdd:PTZ00461 213 vVERGTKGF---------------TQGPKIDKCGMRASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 263 SLGAGDHALRIATRFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVTLLASRGVHTLTEEMSVSSAAVKYLVPTT-- 340
Cdd:PTZ00461 278 AVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVHPGNKNRLGSDAAKLFATPIAkk 357
|
330
....*....|
gi 2020605850 341 -ADELITGMG 349
Cdd:PTZ00461 358 vADSAIQVMG 367
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
37-317 |
4.50e-21 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 95.56 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 37 AARMRELDAAEAFPTEAVARLDALGLPAQYVPARHGGTLDSYEDLLQLVRVVARRDLTVAI---AHTKTYLGAVSTWvgG 113
Cdd:cd01156 22 APLAAKIDRDNEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGSVALsygAHSNLCINQIYRN--G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 114 TAEQAQELGARIASGAVV-SWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTRGYS 192
Cdd:cd01156 100 SAAQKEKYLPKLISGEHIgALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKMWITNGPDADTLVVYAKTDPSAGAHGIT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 193 LLLVDKALlaDGSHTCLPAAKThGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHALR 272
Cdd:cd01156 180 AFIVEKGM--PGFSRAQKLDKL-GMRGSNTCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALD 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2020605850 273 IATRFGLEHRLYGKRLIDLpqahRALTEAYADLFameaVTLLASR 317
Cdd:cd01156 257 VAIPYAHQRKQFGQPIGEF----QLVQGKLADMY----TRLNASR 293
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
113-384 |
7.43e-21 |
|
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: 94.49 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 113 GTAEQAQELGARIASGAVVS-WGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTS-LAGGTRG 190
Cdd:cd01160 95 GSPEQKERVLPQMVAGKKIGaIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVVIVVARTGgEARGAGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 191 YSLLLVDKAllADGSHTCLPAAKThGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHA 270
Cdd:cd01160 175 ISLFLVERG--TPGFSRGRKLKKM-GWKAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAAGALAAAEFM 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 271 LRIATRFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMEA-VTLLASRgvHTLTEEMSVSSAAVKYLVPTTADELITGMG 349
Cdd:cd01160 252 LEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAfLDNCAWR--HEQGRLDVAEASMAKYWATELQNRVAYECV 329
|
250 260 270
....*....|....*....|....*....|....*
gi 2020605850 350 QFLGARSFLSEEFAhglfAKLERDHRIVGIFDGNT 384
Cdd:cd01160 330 QLHGGWGYMREYPI----ARAYRDARVQPIYGGTT 360
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
37-382 |
4.23e-19 |
|
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: 89.42 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 37 AARMRELDAAEAFPTEAVARLDALGLPAQYVPARHGGTldsyeDLLQLVRVVARRDLTVAIAHTKTYLGA--VSTWV--- 111
Cdd:cd01162 21 APHAADWDQKKHFPVDVLRKAAELGFGGIYIRDDVGGS-----GLSRLDASIIFEALSTGCVSTAAYISIhnMCAWMids 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 112 GGTAEQAQELGARIASGAVV-SWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSlAGGTRG 190
Cdd:cd01162 96 FGNDEQRERFLPDLCTMEKLaSYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDSDVYVVMARTG-GEGPKG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 191 YSLLLVDKAllADGSHTCLPAAKThGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHA 270
Cdd:cd01162 175 ISCFVVEKG--TPGLSFGANEKKM-GWNAQPTRAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 271 LRIATRFGLEHRLYGKRLIDLPQAHRALTEAYADLfamEAVTLLASRGVHTLTE---EMSVSSAAVKYLVPTTADELITG 347
Cdd:cd01162 252 LDLARAYLEERKQFGKPLADFQALQFKLADMATEL---VASRLMVRRAASALDRgdpDAVKLCAMAKRFATDECFDVANQ 328
|
330 340 350
....*....|....*....|....*....|....*
gi 2020605850 348 MGQFLGARSFLSEefaHGLfAKLERDHRIVGIFDG 382
Cdd:cd01162 329 ALQLHGGYGYLKD---YPV-EQYVRDLRVHQILEG 359
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
134-391 |
7.09e-19 |
|
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: 89.35 E-value: 7.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 134 GLTERAHGSDLLSGELTATPVAGG-YRLDGEKWLINNATrSDLVCVLARTSLA-GGTRGYSLLLVDKaLLADGSHTCLPA 211
Cdd:cd01154 152 WMTEKQGGSDLGANETTAERSGGGvYRLNGHKWFASAPL-ADAALVLARPEGApAGARGLSLFLVPR-LLEDGTRNGYRI 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 212 AKTH---GIRGADISGIAFDGAVvpaSALIGEEGEGIETVLRSLQITRTICASLSLGAGDHALRIATRFGLEHRLYGKRL 288
Cdd:cd01154 230 RRLKdklGTRSVATGEVEFDDAE---AYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 289 IDLPQAHRALTEAYADLFAMEAVTLLASRGVHTLTEEMSVS-------SAAVKYLVPTTADELITGMGQFLGARSFLsEE 361
Cdd:cd01154 307 IDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKPVEahmarlaTPVAKLIACKRAAPVTSEAMEVFGGNGYL-EE 385
|
250 260 270
....*....|....*....|....*....|
gi 2020605850 362 FAhglFAKLERDHRIVGIFDGNTlvNLNAL 391
Cdd:cd01154 386 WP---VARLHREAQVTPIWEGTG--NIQAL 410
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
47-288 |
9.90e-17 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 82.41 E-value: 9.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 47 EAFPTEAVARLDALGLpAQYVPARHGGTLDSYEDLLQLVRVVARRDLTVAIAHT-KTYLGAVSTWVGGTAEQAQELGARI 125
Cdd:cd01151 43 EKFDRKIIEEMGELGL-LGATIKGYGCAGLSSVAYGLIAREVERVDSGYRSFMSvQSSLVMLPIYDFGSEEQKQKYLPKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 126 ASGAVV-SWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTRGYsllLVDKAllADG 204
Cdd:cd01151 122 ASGELIgCFGLTEPNHGSDPGGMETRARKDGGGYKLNGSKTWITNSPIADVFVVWARNDETGKIRGF---ILERG--MKG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 205 shtcLPAAKTHGIRG--ADISG-IAFDGAVVPASALIgEEGEGIETVLRSLQITRTICASLSLGAGDHALRIATRFGLEH 281
Cdd:cd01151 197 ----LSAPKIQGKFSlrASITGeIVMDNVFVPEENLL-PGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDR 271
|
....*..
gi 2020605850 282 RLYGKRL 288
Cdd:cd01151 272 KQFGRPL 278
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
113-392 |
3.10e-16 |
|
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: 80.90 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 113 GTAEQAQELGARIASGAVVS-WGLTERAHGSDLLSGELTATPVAGG-YRLDGEKWLINNATR----SDLVCVLARTSLAG 186
Cdd:cd01153 100 GTEAQREKWIPRLAEGEWTGtMCLTEPDAGSDLGALRTKAVYQADGsWRINGVKRFISAGEHdmseNIVHLVLARSEGAP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 187 -GTRGYSLLLVDKALLaDGSHTCLPAAKTH---GIRGADISGIAFDGAVVPasaLIGEEGEGIETVLRSLQITRTICASL 262
Cdd:cd01153 180 pGVKGLSLFLVPKFLD-DGERNGVTVARIEekmGLHGSPTCELVFDNAKGE---LIGEEGMGLAQMFAMMNGARLGVGTQ 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 263 SLGAGDHALRIATRFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVTLLASRGVHTLT------EEMSVSSA-AVKY 335
Cdd:cd01153 256 GTGLAEAAYLNALAYAKERKQGGDLIKAAPAVTIIHHPDVRRSLMTQKAYAEGSRALDLYTatvqdlAERKATEGeDRKA 335
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020605850 336 LVPTTadELITGMGQFLGARSFLSEEF----AHGLFAKLE--------RDHRIVGIFDGNTLVNLNALI 392
Cdd:cd01153 336 LSALA--DLLTPVVKGFGSEAALEAVSdaiqVHGGSGYTReypieqyyRDARITTIYEGTTGIQALDLI 402
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
134-228 |
5.55e-15 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 70.77 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 134 GLTERAHGSDLLSGE-LTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTRGYSLLLVDKAllADGSHTcLPAA 212
Cdd:pfam02770 3 ALTEPGAGSDVASLKtTAADGDGGGWVLNGTKWWITNAGIADLFLVLARTGGDDRHGGISLFLVPKD--APGVSV-RRIE 79
|
90
....*....|....*.
gi 2020605850 213 KTHGIRGADISGIAFD 228
Cdd:pfam02770 80 TKLGVRGLPTGELVFD 95
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
16-286 |
7.12e-13 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 70.68 E-value: 7.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 16 DRAGGFDRSLGHPARRDLPFFAARmreLDAAEAFPTEA-----VARLDALGLPAqyvPARHGGTLDSYedllqLVRVVAR 90
Cdd:PLN02519 28 DTQLQFKESVQQFAQENIAPHAAA---IDATNSFPKDVnlwklMGDFNLHGITA---PEEYGGLGLGY-----LYHCIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 91 RDLTVAIAHTKTYLGAVSTWV------GGTAEQAQELGARIASGAVV-SWGLTERAHGSDLLSGELTATPVAGGYRLDGE 163
Cdd:PLN02519 97 EEISRASGSVGLSYGAHSNLCinqlvrNGTPAQKEKYLPKLISGEHVgALAMSEPNSGSDVVSMKCKAERVDGGYVLNGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 164 KWLINNATRSDLVCVLARTSLAGGTRGYSLLLVDKALlaDGSHTCLPAAKThGIRGADISGIAFDGAVVPASALIGEEGE 243
Cdd:PLN02519 177 KMWCTNGPVAQTLVVYAKTDVAAGSKGITAFIIEKGM--PGFSTAQKLDKL-GMRGSDTCELVFENCFVPEENVLGQEGK 253
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2020605850 244 GIETVLRSLQITRTICASLSLGAGDHALRIATRFGLEHRLYGK 286
Cdd:PLN02519 254 GVYVMMSGLDLERLVLAAGPLGLMQACLDVVLPYVRQREQFGR 296
|
|
| PRK11561 |
PRK11561 |
isovaleryl CoA dehydrogenase; Provisional |
128-292 |
5.10e-12 |
|
isovaleryl CoA dehydrogenase; Provisional
Pssm-ID: 183199 [Multi-domain] Cd Length: 538 Bit Score: 68.62 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 128 GAVVSWGLTERAHGSDLLSGELTATPVAGG-YRLDGEKWLINnATRSDLVCVLARTslaggTRGYSLLLVDKaLLADGSH 206
Cdd:PRK11561 177 GLLIGMGMTEKQGGSDVLSNTTRAERLADGsYRLVGHKWFFS-VPQSDAHLVLAQA-----KGGLSCFFVPR-FLPDGQR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 207 TCLPAAKTH---GIRGADISGIAFDGAVvpaSALIGEEGEGIETVLRSLQITRTICASLSLGAGDHALRIATRFGLEHRL 283
Cdd:PRK11561 250 NAIRLERLKdklGNRSNASSEVEFQDAI---GWLLGEEGEGIRLILKMGGMTRFDCALGSHGLMRRAFSVAIYHAHQRQV 326
|
....*....
gi 2020605850 284 YGKRLIDLP 292
Cdd:PRK11561 327 FGKPLIEQP 335
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
44-313 |
3.03e-11 |
|
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: 65.45 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 44 DAAEAFPTEAVARLDALgLPAQYVPARHGGTLDSYEDLLQLVRVVARRDLT------------------VAIAHTKTYLG 105
Cdd:cd01152 1 PSEEAFRAEVRAWLAAH-LPPELREESALGYREGREDRRRWQRALAAAGWAapgwpkeyggrgaslmeqLIFREEMAAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 106 A-------VSTWVG------GTAEQAQELGARIASGAVVsW--GLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNA 170
Cdd:cd01152 80 ApvpfnqiGIDLAGptilayGTDEQKRRFLPPILSGEEI-WcqGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 171 TRSDLVCVLARTSLAGGT-RGYSLLLVDkaLLADGShTCLPAAKTHGirGADISGIAFDGAVVPASALIGEEGEGIETVL 249
Cdd:cd01152 159 HYADWAWLLVRTDPEAPKhRGISILLVD--MDSPGV-TVRPIRSING--GEFFNEVFLDDVRVPDANRVGEVNDGWKVAM 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2020605850 250 RSLQITR-TICASLSLGAGDHALRIAtrfglEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVTL 313
Cdd:cd01152 234 TTLNFERvSIGGSAATFFELLLARLL-----LLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVF 293
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
40-353 |
1.96e-10 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 62.82 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 40 MRELDAAEAFPTEAVARLDALGLPAQYVPARHGGTLDSYEDLLQLVRVVARRDLTVAIAHTKTYLGAVSTWvgGTAEQ-A 118
Cdd:PRK12341 29 FRTCDENGTYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCGAPAFLITNGQCIHSMRRF--GSAEQlR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 119 QELGARIASGAVV-SWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTR-GYSLLLV 196
Cdd:PRK12341 107 KTAESTLETGDPAyALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGAKEYPYMLVLARDPQPKDPKkAFTLWWV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 197 DKalladgSHTCLPAAKTHGIRG--ADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHALRIA 274
Cdd:PRK12341 187 DS------SKPGIKINPLHKIGWhmLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDA 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2020605850 275 TRFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVTLLASRGVHTlTEEMSVSSAAVKYLVPTTADELITGMGQFLG 353
Cdd:PRK12341 261 ARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADN-GQSLRTSAALAKLYCARTAMEVIDDAIQIMG 338
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
49-386 |
2.52e-10 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 62.56 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 49 FPTEAVARLDALGLPaqyvparhGGTLDSY--EDLLQLVRVVARRDLTVAIAHTKTY------LGAVSTWVGGTAEQAQE 120
Cdd:PLN02526 61 FPFHIIPKLGSLGIA--------GGTIKGYgcPGLSITASAIATAEVARVDASCSTFilvhssLAMLTIALCGSEAQKQK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 121 LGARIAS-GAVVSWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTRGYsllLVDKA 199
Cdd:PLN02526 133 YLPSLAQlDTVACWALTEPDYGSDASSLNTTATKVEGGWILNGQKRWIGNSTFADVLVIFARNTTTNQINGF---IVKKG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 200 llADGshtcLPAAKTH---GIRGADISGIAFDGAVVP-ASALIGEegEGIETVLRSLQITRTICASLSLGAGDHALRIAT 275
Cdd:PLN02526 210 --APG----LKATKIEnkiGLRMVQNGDIVLKDVFVPdEDRLPGV--NSFQDTNKVLAVSRVMVAWQPIGISMGVYDMCH 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 276 RFGLEHRLYGKRLIDLPQAHRALTEAYADLFAMeavTLLASRGVHTL-TEEMSVSSAAV-KYLVPTTADELITGMGQFLG 353
Cdd:PLN02526 282 RYLKERKQFGAPLAAFQINQEKLVRMLGNIQAM---FLVGWRLCKLYeSGKMTPGHASLgKAWITKKARETVALGRELLG 358
|
330 340 350
....*....|....*....|....*....|...
gi 2020605850 354 ARSFLSEEFAHGLFAKLERDHRIVGIFDGNTLV 386
Cdd:PLN02526 359 GNGILADFLVAKAFCDLEPIYTYEGTYDINALV 391
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
104-282 |
2.72e-09 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 59.88 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 104 LGAVSTWVG-GTAEQAQELGARIASGavvSWG----LTERAHGSDLLSGELTATPVA-GGYRLDGEKWLI----NNATRS 173
Cdd:PTZ00456 154 IGAANTLMAwGSEEQKEQYLTKLVSG---EWSgtmcLTEPQCGTDLGQVKTKAEPSAdGSYKITGTKIFIsagdHDLTEN 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 174 DLVCVLART-SLAGGTRGYSLLLVDKALL-ADGSH------TCLPAAKTHGIRGADISGIAFDGAVvpaSALIGEEGEGI 245
Cdd:PTZ00456 231 IVHIVLARLpNSLPTTKGLSLFLVPRHVVkPDGSLetaknvKCIGLEKKMGIKGSSTCQLSFENSV---GYLIGEPNAGM 307
|
170 180 190
....*....|....*....|....*....|....*..
gi 2020605850 246 ETVLRSLQITRTICASLSLGAGDHALRIATRFGLEHR 282
Cdd:PTZ00456 308 KQMFTFMNTARVGTALEGVCHAELAFQNALRYARERR 344
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
36-180 |
7.31e-09 |
|
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: 58.10 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 36 FAARMRELDAAEAFPTEAVARLDALGLPAQYVPARHGGTLDSYEDLLQLVRVVARRDLTVAIAHTKTYLGAVSTWVGGTA 115
Cdd:cd01163 10 IAEGAAERDRQRGLPYEEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAQALRAHFGFVEALLLAGPE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2020605850 116 EQAQELGARIASGAVVSWGLTERahGSDLLSGELTATPV-AGGYRLDGEKWLINNATRSDLVCVLA 180
Cdd:cd01163 90 QFRKRWFGRVLNGWIFGNAVSER--GSVRPGTFLTATVRdGGGYVLNGKKFYSTGALFSDWVTVSA 153
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
37-128 |
8.92e-07 |
|
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: 47.84 E-value: 8.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 37 AARMRELDAAEAFPTEAVARLDALGLPAQYVPARHGGTLDSYEDLLQLVRVVARRDLTVAIAH-TKTYLGAVSTWVGGTA 115
Cdd:pfam02771 20 APHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASVALALsVHSSLGAPPILRFGTE 99
|
90
....*....|...
gi 2020605850 116 EQAQELGARIASG 128
Cdd:pfam02771 100 EQKERYLPKLASG 112
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
242-389 |
1.44e-06 |
|
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: 48.02 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 242 GEGIETVLRSLQITRTICASLSLGAGDHALRIATRFGLEHRLYGKRLIDLPQAHRALTEAYADLfamEAVTLLASRGVHT 321
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEI---EAARLLVYRAAEA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 322 LTEE--MSVSSAAVKYLVPTTADELITGMGQFLGARSFLseefAHGLFAKLERDHRIVGIFDGNTLVNLN 389
Cdd:pfam00441 78 LDAGgpDGAEASMAKLYASEAAVEVADLAMQLHGGYGYL----REYPVERLYRDARVLRIGEGTSEIQRN 143
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
113-391 |
7.56e-05 |
|
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: 45.46 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 113 GTAEQAQE-----LGARIASGavvsWGLTERA-HGSDLLSGELTATPVAGGYRLDGEKWLINNAT--RSDLVCVLARTSL 184
Cdd:cd01155 108 GSEEQKKQwleplLDGKIRSA----FAMTEPDvASSDATNIECSIERDGDDYVINGRKWWSSGAGdpRCKIAIVMGRTDP 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 185 AGGTRG--YSLLLVDkalladgSHTclPAAKThgIRGADISG----------IAFDGAVVPASALIGEEGEGIETVLRSL 252
Cdd:cd01155 184 DGAPRHrqQSMILVP-------MDT--PGVTI--IRPLSVFGyddaphghaeITFDNVRVPASNLILGEGRGFEIAQGRL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 253 QITRTICASLSLGAGDHALRIATRFGLEHRLYGKRLIdlpqAHRALTEAYADL-FAMEAVTLLASRGVHTLTEEMSVSS- 330
Cdd:cd01155 253 GPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLA----QHGVVAHWIAKSrIEIEQARLLVLKAAHMIDTVGNKAAr 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2020605850 331 ---AAVKYLVPTTADELITGMGQFLGARSfLSEEFAhglFAKLERDHRIVGIFDGNTLVNLNAL 391
Cdd:cd01155 329 keiAMIKVAAPRMALKIIDRAIQVHGAAG-VSQDTP---LANMYAWARTLRIADGPDEVHLRSI 388
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
38-376 |
5.12e-04 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 42.51 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 38 ARMRELDAAEAFPTEAVARLDALGLPAQYVPARHGGTLDSYEDLLQLVRVVARrdltvaiAHTKTYL-----GAVSTWV- 111
Cdd:PRK03354 27 AYFAECDRDSVYPERFVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGR-------LGAPTYVlyqlpGGFNTFLr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 112 GGTAEQAQELGARIASGA-VVSWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTRG 190
Cdd:PRK03354 100 EGTQEQIDKIMAFRGTGKqMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASPDKPV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 191 YSLLLVDkalLADGSHTCLPAAKThGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHA 270
Cdd:PRK03354 180 YTEWFVD---MSKPGIKVTKLEKL-GLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 271 LRIATRFGLEHRLYGK-----RLIDLPQAHRALteayaDLFAMEAVTLLAS----RGVHTlteemSVSSAAVKYLVPTTA 341
Cdd:PRK03354 256 FEDAARYANQRVQFGEaigrfQLIQEKFAHMAI-----KLNSMKNMLYEAAwkadNGTIT-----SGDAAMCKYFCANAA 325
|
330 340 350
....*....|....*....|....*....|....*
gi 2020605850 342 DELITGMGQFLGARSFLSEefaHGLfAKLERDHRI 376
Cdd:PRK03354 326 FEVVDSAMQVLGGVGIAGN---HRI-SRFWRDLRV 356
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
42-570 |
8.39e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.55 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 42 ELDAAEAFPTEAVARLDALGLPAQ---YVPARHGGTLDSYEDLLQLVRVVARRDLTVAIAHTKTYLGAVSTWVGGTAEQA 118
Cdd:COG3321 846 PVDWSALYPGRGRRRVPLPTYPFQredAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAA 925
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 119 QELGARIASGAVVSWGLTERAHGSDLLSGELTATPVAGGYRLDGEKWLINNATRSDLVCVLARTSLAGGTRGYSLLLVDK 198
Cdd:COG3321 926 LAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALL 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 199 ALLADGSHTCLPAAKTHGIRGADISGIAFDGAVVPASALIGEEGEGIETVLRSLQITRTICASLSLGAGDHALRIATRFG 278
Cdd:COG3321 1006 AAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALA 1085
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 279 LEHRLYGKRLIDLPQAHRALTEAYADLFAMEAVTLLASRGVHTLTEEMSVSSAAVKYLVPTTADELITGMGQFLGARSFL 358
Cdd:COG3321 1086 LAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAA 1165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 359 --SEEFAHGLFAKLERDHRIVGIFDGNTLVNLNALINQFAALARGYRAGRTDAEGLAAAAMLDAQIPVFDPARLQLTSRT 436
Cdd:COG3321 1166 alLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAV 1245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2020605850 437 GNSVAASLPRAVAELRELVTSGEAPESLLTVAEKLLRISDTTHEQMAAHRPSPRDVPAAAFDLAHRYTLCSAAAACLQVW 516
Cdd:COG3321 1246 AALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAAL 1325
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2020605850 517 LRNRTTVAADTTATAGLWQDGLWAEAALCRLAERLTPGTLPEEGADGSAVLDRL 570
Cdd:COG3321 1326 LAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
|
|
| |
