NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|500246517|ref|WP_011906870|]
View 

acyl-CoA dehydrogenase family protein [Novosphingobium aromaticivorans]

Protein Classification

acyl-CoA dehydrogenase family protein( domain architecture ID 550)

acyl-CoA dehydrogenase (ACAD) family protein similar to acyl-CoA dehydrogenase that catalyzes the alpha,beta dehydrogenation of an acyl-CoA to form 2,3-dehydroacyl-CoA; requires an acceptor such as FAD, which becomes reduced

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ACAD super family cl09933
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 12-378 2.08e-93

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)


The actual alignment was detected with superfamily member cd01152:

Pssm-ID: 447864 [Multi-domain]  Cd Length: 380  Bit Score: 284.63  E-value: 2.08e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  12 DEDEALRPAIRAFIAKHVdglPADRRARSWQGF------DAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLS 85
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHL---PPELREESALGYregredRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  86 AGAPVAAHWIADRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTG 165
Cdd:cd01152   78 AGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 166 GMHCDYMIALVRTSGTpADRHAGLSQLIIDLKAPGVTVRPIVDLTGDAHFSEVFFDNVQLGEDALIGNEGDGWKQCTAEL 245
Cdd:cd01152  158 AHYADWAWLLVRTDPE-APKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 246 AFERSGPERIYSSVV--LLDAWVRHLRTAGRGDAAPLV----GRLTAELATLRAMSIACTARLAAGESPVVEASIVKDRG 319
Cdd:cd01152  237 NFERVSIGGSAATFFelLLARLLLLTRDGRPLIDDPLVrqrlARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500246517 320 TGLEQELPV----VIGDDlAAHPDEPVSEELYRTLVYVTHVAPSFSLRGGTREILRGIIARGM 378
Cdd:cd01152  317 SELAQELAElaleLLGTA-ALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERL 378
 
Name Accession Description Interval E-value
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 12-378 2.08e-93

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: 284.63  E-value: 2.08e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  12 DEDEALRPAIRAFIAKHVdglPADRRARSWQGF------DAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLS 85
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHL---PPELREESALGYregredRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  86 AGAPVAAHWIADRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTG 165
Cdd:cd01152   78 AGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 166 GMHCDYMIALVRTSGTpADRHAGLSQLIIDLKAPGVTVRPIVDLTGDAHFSEVFFDNVQLGEDALIGNEGDGWKQCTAEL 245
Cdd:cd01152  158 AHYADWAWLLVRTDPE-APKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 246 AFERSGPERIYSSVV--LLDAWVRHLRTAGRGDAAPLV----GRLTAELATLRAMSIACTARLAAGESPVVEASIVKDRG 319
Cdd:cd01152  237 NFERVSIGGSAATFFelLLARLLLLTRDGRPLIDDPLVrqrlARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500246517 320 TGLEQELPV----VIGDDlAAHPDEPVSEELYRTLVYVTHVAPSFSLRGGTREILRGIIARGM 378
Cdd:cd01152  317 SELAQELAElaleLLGTA-ALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERL 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 9-381 1.40e-77

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: 243.98  E-value: 1.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517   9 TLPDEDEALRPAIRAFIAKHVDglPADRRARSWQGFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGA 88
Cdd:COG1960    4 ELTEEQRALRDEVREFAEEEIA--PEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  89 PVA----AHWIAdrqsAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTT 164
Cdd:COG1960   82 SLAlpvgVHNGA----AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 165 GGMHCDYMIALVRTSgtPADRHAGLSQLIIDLKAPGVTVRPIVDLTG--DAHFSEVFFDNVQLGEDALIGNEGDGWKQCT 242
Cdd:COG1960  158 NAPVADVILVLARTD--PAAGHRGISLFLVPKDTPGVTVGRIEDKMGlrGSDTGELFFDDVRVPAENLLGEEGKGFKIAM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 243 AELAFERSG--------PERIYSSVVlldAWVRHLRTAGRGDAA-PLV----GRLTAELATLRAMSIACTARLAAGESPV 309
Cdd:COG1960  236 STLNAGRLGlaaqalgiAEAALELAV---AYAREREQFGRPIADfQAVqhrlADMAAELEAARALVYRAAWLLDAGEDAA 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 310 VEASIVK-----------DR------GTGLEQELPVvigddlaahpdepvsEELYRTlvyvthvAPSFSLRGGTREILRG 372
Cdd:COG1960  313 LEAAMAKlfateaalevaDEalqihgGYGYTREYPL---------------ERLYRD-------ARILTIYEGTNEIQRL 370


                 ....*....
gi 500246517 373 IIARGMGLR 381
Cdd:COG1960  371 IIARRLLGR 379
PRK12341 PRK12341
acyl-CoA dehydrogenase;
10-249 4.48e-30

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 118.68  E-value: 4.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  10 LPDEDEALRPAIRAFIAKHVdglPADRRARSWQG--FDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAG 87
Cdd:PRK12341   5 LTEEQELLLASIRELITRNF---PEEYFRTCDENgtYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  88 APvaAHWIADRQSAPLILNFGNEAQRRRHIP-AICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTGG 166
Cdd:PRK12341  82 AP--AFLITNGQCIHSMRRFGSAEQLRKTAEsTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 167 MHCDYMIALVRTSgTPADRHAGLSQLIIDLKAPGVTVRPIVDLTGD-AHFSEVFFDNVQLGEDALIGNEGDGWKQCTAEL 245
Cdd:PRK12341 160 KEYPYMLVLARDP-QPKDPKKAFTLWWVDSSKPGIKINPLHKIGWHmLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNF 238


                 ....
gi 500246517 246 AFER 249
Cdd:PRK12341 239 EMER 242
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 11-124 2.34e-28

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: 106.78  E-value: 2.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517   11 PDEDEALRPAIRAFIAKHVdgLPADRRARSWQGFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPV 90
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEI--APHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 500246517   91 A-AHWIADRQSAPLILNFGNEAQRRRHIPAICRGE 124
Cdd:pfam02771  79 AlALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
 
Name Accession Description Interval E-value
ACAD_fadE6_17_26 cd01152
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ...
 12-378 2.08e-93

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: 284.63  E-value: 2.08e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  12 DEDEALRPAIRAFIAKHVdglPADRRARSWQGF------DAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLS 85
Cdd:cd01152    1 PSEEAFRAEVRAWLAAHL---PPELREESALGYregredRRRWQRALAAAGWAAPGWPKEYGGRGASLMEQLIFREEMAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  86 AGAPVAAHWIADRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTG 165
Cdd:cd01152   78 AGAPVPFNQIGIDLAGPTILAYGTDEQKRRFLPPILSGEEIWCQGFSEPGAGSDLAGLRTRAVRDGDDWVVNGQKIWTSG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 166 GMHCDYMIALVRTSGTpADRHAGLSQLIIDLKAPGVTVRPIVDLTGDAHFSEVFFDNVQLGEDALIGNEGDGWKQCTAEL 245
Cdd:cd01152  158 AHYADWAWLLVRTDPE-APKHRGISILLVDMDSPGVTVRPIRSINGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMTTL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 246 AFERSGPERIYSSVV--LLDAWVRHLRTAGRGDAAPLV----GRLTAELATLRAMSIACTARLAAGESPVVEASIVKDRG 319
Cdd:cd01152  237 NFERVSIGGSAATFFelLLARLLLLTRDGRPLIDDPLVrqrlARLEAEAEALRLLVFRLASALAAGKPPGAEASIAKLFG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500246517 320 TGLEQELPV----VIGDDlAAHPDEPVSEELYRTLVYVTHVAPSFSLRGGTREILRGIIARGM 378
Cdd:cd01152  317 SELAQELAElaleLLGTA-ALLRDPAPGAELAGRWEADYLRSRATTIYGGTSEIQRNIIAERL 378
CaiA COG1960
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ...
 9-381 1.40e-77

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: 243.98  E-value: 1.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517   9 TLPDEDEALRPAIRAFIAKHVDglPADRRARSWQGFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGA 88
Cdd:COG1960    4 ELTEEQRALRDEVREFAEEEIA--PEAREWDREGEFPRELWRKLAELGLLGLTIPEEYGGLGLSLVELALVLEELARADA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  89 PVA----AHWIAdrqsAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTT 164
Cdd:COG1960   82 SLAlpvgVHNGA----AEALLRFGTEEQKERYLPRLASGEWIGAFALTEPGAGSDAAALRTTAVRDGDGYVLNGQKTFIT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 165 GGMHCDYMIALVRTSgtPADRHAGLSQLIIDLKAPGVTVRPIVDLTG--DAHFSEVFFDNVQLGEDALIGNEGDGWKQCT 242
Cdd:COG1960  158 NAPVADVILVLARTD--PAAGHRGISLFLVPKDTPGVTVGRIEDKMGlrGSDTGELFFDDVRVPAENLLGEEGKGFKIAM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 243 AELAFERSG--------PERIYSSVVlldAWVRHLRTAGRGDAA-PLV----GRLTAELATLRAMSIACTARLAAGESPV 309
Cdd:COG1960  236 STLNAGRLGlaaqalgiAEAALELAV---AYAREREQFGRPIADfQAVqhrlADMAAELEAARALVYRAAWLLDAGEDAA 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 310 VEASIVK-----------DR------GTGLEQELPVvigddlaahpdepvsEELYRTlvyvthvAPSFSLRGGTREILRG 372
Cdd:COG1960  313 LEAAMAKlfateaalevaDEalqihgGYGYTREYPL---------------ERLYRD-------ARILTIYEGTNEIQRL 370


                 ....*....
gi 500246517 373 IIARGMGLR 381
Cdd:COG1960  371 IIARRLLGR 379
LCAD cd01160
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ...
 13-379 1.17e-50

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: 173.84  E-value: 1.17e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  13 EDEALRPAIRAFIAKHVdgLPADRRARSWQGFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVAA 92
Cdd:cd01160    2 EHDAFRDVVRRFFAKEV--APFHHEWEKAGEVPREVWRKAGEQGLLGVGFPEEYGGIGGDLLSAAVLWEELARAGGSGPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  93 HWIADRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTGGMHCDYM 172
Cdd:cd01160   80 LSLHTDIVSPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPGAGSDLQGIRTTARKDGDHYVLNGSKTFITNGMLADVV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 173 IALVRTSGtPADRHAGLSQLIIDLKAPGVTV-RPIVDLTGDAH-FSEVFFDNVQLGEDALIGNEGDGWKQCTAELAFER- 249
Cdd:cd01160  160 IVVARTGG-EARGAGGISLFLVERGTPGFSRgRKLKKMGWKAQdTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERl 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 250 -SGPERIYSSVVLLD---AWVRHLRTAGRGDAAPLVGR-----LTAELATLRAMSIACTARLAAGESPVVEASIVKDRGT 320
Cdd:cd01160  239 lIAAGALAAAEFMLEetrNYVKQRKAFGKTLAQLQVVRhkiaeLATKVAVTRAFLDNCAWRHEQGRLDVAEASMAKYWAT 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500246517 321 GLEQElpvVIGDDLAAHPD-----EPVSEELYRTlvyvthvAPSFSLRGGTREILRGIIARGMG 379
Cdd:cd01160  319 ELQNR---VAYECVQLHGGwgymrEYPIARAYRD-------ARVQPIYGGTTEIMKELISRQMV 372
ACAD cd00567
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ...
 73-376 1.10e-44

Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)


Pssm-ID: 173838 [Multi-domain]  Cd Length: 327  Bit Score: 156.68  E-value: 1.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  73 AFARFVVVEELLSAGAPVAAHW-----IADRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRA 147
Cdd:cd00567   12 EFAAEELEPYARERRETPEEPWellaeLGLLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPGAGSDLAGIRTTA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 148 ERNDKGWVVNGQKIWTTGGMHCDYMIALVRTSGTPADRHaGLSQLIIDLKAPGVTVRPIVDLTGDAH--FSEVFFDNVQL 225
Cdd:cd00567   92 RKDGDGYVLNGRKIFISNGGDADLFIVLARTDEEGPGHR-GISAFLVPADTPGVTVGRIWDKMGMRGsgTGELVFDDVRV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 226 GEDALIGNEGDGWKQCTAELAFERSGperiYSSVVL------LDAWVRHLRTAGRGDAA----PLV----GRLTAELATL 291
Cdd:cd00567  171 PEDNLLGEEGGGFELAMKGLNVGRLL----LAAVALgaaraaLDEAVEYAKQRKQFGKPlaefQAVqfklADMAAELEAA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 292 RAMSIACTARLAAGESPV-VEASIVKDRGTGLEQElpVVigdDLAA--------HPDEPVsEELYRTLvyvtHVAPSFsl 362
Cdd:cd00567  247 RLLLYRAAWLLDQGPDEArLEAAMAKLFATEAARE--VA---DLAMqihggrgySREYPV-ERYLRDA----RAARIA-- 314

                        330
                 ....*....|....
gi 500246517 363 rGGTREILRGIIAR 376
Cdd:cd00567  315 -EGTAEIQRLIIAR 327
SCAD_SBCAD cd01158
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ...
 12-240 2.54e-42

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: 151.65  E-value: 2.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  12 DEDEALRPAIRAFIAKHVDGLPA--DRRARswqgFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEEL----LS 85
Cdd:cd01158    1 EEHQMIRKTVRDFAEKEIAPLAAemDEKGE----FPREVIKEMAELGLMGIPIPEEYGGAGLDFLAYAIAIEELakvdAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  86 AGAPVAAHwiaDRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTG 165
Cdd:cd01158   77 VAVIVSVH---NSLGANPIIKFGTEEQKKKYLPPLATGEKIGAFALSEPGAGSDAAALKTTAKKDGDDYVLNGSKMWITN 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500246517 166 GMHCDYMIALVRTSgtPADRHAGLSQLIIDLKAPGVTVRPIVDLTGD--AHFSEVFFDNVQLGEDALIGNEGDGWKQ 240
Cdd:cd01158  154 GGEADFYIVFAVTD--PSKGYRGITAFIVERDTPGLSVGKKEDKLGIrgSSTTELIFEDVRVPKENILGEEGEGFKI 228
IVD cd01156
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ...
 10-249 5.13e-42

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: 151.02  E-value: 5.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  10 LPDEDEALRPAIRAFIAKHVDGLpADRRARSwQGFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAP 89
Cdd:cd01156    2 LDDEIEMLRQSVREFAQKEIAPL-AAKIDRD-NEFPRDLWRKMGKLGLLGITAPEEYGGSGMGYLAHVIIMEEISRASGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  90 VA----AHwiadrqsAPLILN----FGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKI 161
Cdd:cd01156   80 VAlsygAH-------SNLCINqiyrNGSAAQKEKYLPKLISGEHIGALAMSEPNAGSDVVSMKLRAEKKGDRYVLNGSKM 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 162 WTTGGMHCDYMIALVRTSGTPADRhaGLSQLIIDLKAPGVTVRPIVDLTG--DAHFSEVFFDNVQLGEDALIGNEGDGWK 239
Cdd:cd01156  153 WITNGPDADTLVVYAKTDPSAGAH--GITAFIVEKGMPGFSRAQKLDKLGmrGSNTCELVFEDCEVPEENILGGENKGVY 230

                        250
                 ....*....|
gi 500246517 240 QCTAELAFER 249
Cdd:cd01156  231 VLMSGLDYER 240
PRK12341 PRK12341
acyl-CoA dehydrogenase;
10-249 4.48e-30

acyl-CoA dehydrogenase;


Pssm-ID: 183454 [Multi-domain]  Cd Length: 381  Bit Score: 118.68  E-value: 4.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  10 LPDEDEALRPAIRAFIAKHVdglPADRRARSWQG--FDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAG 87
Cdd:PRK12341   5 LTEEQELLLASIRELITRNF---PEEYFRTCDENgtYPREFMRALADNGISMLGVPEEFGGTPADYVTQMLVLEEVSKCG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  88 APvaAHWIADRQSAPLILNFGNEAQRRRHIP-AICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTGG 166
Cdd:PRK12341  82 AP--AFLITNGQCIHSMRRFGSAEQLRKTAEsTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYLNGQKTFITGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 167 MHCDYMIALVRTSgTPADRHAGLSQLIIDLKAPGVTVRPIVDLTGD-AHFSEVFFDNVQLGEDALIGNEGDGWKQCTAEL 245
Cdd:PRK12341 160 KEYPYMLVLARDP-QPKDPKKAFTLWWVDSSKPGIKINPLHKIGWHmLSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNF 238


                 ....
gi 500246517 246 AFER 249
Cdd:PRK12341 239 EMER 242
Acyl-CoA_dh_N pfam02771
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ...
 11-124 2.34e-28

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: 106.78  E-value: 2.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517   11 PDEDEALRPAIRAFIAKHVdgLPADRRARSWQGFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPV 90
Cdd:pfam02771   1 TEEQEALRDTVREFAEEEI--APHAAEWDEEGEFPRELWKKLGELGLLGITIPEEYGGAGLDYLAYALVAEELARADASV 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 500246517   91 A-AHWIADRQSAPLILNFGNEAQRRRHIPAICRGE 124
Cdd:pfam02771  79 AlALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
PTZ00461 PTZ00461
isovaleryl-CoA dehydrogenase; Provisional
 13-249 4.30e-28

isovaleryl-CoA dehydrogenase; Provisional


Pssm-ID: 185640 [Multi-domain]  Cd Length: 410  Bit Score: 113.88  E-value: 4.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  13 EDEALRPAIRAFIAKHVDglPADRRARSWQGFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVAA 92
Cdd:PTZ00461  40 EHAALRETVAKFSREVVD--KHAREDDINMHFNRDLFKQLGDLGVMGVTVPEADGGAGMDAVAAVIIHHELSKYDPGFCL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  93 HWIAdrQSAPLILNFGNEA---QRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKG-WVVNGQKIWTTGGMH 168
Cdd:PTZ00461 118 AYLA--HSMLFVNNFYYSAspaQRARWLPKVLTGEHVGAMGMSEPGAGTDVLGMRTTAKKDSNGnYVLNGSKIWITNGTV 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 169 CDYMIALVRTSGTpadrhagLSQLIIDLKAPGVTVRPIVDLTG--DAHFSEVFFDNVQLGEDALIGNEGDGWKQCTAELA 246
Cdd:PTZ00461 196 ADVFLIYAKVDGK-------ITAFVVERGTKGFTQGPKIDKCGmrASHMCQLFFEDVVVPAENLLGEEGKGMVGMMRNLE 268


                 ...
gi 500246517 247 FER 249
Cdd:PTZ00461 269 LER 271
VLCAD cd01161
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ...
 51-239 4.52e-27

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: 111.02  E-value: 4.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  51 ALGEAGFLGLTLPAEYGGQGRGAFARFVVVEEL---LSAGAPVAAHwiadrQSAPL--ILNFGNEAQRRRHIPAICRGEQ 125
Cdd:cd01161   64 QLKELGLFGLQVPEEYGGLGLNNTQYARLAEIVgmdLGFSVTLGAH-----QSIGFkgILLFGTEAQKEKYLPKLASGEW 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 126 LFCIGMSEPGSGSDLASVRTRAERNDKG--WVVNGQKIWTTGGMHCDYMIALVRTSGTPADRHA--GLSQLIIDLKAPGV 201
Cdd:cd01161  139 IAAFALTEPSSGSDAASIRTTAVLSEDGkhYVLNGSKIWITNGGIADIFTVFAKTEVKDATGSVkdKITAFIVERSFGGV 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 500246517 202 TVRPIVDLTG--DAHFSEVFFDNVQLGEDALIGNEGDGWK 239
Cdd:cd01161  219 TNGPPEKKMGikGSNTAEVYFEDVKIPVENVLGEVGDGFK 258
PLN02519 PLN02519
isovaleryl-CoA dehydrogenase
 50-252 8.37e-26

isovaleryl-CoA dehydrogenase


Pssm-ID: 215284 [Multi-domain]  Cd Length: 404  Bit Score: 107.27  E-value: 8.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  50 RALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVAAHWIADRQSA--PLILNfGNEAQRRRHIPAICRGEQLF 127
Cdd:PLN02519  66 KLMGDFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVGLSYGAHSNLCinQLVRN-GTPAQKEKYLPKLISGEHVG 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 128 CIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTGGMHCDYMIALVRTSGTPADRhaGLSQLIIDLKAPGVTVRPIV 207
Cdd:PLN02519 145 ALAMSEPNSGSDVVSMKCKAERVDGGYVLNGNKMWCTNGPVAQTLVVYAKTDVAAGSK--GITAFIIEKGMPGFSTAQKL 222

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 500246517 208 DLTG--DAHFSEVFFDNVQLGEDALIGNEGDGWKQCTAELAFER----SGP 252
Cdd:PLN02519 223 DKLGmrGSDTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERlvlaAGP 273
Acyl-CoA_dh_M pfam02770
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ...
 128-221 7.54e-25

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: 96.97  E-value: 7.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  128 CIGMSEPGSGSDLASVRTRA-ERNDKGWVVNGQKIWTTGGMHCDYMIALVRTSGTpaDRHAGLSQLIIDLKAPGVTVRPI 206
Cdd:pfam02770   1 AFALTEPGAGSDVASLKTTAaDGDGGGWVLNGTKWWITNAGIADLFLVLARTGGD--DRHGGISLFLVPKDAPGVSVRRI 78

                          90
                  ....*....|....*..
gi 500246517  207 VDLTG--DAHFSEVFFD 221
Cdd:pfam02770  79 ETKLGvrGLPTGELVFD 95
PRK03354 PRK03354
crotonobetainyl-CoA dehydrogenase; Validated
 48-249 1.94e-23

crotonobetainyl-CoA dehydrogenase; Validated


Pssm-ID: 179566 [Multi-domain]  Cd Length: 380  Bit Score: 100.29  E-value: 1.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  48 FSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVAAHWiadrqSAPL----ILNFGNEAQRRRHIPAICRG 123
Cdd:PRK03354  42 FVKALADMGIDSLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLY-----QLPGgfntFLREGTQEQIDKIMAFRGTG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 124 EQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTGGMHCDYMIALVRTSGTPadRHAGLSQLIIDLKAPGVTV 203
Cdd:PRK03354 117 KQMWNSAITEPGAGSDVGSLKTTYTRRNGKVYLNGSKCFITSSAYTPYIVVMARDGASP--DKPVYTEWFVDMSKPGIKV 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 500246517 204 RPI--VDLTGDAhFSEVFFDNVQLGEDALIGNEGDGWKQCTAELAFER 249
Cdd:PRK03354 195 TKLekLGLRMDS-CCEITFDDVELDEKDMFGREGNGFNRVKEEFDHER 241
GCD cd01151
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ...
 2-233 4.33e-23

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: 99.35  E-value: 4.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517   2 FDSLtlatLPDEDEALRPAIRAFIAKHVdglpADRRARSW--QGFDAAFSRALGEAGFLGLTlPAEYGGQGRGAFARFVV 79
Cdd:cd01151    9 LDDL----LTEEERAIRDTAREFCQEEL----APRVLEAYreEKFDRKIIEEMGELGLLGAT-IKGYGCAGLSSVAYGLI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  80 VEELLSAGAPVAAhWIADRQSAPL--ILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVN 157
Cdd:cd01151   80 AREVERVDSGYRS-FMSVQSSLVMlpIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNHGSDPGGMETRARKDGGGYKLN 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 158 GQKIWTTGGMHCDYMIALVRTSGTpadrhAGLSQLIIDLKAPGVTVRPIvdlTGDAHF-----SEVFFDNVQLGEDALIG 232
Cdd:cd01151  159 GSKTWITNSPIADVFVVWARNDET-----GKIRGFILERGMKGLSAPKI---QGKFSLrasitGEIVMDNVFVPEENLLP 230


                 .
gi 500246517 233 N 233
Cdd:cd01151  231 G 231
ACAD_fadE5 cd01153
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ...
 35-331 5.15e-23

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: 99.39  E-value: 5.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  35 DRRARSWQGFDAAFsRALGEAGFLGLTLPAEYGGQGrgaFARFVV--VEELLSAGAPVAAHWIADRQSAPLILNFGNEAQ 112
Cdd:cd01153   29 DGRVVVPPPFKEAL-DAFAEAGWMALGVPEEYGGQG---LPITVYsaLAEIFSRGDAPLMYASGTQGAAATLLAHGTEAQ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 113 RRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAE-RNDKGWVVNGQKIWTTGGMHCDYM----IALVRTSGTPADRHa 187
Cdd:cd01153  105 REKWIPRLAEGEWTGTMCLTEPDAGSDLGALRTKAVyQADGSWRINGVKRFISAGEHDMSEnivhLVLARSEGAPPGVK- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 188 GLSQLII-----DLKAPGVTVRPIVDLTGdAHFS---EVFFDNvqlGEDALIGNEGDGWKQCTAELAFERSGPERiySSV 259
Cdd:cd01153  184 GLSLFLVpkfldDGERNGVTVARIEEKMG-LHGSptcELVFDN---AKGELIGEEGMGLAQMFAMMNGARLGVGT--QGT 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 260 VLLDAWVRHL------RTAGR--GDAAPLV--------------GRLTAElaTLRAMSIACTARLAAGESPVVEASIVKD 317
Cdd:cd01153  258 GLAEAAYLNAlayakeRKQGGdlIKAAPAVtiihhpdvrrslmtQKAYAE--GSRALDLYTATVQDLAERKATEGEDRKA 335

                        330
                 ....*....|....
gi 500246517 318 RGTGLEQELPVVIG 331
Cdd:cd01153  336 LSALADLLTPVVKG 349
IBD cd01162
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ...
 10-238 5.18e-23

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: 99.05  E-value: 5.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  10 LPDEDEALRPAIRAFIAKHVDGLPADRRARswQGFDAAFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAP 89
Cdd:cd01162    1 LNEEQRAIQEVARAFAAKEMAPHAADWDQK--KHFPVDVLRKAAELGFGGIYIRDDVGGSGLSRLDASIIFEALSTGCVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  90 VAAHWIADRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTGGMHC 169
Cdd:cd01162   79 TAAYISIHNMCAWMIDSFGNDEQRERFLPDLCTMEKLASYCLTEPGSGSDAAALRTRAVREGDHYVLNGSKAFISGAGDS 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500246517 170 DYMIALVRTSGTPAdrhAGLSQLIIDLKAPGVTVRPIVDLTG--DAHFSEVFFDNVQLGEDALIGNEGDGW 238
Cdd:cd01162  159 DVYVVMARTGGEGP---KGISCFVVEKGTPGLSFGANEKKMGwnAQPTRAVIFEDCRVPVENRLGGEGQGF 226
ACAD_FadE2 cd01155
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ...
 15-256 1.46e-20

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: 92.07  E-value: 1.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  15 EALRPAIRAFIAKHVdgLPAD--------RRARSWQGFDAAFSRALGEAGFLGL---TLPAEYGGQGRGAF--------- 74
Cdd:cd01155    4 QELRARVKAFMEEHV--YPAEqefleyyaEGGDRWWTPPPIIEKLKAKAKAEGLwnlFLPEVSGLSGLTNLeyaylaeet 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  75 ARFVVVEELLSAGAPvaahwiaDRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPG-SGSDLASVRTRAERNDKG 153
Cdd:cd01155   82 GRSFFAPEVFNCQAP-------DTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDvASSDATNIECSIERDGDD 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 154 WVVNGQKIWTTGGMH--CDYMIALVRTSGTPADRHAGLSQLIIDLKAPGVTV-RPI-VDLTGDAH--FSEVFFDNVQLGE 227
Cdd:cd01155  155 YVINGRKWWSSGAGDprCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIiRPLsVFGYDDAPhgHAEITFDNVRVPA 234

                        250       260
                 ....*....|....*....|....*....
gi 500246517 228 DALIGNEGDGWkqctaELAFERSGPERIY 256
Cdd:cd01155  235 SNLILGEGRGF-----EIAQGRLGPGRIH 258
MCAD cd01157
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ...
 54-252 2.31e-20

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: 91.49  E-value: 2.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  54 EAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVAAHWIADRQS-APLILNfGNEAQRRRHI------PAICRgeql 126
Cdd:cd01157   43 ELGLMNTHIPEDCGGLGLGTFDTCLITEELAYGCTGVQTAIEANSLGqMPVIIS-GNDEQKKKYLgrmteePLMCA---- 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 127 FCIgmSEPGSGSDLASVRTRAERNDKGWVVNGQKIWTTGGMHCDYMIALVRTSGTP-ADRHAGLSQLIIDLKAPGVTV-R 204
Cdd:cd01157  118 YCV--TEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPkCPASKAFTGFIVEADTPGIQPgR 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 500246517 205 PIVDLTGDAHFSEVF-FDNVQLGEDALIGNEGDGWKqcTAELAFERSGP 252
Cdd:cd01157  196 KELNMGQRCSDTRGItFEDVRVPKENVLIGEGAGFK--IAMGAFDKTRP 242
PLN02526 PLN02526
acyl-coenzyme A oxidase
 2-232 3.06e-16

acyl-coenzyme A oxidase


Pssm-ID: 178141 [Multi-domain]  Cd Length: 412  Bit Score: 79.51  E-value: 3.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517   2 FDSLtlatLPDEDEALRPAIRAFIAKHVdglpADRRARSWQGFDAAFS--RALGEAGFLGLTLPAeYGGQGRGAFARFVV 79
Cdd:PLN02526  25 FDDL----LTPEEQALRKRVRECMEKEV----APIMTEYWEKAEFPFHiiPKLGSLGIAGGTIKG-YGCPGLSITASAIA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  80 VEELLSAGAPVAAHWIADRQSAPLILNF-GNEAQRRRHIPAICRGEQLFCIGMSEPGSGSDLASVRTRAERNDKGWVVNG 158
Cdd:PLN02526  96 TAEVARVDASCSTFILVHSSLAMLTIALcGSEAQKQKYLPSLAQLDTVACWALTEPDYGSDASSLNTTATKVEGGWILNG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 159 QKIWTTGGMHCDYMIALVRTSGTPAdrhagLSQLIIDLKAPGVTVRPI---VDL----TGDAHFSEVFFDNvqlgEDALI 231
Cdd:PLN02526 176 QKRWIGNSTFADVLVIFARNTTTNQ-----INGFIVKKGAPGLKATKIenkIGLrmvqNGDIVLKDVFVPD----EDRLP 246


                 .
gi 500246517 232 G 232
Cdd:PLN02526 247 G 247
PLN02876 PLN02876
acyl-CoA dehydrogenase
 76-318 3.83e-12

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 67.90  E-value: 3.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  76 RFVVVEELLSAGAPvaahwiaDRQSAPLILNFGNEAQRRRHIPAICRGEQLFCIGMSEPG-SGSDLASVRTRAERNDKGW 154
Cdd:PLN02876 508 RSVWAPQVFNCGAP-------DTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTEPQvASSDATNIECSIRRQGDSY 580

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 155 VVNGQKIWTTGGM--HCDYMIALVRTSGTpADRHAGLSQLIIDLKAPGVTV-RPIV----DLTGDAHfSEVFFDNVQLGE 227
Cdd:PLN02876 581 VINGTKWWTSGAMdpRCRVLIVMGKTDFN-APKHKQQSMILVDIQTPGVQIkRPLLvfgfDDAPHGH-AEISFENVRVPA 658

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 228 DALIGNEGDGWkqctaELAFERSGPERIYSSVVLLDAWVRHLR-TAGRGDAAPLVGRLTAELATLRAMSIACTARLAAGE 306
Cdd:PLN02876 659 KNILLGEGRGF-----EIAQGRLGPGRLHHCMRLIGAAERGMQlMVQRALSRKAFGKLIAQHGSFLSDLAKCRVELEQTR 733

                        250
                 ....*....|..
gi 500246517 307 SPVVEASIVKDR 318
Cdd:PLN02876 734 LLVLEAADQLDR 745
PTZ00456 PTZ00456
acyl-CoA dehydrogenase; Provisional
 42-168 6.48e-11

acyl-CoA dehydrogenase; Provisional


Pssm-ID: 185635 [Multi-domain]  Cd Length: 622  Bit Score: 63.73  E-value: 6.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  42 QGFDAAFsRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVAAHWIADRQSAPLILNFGNEAQRRRHIPAIC 121
Cdd:PTZ00456  99 KGFKEAY-QALKAGGWTGISEPEEYGGQALPLSVGFITRELMATANWGFSMYPGLSIGAANTLMAWGSEEQKEQYLTKLV 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 500246517 122 RGEQLFCIGMSEPGSGSDLASVRTRAERNDKG-WVVNGQKIWTTGGMH 168
Cdd:PTZ00456 178 SGEWSGTMCLTEPQCGTDLGQVKTKAEPSADGsYKITGTKIFISAGDH 225
DszC cd01163
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ...
 47-232 2.76e-10

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: 61.18  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  47 AFSRALGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVA----AH--WIADrqsaplILNFGNEAQRRRHIPAI 120
Cdd:cd01163   26 EEVALLRQSGLGTLRVPKEYGGLGASLPDLYEVVRELAAADSNIAqalrAHfgFVEA------LLLAGPEQFRKRWFGRV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 121 CRGeQLFCIGMSEPGSgSDLASVRTRAERNDKGWVVNGQKIWTTGGMHCDYMIalvrTSGT-PADRHAglsQLIIDLKAP 199
Cdd:cd01163  100 LNG-WIFGNAVSERGS-VRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVT----VSALdEEGKLV---FAAVPTDRP 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 500246517 200 GVTVrpiVD--------LTGDAhfsEVFFDNVQLGEDALIG 232
Cdd:cd01163  171 GITV---VDdwdgfgqrLTASG---TVTFDNVRVEPDEVLP 205
PRK13026 PRK13026
acyl-CoA dehydrogenase; Reviewed
 52-143 5.07e-07

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 237277 [Multi-domain]  Cd Length: 774  Bit Score: 51.88  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  52 LGEAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVAAHWIADRQSAP--LILNFGNEAQRRRHIPAICRGEQLFCI 129
Cdd:PRK13026 117 LKKEGFFALIIPKEYGGKGFSAYANSTIVSKIATRSVSAAVTVMVPNSLGPgeLLTHYGTQEQKDYWLPRLADGTEIPCF 196

                         90
                 ....*....|....
gi 500246517 130 GMSEPGSGSDLASV 143
Cdd:PRK13026 197 ALTGPEAGSDAGAI 210
fadE PRK09463
acyl-CoA dehydrogenase; Reviewed
 54-142 1.59e-06

acyl-CoA dehydrogenase; Reviewed


Pssm-ID: 236528 [Multi-domain]  Cd Length: 777  Bit Score: 50.20  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  54 EAGFLGLTLPAEYGGQGRGAFARFVVVEELLSAGAPVAAhwiadrqS---------APLILNFGNEAQRRRHIPAICRGE 124
Cdd:PRK09463 120 EHGFFGMIIPKEYGGLEFSAYAHSRVLQKLASRSGTLAV-------TvmvpnslgpGELLLHYGTDEQKDHYLPRLARGE 192

                         90
                 ....*....|....*...
gi 500246517 125 QLFCIGMSEPGSGSDLAS 142
Cdd:PRK09463 193 EIPCFALTSPEAGSDAGS 210
AidB cd01154
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ...
 130-237 5.12e-05

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: 45.05  E-value: 5.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517 130 GMSEPGSGSDLASVRTRAERNDKG-WVVNGQKiWTTGGMHCDYMIALVRTSGTPADRHaGLSQLIIDLKAP-----GVTV 203
Cdd:cd01154  152 WMTEKQGGSDLGANETTAERSGGGvYRLNGHK-WFASAPLADAALVLARPEGAPAGAR-GLSLFLVPRLLEdgtrnGYRI 229

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 500246517 204 RPIVDLTGDAHF--SEVFFDNvqlGEDALIGNEGDG 237
Cdd:cd01154  230 RRLKDKLGTRSVatGEVEFDD---AEAYLIGDEGKG 262
Acyl-CoA_dh_1 pfam00441
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ...
 235-378 3.38e-03

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: 37.62  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  235 GDGWKQCTAELAFER-----SGPERIYSSVVLLDAWVRHLRTAGRGDAA-PLV----GRLTAELATLRAMSIACTARLAA 304
Cdd:pfam00441   1 GRGFRVAMETLNHERlaiaaMALGLARRALDEALAYARRRKAFGRPLIDfQLVrhklAEMAAEIEAARLLVYRAAEALDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  305 GESPVVEASIVKDRGTGLEQElpvvIGDD-------LAAHPDEPVsEELYRTlvyvthvAPSFSLRGGTREILRGIIARG 377
Cdd:pfam00441  81 GGPDGAEASMAKLYASEAAVE----VADLamqlhggYGYLREYPV-ERLYRD-------ARVLRIGEGTSEIQRNIIARR 148


                  .
gi 500246517  378 M 378
Cdd:pfam00441 149 L 149
NcnH cd01159
Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, ...
 50-173 4.98e-03

Naphthocyclinone hydroxylase; Naphthocyclinone is an aromatic polyketide and an antibiotic, which is active against Gram-positive bacteria. Polyketides are secondary metabolites, which have important biological functions such as antitumor, immunosupressive or antibiotic activities. NcnH is a hydroxylase involved in the biosynthesis of naphthocyclinone and possibly other polyketides.


Pssm-ID: 173848 [Multi-domain]  Cd Length: 370  Bit Score: 38.48  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500246517  50 RALGEAGFLGLTLPAEYGGQgRGAFARFV-VVEELlsAGAPVAAHWIADRQSA-PLILN-FGNEAQrrrhipaicrgEQL 126
Cdd:cd01159   29 RALREIGFFRMFVPKRYGGL-EGDFAEFAeAIATL--AEACGSAAWVASIVAThSRMLAaFPPEAQ-----------EEV 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 500246517 127 FcigmsepGSGSDLASVRT-----RAERNDKGWVVNGQKIWTTGGMHCDYMI 173
Cdd:cd01159   95 W-------GDGPDTLLAGSyapggRAERVDGGYRVSGTWPFASGCDHADWIL 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH