NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18266680|ref|NP_077150|]
View 

succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial precursor [Mus musculus]

Protein Classification

3-oxoacid CoA-transferase( domain architecture ID 10004516)

3-oxoacid CoA-transferase such as succinyl-CoA:3-ketoacid coenzyme A transferase that catalyzes the transfer of the CoA moiety from succinate to acetoacetate

CATH:  3.40.1080.10
EC:  2.8.3.5
Gene Ontology:  GO:0008410|GO:0046952
PubMed:  11749953

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
41-279 6.02e-110

Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 325.88  E-value: 6.02e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680  41 KFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDnfGLGLLLRSKQIKRMISSY---VG 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 118 ENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK--Y 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 18266680 276 EKRI 279
Cdd:COG1788 223 DKRI 226
SugarP_isomerase super family cl00339
SugarP_isomerase: Sugar Phosphate Isomerase family; includes type A ribose 5-phosphate ...
300-508 6.46e-108

SugarP_isomerase: Sugar Phosphate Isomerase family; includes type A ribose 5-phosphate isomerase (RPI_A), glucosamine-6-phosphate (GlcN6P) deaminase, and 6-phosphogluconolactonase (6PGL). RPI catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate, the first step of the non-oxidative branch of the pentose phosphate pathway. GlcN6P deaminase catalyzes the reversible conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and ammonium, the last step of the metabolic pathway of N-acetyl-D-glucosamine-6-phosphate. 6PGL converts 6-phosphoglucono-1,5-lactone to 6-phosphogluconate, the second step of the oxidative phase of the pentose phosphate pathway.


The actual alignment was detected with superfamily member TIGR02428:

Pssm-ID: 469729  Cd Length: 207  Bit Score: 320.39  E-value: 6.46e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   380 FSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 18266680   460 LTGKQCVNRIITEKGVFDVDKKnGLTLIELWEGLTVDDIKKSTGCDFAV 508
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVTDG-GLILRELAPGVTVEELQAKTEADLII 207
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
41-279 6.02e-110

Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 441394  Cd Length: 226  Bit Score: 325.88  E-value: 6.02e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680  41 KFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDnfGLGLLLRSKQIKRMISSY---VG 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 118 ENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK--Y 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 18266680 276 EKRI 279
Cdd:COG1788 223 DKRI 226
pcaJ_scoB_fam TIGR02428
3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the ...
300-508 6.46e-108

3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the B subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The A subunit represents a different clade in pfam01144.


Pssm-ID: 188219  Cd Length: 207  Bit Score: 320.39  E-value: 6.46e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   380 FSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 18266680   460 LTGKQCVNRIITEKGVFDVDKKnGLTLIELWEGLTVDDIKKSTGCDFAV 508
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVTDG-GLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
302-516 2.22e-92

Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];


Pssm-ID: 441660  Cd Length: 235  Bit Score: 281.28  E-value: 2.22e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 302 RERIIKRAALEFEDGMYANLGIGIPLLASNFI--SPNMTVHLQSENGVLGLGPYPLKDE-ADADLINAGKEtvtvlpgas 378
Cdd:COG2057   5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPGSvGDPDLINAGKQ--------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 379 FFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSSKtKVVVTMEHSAKgnahKIM 453
Cdd:COG2057  76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18266680 454 EKCTLpLTGKQCVN---RIITEKGVFDVDKKNGLTLIELWEGLTVDDIKKSTGCDFAVSPNLMPMQ 516
Cdd:COG2057 151 EKCDL-LTGPGVVDgprRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADDVPETP 215
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
41-270 2.92e-79

3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the A subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The B subunit represents a different clade in pfam01144, described by TIGR02428. The two are found in general as tandem genes and occasionally as a fusion.


Pssm-ID: 131482  Cd Length: 222  Bit Score: 247.37  E-value: 2.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    41 KFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSY--VGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   119 NAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFI 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18266680   199 LEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 1.07e-78

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 245.67  E-value: 1.07e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    43 YTDPVEAV-KDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVdnFGLGLLLRSKQIKRMISSYVGE--N 119
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   120 AEFERQFLSGELEVELTPQGTLAERIRAGGAGVP--AFYTSTGYGTLVQEGGspikynkdgsvaiaskprEVREFNGQHF 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK------------------RVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18266680   198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMC-KAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKG 272
Cdd:pfam01144 141 LLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
48-270 1.32e-73

Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.


Pssm-ID: 214882 [Multi-domain]  Cd Length: 212  Bit Score: 232.10  E-value: 1.32e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680     48 EAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGvdnFGLGLLLRSKQIKRMISSYVGENAEFERQFL 127
Cdd:smart00882   4 EAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    128 SGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSpikynkdgsvaiaskPREVREFN-GQHFILEEAITGD 206
Cdd:smart00882  81 DGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYE---------------GGKVRPFGmGGAYLLVPAIRPD 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18266680    207 FALVKAWKADRAGNVIFRKSARNFNLP-MCKAAGTTVVEVEEIVDIGSFAPEDIH--IPKIYVHRLI 270
Cdd:smart00882 146 VALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-274 3.93e-58

acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 192.27  E-value: 3.93e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   55 NGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVE 134
Cdd:PRK09920  17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680  135 LTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFILEEAITGDFALVKAWK 214
Cdd:PRK09920  97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680  215 ADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK 274
Cdd:PRK09920 159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQE 218
CoA_trans pfam01144
Coenzyme A transferase;
302-501 7.87e-58

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 191.36  E-value: 7.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   302 RERIIKRAALEFEDGMYANLG----IGIP-LLASNFISPNMT--VHLQSENGVLGLGPYPLKDEADADLINAGKETVTVL 374
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   375 PGASFFSSDESFA-MIRGGHVNLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSSKTKVVVTMEHSAKGN 448
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18266680   449 AHKIMEKCTLPLTGKQCVN--RIITEKGVFDVD-KKNGLTLIELWEGLTVDDIKKS 501
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVeKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
305-499 1.47e-48

Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.


Pssm-ID: 214882 [Multi-domain]  Cd Length: 212  Bit Score: 166.61  E-value: 1.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    305 IIKRAALEFEDGMYANLGIG--IPLLASNFI----SPNMTVHLQSENGVLGLGPYPLkdEADADLINAGKETVTVLPGAS 378
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILalirQGPKDLTLISENGGLGLGLLAG--EGDVKKIIAGHVGLTPLLGRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    379 FFSSD-ESFAMIRGGHVNLTMLGAMQVSKYGDLANWM-------IPGKMVK-GMGGAMDLVSSSKTKVVVTMEHSAK--G 447
Cdd:smart00882  79 YFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADefG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 18266680    448 NA--HKIMEKCTLPLTGKQ-----CVNRIITEKGVFDVDKKNGLTlielwEGLTVDDIK 499
Cdd:smart00882 159 NLvyEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRLLI-----PGVLVDAVV 212
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
41-279 6.02e-110

Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];


Pssm-ID: 441394  Cd Length: 226  Bit Score: 325.88  E-value: 6.02e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680  41 KFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDnfGLGLLLRSKQIKRMISSY---VG 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 118 ENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK--Y 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 18266680 276 EKRI 279
Cdd:COG1788 223 DKRI 226
pcaJ_scoB_fam TIGR02428
3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the ...
300-508 6.46e-108

3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the B subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The A subunit represents a different clade in pfam01144.


Pssm-ID: 188219  Cd Length: 207  Bit Score: 320.39  E-value: 6.46e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLKDEADADLINAGKETVTVLPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   380 FSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSSKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 18266680   460 LTGKQCVNRIITEKGVFDVDKKnGLTLIELWEGLTVDDIKKSTGCDFAV 508
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVTDG-GLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
302-516 2.22e-92

Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];


Pssm-ID: 441660  Cd Length: 235  Bit Score: 281.28  E-value: 2.22e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 302 RERIIKRAALEFEDGMYANLGIGIPLLASNFI--SPNMTVHLQSENGVLGLGPYPLKDE-ADADLINAGKEtvtvlpgas 378
Cdd:COG2057   5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPGSvGDPDLINAGKQ--------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 379 FFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSSKtKVVVTMEHSAKgnahKIM 453
Cdd:COG2057  76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18266680 454 EKCTLpLTGKQCVN---RIITEKGVFDVDKKNGLTLIELWEGLTVDDIKKSTGCDFAVSPNLMPMQ 516
Cdd:COG2057 151 EKCDL-LTGPGVVDgprRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADDVPETP 215
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
41-270 2.92e-79

3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the A subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The B subunit represents a different clade in pfam01144, described by TIGR02428. The two are found in general as tandem genes and occasionally as a fusion.


Pssm-ID: 131482  Cd Length: 222  Bit Score: 247.37  E-value: 2.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    41 KFYTDPVEAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSY--VGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   119 NAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFI 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18266680   199 LEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 1.07e-78

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 245.67  E-value: 1.07e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    43 YTDPVEAV-KDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVdnFGLGLLLRSKQIKRMISSYVGE--N 119
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   120 AEFERQFLSGELEVELTPQGTLAERIRAGGAGVP--AFYTSTGYGTLVQEGGspikynkdgsvaiaskprEVREFNGQHF 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK------------------RVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18266680   198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMC-KAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKG 272
Cdd:pfam01144 141 LLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
48-270 1.32e-73

Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.


Pssm-ID: 214882 [Multi-domain]  Cd Length: 212  Bit Score: 232.10  E-value: 1.32e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680     48 EAVKDIPNGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGvdnFGLGLLLRSKQIKRMISSYVGENAEFERQFL 127
Cdd:smart00882   4 EAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    128 SGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGGSpikynkdgsvaiaskPREVREFN-GQHFILEEAITGD 206
Cdd:smart00882  81 DGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYE---------------GGKVRPFGmGGAYLLVPAIRPD 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18266680    207 FALVKAWKADRAGNVIFRKSARNFNLP-MCKAAGTTVVEVEEIVDIGSFAPEDIH--IPKIYVHRLI 270
Cdd:smart00882 146 VALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-274 3.93e-58

acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 192.27  E-value: 3.93e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   55 NGATLLVGGFGLCGIPENLIGALLKTGVKDLTAVSNNAGVDNFGLGLLLRSKQIKRMISSYVGENAEFERQFLSGELEVE 134
Cdd:PRK09920  17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680  135 LTPQGTLAERIRAGGAGVPAFYTSTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFILEEAITGDFALVKAWK 214
Cdd:PRK09920  97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680  215 ADRAGNVIFRKSARNFNLPMCKAAGTTVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK 274
Cdd:PRK09920 159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQE 218
CoA_trans pfam01144
Coenzyme A transferase;
302-501 7.87e-58

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 191.36  E-value: 7.87e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   302 RERIIKRAALEFEDGMYANLG----IGIP-LLASNFISPNMT--VHLQSENGVLGLGPYPLKDEADADLINAGKETVTVL 374
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680   375 PGASFFSSDESFA-MIRGGHVNLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSSKTKVVVTMEHSAKGN 448
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18266680   449 AHKIMEKCTLPLTGKQCVN--RIITEKGVFDVD-KKNGLTLIELWEGLTVDDIKKS 501
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVeKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
305-499 1.47e-48

Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.


Pssm-ID: 214882 [Multi-domain]  Cd Length: 212  Bit Score: 166.61  E-value: 1.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    305 IIKRAALEFEDGMYANLGIG--IPLLASNFI----SPNMTVHLQSENGVLGLGPYPLkdEADADLINAGKETVTVLPGAS 378
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILalirQGPKDLTLISENGGLGLGLLAG--EGDVKKIIAGHVGLTPLLGRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680    379 FFSSD-ESFAMIRGGHVNLTMLGAMQVSKYGDLANWM-------IPGKMVK-GMGGAMDLVSSSKTKVVVTMEHSAK--G 447
Cdd:smart00882  79 YFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADefG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 18266680    448 NA--HKIMEKCTLPLTGKQ-----CVNRIITEKGVFDVDKKNGLTlielwEGLTVDDIK 499
Cdd:smart00882 159 NLvyEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRLLI-----PGVLVDAVV 212
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
41-515 3.30e-35

Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 137.94  E-value: 3.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680  41 KFYTdPVEAVKDIPNGATLLVGGFGLCGIPENLIGAL----LKTGV-KDLTAVSNNA-------GVDNFGL-GLllrskq 107
Cdd:COG4670   2 KIIS-AEEAAALIKDGDTVATSGFVGAGVPEELLKALeerfLETGHpRDLTLIHAAGqgdgkgrGLDHLAHeGL------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 108 IKRMISSYVGENAEFERQFLSGELEVELTPQGTLAERIRAGGAGVPAFYTSTGYGTLV---QEGGspiKYNkdgsvAIAS 184
Cdd:COG4670  75 VKRVIGGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVdprLEGG---KLN-----ERTT 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 185 KPR-EVREFNGQHFILEEAITGDFALVKAWKADRAGNVIF-RKSARNFNLPMCKAA----GTTVVEVEEIVDIGSFAPED 258
Cdd:COG4670 147 EDLvELVEIDGEEYLFYKAFPIDVALIRGTTADEDGNLSMeHEALTLEVLAIAQAAknsgGIVIAQVERIVKRGSLHPKD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 259 IHIPKIYV----------HRLIKGEKYEKRI---ERLSLrkegdgkGKSGKPGGDVRERIIKRAALEFEDGMYANLGIGI 325
Cdd:COG4670 227 VKVPGILVdyvvvappedHMQTFSTQYNPAYsgeIRVPL-------SSLPPLPLDERKVIARRAAMELRPGAVVNLGIGI 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 326 PLLASNF-----ISPNMTvhLQSENGVLGlGpyplkdeadadlinagketvTVLPGASFFSSDESFAMIR---------G 391
Cdd:COG4670 300 PEGVAAVaaeegISDLIT--LTVESGPIG-G--------------------VPAGGLDFGAAVNAEAIIDqpdqfdfydG 356
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 392 GHVNLTMLGAMQVSKYGDLANWMIPGKMVkGMGGAMDLVSSSKT-------------------KVVVTMEhsakGNAHKI 452
Cdd:COG4670 357 GGLDIAFLGFAQVDRHGNVNVSKFGGRIA-GCGGFINITQNAKKvvfcgtftagglkvevedgKLRILQE----GKIKKF 431
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18266680 453 MEKctlpltgkqcVNRI----------------ITEKGVFDVdKKNGLTLIELWEGLTVD-DI--KkstgCDF--AVSPN 511
Cdd:COG4670 432 VKK----------VEQItfsgkyarergqevlyVTERAVFEL-TPEGLELTEIAPGIDLErDIlaQ----MEFrpIIADD 496

                ....
gi 18266680 512 LMPM 515
Cdd:COG4670 497 LKLM 500
 
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