NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4557817|ref|NP_000427|]
View 

succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial isoform 3 precursor [Homo sapiens]

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 1.07e-113

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


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 335.51  E-value: 1.07e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817   41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDnfGLGLLLRSKQIKRMVSSY---VG 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  118 ENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK--Y 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 4557817  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 1.37e-109

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: 324.63  E-value: 1.37e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    380 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 4557817    460 LTGKQCVNRIITEKAVFDVDkKKGLTLIELWEGLTVDDVQKSTGCDFAV 508
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
41-279 1.07e-113

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 335.51  E-value: 1.07e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817   41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDnfGLGLLLRSKQIKRMVSSY---VG 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  118 ENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK--Y 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 4557817  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 1.37e-109

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: 324.63  E-value: 1.37e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    380 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 4557817    460 LTGKQCVNRIITEKAVFDVDkKKGLTLIELWEGLTVDDVQKSTGCDFAV 508
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
302-516 1.73e-93

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 284.36  E-value: 1.73e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  302 RERIIKRAALEFEDGMYANLGIGIPLLASNFI--SPNITVHLQSENGVLGLGPYPRQ-HEADADLINAGKEtvtilpgas 378
Cdd:COG2057   5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPgSVGDPDLINAGKQ--------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  379 FFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKgnahKIM 453
Cdd:COG2057  76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557817  454 EKCTLpLTGKQCVN---RIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQ 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 1.70e-82

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: 255.46  E-value: 1.70e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSY--VGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    119 NAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFI 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557817    199 LEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 3.94e-80

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 249.14  E-value: 3.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     43 YTDPVEAV-KDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVdnFGLGLLLRSKQIKRMVSSYVGE--N 119
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    120 AEFERQYLSGELEVELTPQGTLAERIRAGGAGVP--AFYTPTGYGTLVQEGGspikynkdgsvaiaskprEVREFNGQHF 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK------------------RVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557817    198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMC-KAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKG 272
Cdd:pfam01144 141 LLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
48-270 3.16e-75

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: 236.33  E-value: 3.16e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817      48 EAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGvdnFGLGLLLRSKQIKRMVSSYVGENAEFERQYL 127
Cdd:smart00882   4 EAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     128 SGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSpikynkdgsvaiaskPREVREFN-GQHFILEEAITGD 206
Cdd:smart00882  81 DGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYE---------------GGKVRPFGmGGAYLLVPAIRPD 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557817     207 FALVKAWKADRAGNVIFRKSARNFNLP-MCKAAETTVVEVEEIVDIGAFAPEDIH--IPQIYVHRLI 270
Cdd:smart00882 146 VALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
CoA_trans pfam01144
Coenzyme A transferase;
302-501 3.62e-60

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 197.52  E-value: 3.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    302 RERIIKRAALEFEDGMYANLG----IGIP-LLASNFISPNIT--VHLQSENGVLGLGPYPRQHEADADLINAGKETVTIL 374
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    375 PGASFFSSDESFA-MIRGGHVDLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGN 448
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557817    449 AHKIMEKCTLPLTGKQCVN--RIITEKAVFDVD-KKKGLTLIELWEGLTVDDVQKS 501
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVeKGELLPLTVHTPGVLVDAVVEA 216
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-274 3.64e-60

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 197.67  E-value: 3.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    55 DGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVE 134
Cdd:PRK09920  17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817   135 LTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFILEEAITGDFALVKAWK 214
Cdd:PRK09920  97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817   215 ADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK 274
Cdd:PRK09920 159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQE 218
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
305-499 3.35e-50

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: 171.23  E-value: 3.35e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     305 IIKRAALEFEDGMYANLGIG--IPLLASNFIS------PNITvhLQSENGVLGLGPYPrqHEADADLINAGKETVTILPG 376
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILAlirqgpKDLT--LISENGGLGLGLLA--GEGDVKKIIAGHVGLTPLLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     377 ASFFSSD-ESFAMIRGGHVDLTMLGAMQVSKYGDLANWM-------IPGKMVK-GMGGAMDLVSSAKTKVVVTMEHSAK- 446
Cdd:smart00882  77 RLYFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADe 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557817     447 -GNA--HKIMEKCTLPLTGKQ-----CVNRIITEKAVFDVDKKKGLTlielwEGLTVDDVQ 499
Cdd:smart00882 157 fGNLvyEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRLLI-----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 1.07e-113

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 335.51  E-value: 1.07e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817   41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDnfGLGLLLRSKQIKRMVSSY---VG 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  118 ENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK--Y 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 4557817  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 1.37e-109

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: 324.63  E-value: 1.37e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    380 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 4557817    460 LTGKQCVNRIITEKAVFDVDkKKGLTLIELWEGLTVDDVQKSTGCDFAV 508
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
302-516 1.73e-93

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 284.36  E-value: 1.73e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  302 RERIIKRAALEFEDGMYANLGIGIPLLASNFI--SPNITVHLQSENGVLGLGPYPRQ-HEADADLINAGKEtvtilpgas 378
Cdd:COG2057   5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPgSVGDPDLINAGKQ--------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  379 FFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKgnahKIM 453
Cdd:COG2057  76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557817  454 EKCTLpLTGKQCVN---RIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQ 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 1.70e-82

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: 255.46  E-value: 1.70e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSY--VGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    119 NAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFI 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4557817    199 LEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 3.94e-80

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 249.14  E-value: 3.94e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     43 YTDPVEAV-KDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVdnFGLGLLLRSKQIKRMVSSYVGE--N 119
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    120 AEFERQYLSGELEVELTPQGTLAERIRAGGAGVP--AFYTPTGYGTLVQEGGspikynkdgsvaiaskprEVREFNGQHF 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK------------------RVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4557817    198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMC-KAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKG 272
Cdd:pfam01144 141 LLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
48-270 3.16e-75

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: 236.33  E-value: 3.16e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817      48 EAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGvdnFGLGLLLRSKQIKRMVSSYVGENAEFERQYL 127
Cdd:smart00882   4 EAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     128 SGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSpikynkdgsvaiaskPREVREFN-GQHFILEEAITGD 206
Cdd:smart00882  81 DGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYE---------------GGKVRPFGmGGAYLLVPAIRPD 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4557817     207 FALVKAWKADRAGNVIFRKSARNFNLP-MCKAAETTVVEVEEIVDIGAFAPEDIH--IPQIYVHRLI 270
Cdd:smart00882 146 VALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
CoA_trans pfam01144
Coenzyme A transferase;
302-501 3.62e-60

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 197.52  E-value: 3.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    302 RERIIKRAALEFEDGMYANLG----IGIP-LLASNFISPNIT--VHLQSENGVLGLGPYPRQHEADADLINAGKETVTIL 374
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    375 PGASFFSSDESFA-MIRGGHVDLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGN 448
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557817    449 AHKIMEKCTLPLTGKQCVN--RIITEKAVFDVD-KKKGLTLIELWEGLTVDDVQKS 501
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVeKGELLPLTVHTPGVLVDAVVEA 216
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-274 3.64e-60

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 197.67  E-value: 3.64e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817    55 DGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVE 134
Cdd:PRK09920  17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817   135 LTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFILEEAITGDFALVKAWK 214
Cdd:PRK09920  97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817   215 ADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK 274
Cdd:PRK09920 159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQE 218
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
305-499 3.35e-50

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: 171.23  E-value: 3.35e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     305 IIKRAALEFEDGMYANLGIG--IPLLASNFIS------PNITvhLQSENGVLGLGPYPrqHEADADLINAGKETVTILPG 376
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILAlirqgpKDLT--LISENGGLGLGLLA--GEGDVKKIIAGHVGLTPLLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817     377 ASFFSSD-ESFAMIRGGHVDLTMLGAMQVSKYGDLANWM-------IPGKMVK-GMGGAMDLVSSAKTKVVVTMEHSAK- 446
Cdd:smart00882  77 RLYFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADe 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4557817     447 -GNA--HKIMEKCTLPLTGKQ-----CVNRIITEKAVFDVDKKKGLTlielwEGLTVDDVQ 499
Cdd:smart00882 157 fGNLvyEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRLLI-----PGVLVDAVV 212
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
41-500 9.75e-37

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 142.17  E-value: 9.75e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817   41 KFYTdPVEAVKDIPDGATVLVGGFGLCGIPENLIDAL----LKTGV-KGLTAVSNNA-------GVDNFGL-GLllrskq 107
Cdd:COG4670   2 KIIS-AEEAAALIKDGDTVATSGFVGAGVPEELLKALeerfLETGHpRDLTLIHAAGqgdgkgrGLDHLAHeGL------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  108 IKRMVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLV---QEGGspiKYNkdgsvAIAS 184
Cdd:COG4670  75 VKRVIGGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVdprLEGG---KLN-----ERTT 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  185 KPR-EVREFNGQHFILEEAITGDFALVKAWKADRAGNVIF-RKSARNFNLPMCKAAE----TTVVEVEEIVDIGAFAPED 258
Cdd:COG4670 147 EDLvELVEIDGEEYLFYKAFPIDVALIRGTTADEDGNLSMeHEALTLEVLAIAQAAKnsggIVIAQVERIVKRGSLHPKD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  259 IHIPQIYV----------HRLIKGEKYEKRIErlsirkegdGEAK-----SAKPGDDVRERIIKRAALEFEDGMYANLGI 323
Cdd:COG4670 227 VKVPGILVdyvvvappedHMQTFSTQYNPAYS---------GEIRvplssLPPLPLDERKVIARRAAMELRPGAVVNLGI 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  324 GIPLLASNFIspnitvhlqSENGVlglgpyprqheadADLInagkeTVTILPGA---------SFFSSDESFAMIR---- 390
Cdd:COG4670 298 GIPEGVAAVA---------AEEGI-------------SDLI-----TLTVESGPiggvpagglDFGAAVNAEAIIDqpdq 350
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  391 -----GGHVDLTMLGAMQVSKYGDLANWMIPGKMVkGMGGAMDLVSSAKT-------------------KVVVTMEhsak 446
Cdd:COG4670 351 fdfydGGGLDIAFLGFAQVDRHGNVNVSKFGGRIA-GCGGFINITQNAKKvvfcgtftagglkvevedgKLRILQE---- 425
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557817  447 GNAHKIMEKctlpltgkqcVNRI----------------ITEKAVFDVdKKKGLTLIELWEGLtvdDVQK 500
Cdd:COG4670 426 GKIKKFVKK----------VEQItfsgkyarergqevlyVTERAVFEL-TPEGLELTEIAPGI---DLER 481
 
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