NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1823847314|ref|XP_032966629|]
View 

succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial [Rhinolophus ferrumequinum]

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 3.35e-110

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


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 326.66  E-value: 3.35e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  41 KFYTDPVEAVKDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGcdNFGLGLLLQSKQIKRMVSSY---VG 117
Cdd:COG1788     3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAG--VDGLGLLIGAGQVKKVIASYvggVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 118 ENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHF 197
Cdd:COG1788    81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 198 ILEEAITGDFALVKAWKADQAGNIIFRKSARNFNLPMCKAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK--Y 275
Cdd:COG1788   143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                  ....
gi 1823847314 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 2.87e-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: 323.47  E-value: 2.87e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 300 NVRERIIRRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLQNEVDADLINAGKETVTVLPGASY 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 380 FSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1823847314 460 LTGKQCVSRIITEKAVFDVDsKKGLTLIELWEGLTVDDIKKSTGCDFAV 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 3.35e-110

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 326.66  E-value: 3.35e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  41 KFYTDPVEAVKDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGcdNFGLGLLLQSKQIKRMVSSY---VG 117
Cdd:COG1788     3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAG--VDGLGLLIGAGQVKKVIASYvggVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 118 ENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHF 197
Cdd:COG1788    81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 198 ILEEAITGDFALVKAWKADQAGNIIFRKSARNFNLPMCKAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK--Y 275
Cdd:COG1788   143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                  ....
gi 1823847314 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 2.87e-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: 323.47  E-value: 2.87e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 300 NVRERIIRRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLQNEVDADLINAGKETVTVLPGASY 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 380 FSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1823847314 460 LTGKQCVSRIITEKAVFDVDsKKGLTLIELWEGLTVDDIKKSTGCDFAV 508
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
302-519 6.08e-94

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 285.52  E-value: 6.08e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 302 RERIIRRAALEFEDGMYANLGIGIPLLASNFI--SPNMTVHLQSENGVLGLGPYPLQNEV-DADLINAGKEtvtvlpgas 378
Cdd:COG2057     5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPGSVgDPDLINAGKQ--------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 379 YFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKgnahKIM 453
Cdd:COG2057    76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823847314 454 EKCTLpLTGKQCVS---RIITEKAVFDVDSKKGLTLIELWEGLTVDDIKKSTGCDFAVSPKLMPMQQIT 519
Cdd:COG2057   151 EKCDL-LTGPGVVDgprRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADDVPETPPPT 218
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
41-270 5.81e-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: 246.60  E-value: 5.81e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  41 KFYTDPVEAVKDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGCDNFGLGLLLQSKQIKRMVSSY--VGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 119 NAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHFI 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823847314 199 LEEAITGDFALVKAWKADQAGNIIFRKSARNFNLPMCKAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 4.82e-77

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 241.44  E-value: 4.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  43 YTDPVEAV-KDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGcdNFGLGLLLQSKQIKRMVSSYVGE--N 119
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAG--VLGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 120 AEFERQYLAGELEVELTPQGTLAERIRAGGAGVP--AFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHF 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPK------------------KRVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823847314 198 ILEEAITGDFALVKAWKADQAGNIIFRKSARNFNLPMC-KAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKG 272
Cdd:pfam01144 141 LLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
48-270 1.36e-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: 1.36e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314   48 EAVKDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGcdnFGLGLLLQSKQIKRMVSSYVGENAEFERQYL 127
Cdd:smart00882   4 EAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  128 AGELEVELTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGGSPikynkdgsiaiaskPKEVKEFNGQHFILEEAITGDF 207
Cdd:smart00882  81 DGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYEG--------------GKVRPFGMGGAYLLVPAIRPDV 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823847314  208 ALVKAWKADQAGNIIFRKSARNFNLP-MCKAAETSVVEVEEIVDIGSFAPEDIH--IPKIYVHRLI 270
Cdd:smart00882 147 ALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
CoA_trans pfam01144
Coenzyme A transferase;
302-501 1.39e-59

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 195.98  E-value: 1.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 302 RERIIRRAALEFEDGMYANLG----IGIP-LLASNFISPNMT--VHLQSENGVLGLGPYPLQNEVDADLINAGKETVTVL 374
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 375 PGASYFSSDESFA-MIRGGHVNLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGN 448
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823847314 449 AHKIMEKCTLPLTGKQCVS--RIITEKAVFDVDSK-KGLTLIELWEGLTVDDIKKS 501
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVEKgELLPLTVHTPGVLVDAVVEA 216
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-274 1.68e-58

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 193.43  E-value: 1.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  55 DGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGCDNFGLGLLLQSKQIKRMVSSYVGENAEFERQYLAGELEVE 134
Cdd:PRK09920   17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 135 LTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHFILEEAITGDFALVKAWK 214
Cdd:PRK09920   97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 215 ADQAGNIIFRKSARNFNLPMCKAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK 274
Cdd:PRK09920  159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQE 218
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
305-499 2.83e-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: 2.83e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  305 IIRRAALEFEDGMYANLGIG--IPLLASNFI----SPNMTVHLQSENGVLGLGPYPLqnEVDADLINAGKETVTVLPGAS 378
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILalirQGPKDLTLISENGGLGLGLLAG--EGDVKKIIAGHVGLTPLLGRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  379 YFSSD-ESFAMIRGGHVNLTMLGAMQVSKYGDLANWM-------IPGKMVK-GMGGAMDLVSSAKTKVVVTMEHSAK--G 447
Cdd:smart00882  79 YFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADefG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1823847314  448 NA--HKIMEKCTLPLTGKQ-----CVSRIITEKAVFDVDSKKGLTlielwEGLTVDDIK 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 3.35e-110

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 326.66  E-value: 3.35e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  41 KFYTDPVEAVKDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGcdNFGLGLLLQSKQIKRMVSSY---VG 117
Cdd:COG1788     3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAG--VDGLGLLIGAGQVKKVIASYvggVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 118 ENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHF 197
Cdd:COG1788    81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 198 ILEEAITGDFALVKAWKADQAGNIIFRKSARNFNLPMCKAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK--Y 275
Cdd:COG1788   143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                  ....
gi 1823847314 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 2.87e-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: 323.47  E-value: 2.87e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 300 NVRERIIRRAALEFEDGMYANLGIGIPLLASNFISPNMTVHLQSENGVLGLGPYPLQNEVDADLINAGKETVTVLPGASY 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 380 FSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKGNAHKIMEKCTLP 459
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1823847314 460 LTGKQCVSRIITEKAVFDVDsKKGLTLIELWEGLTVDDIKKSTGCDFAV 508
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
302-519 6.08e-94

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 285.52  E-value: 6.08e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 302 RERIIRRAALEFEDGMYANLGIGIPLLASNFI--SPNMTVHLQSENGVLGLGPYPLQNEV-DADLINAGKEtvtvlpgas 378
Cdd:COG2057     5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPGSVgDPDLINAGKQ--------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 379 YFSSDESFAMIRGGHVNLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAKtKVVVTMEHSAKgnahKIM 453
Cdd:COG2057    76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1823847314 454 EKCTLpLTGKQCVS---RIITEKAVFDVDSKKGLTLIELWEGLTVDDIKKSTGCDFAVSPKLMPMQQIT 519
Cdd:COG2057   151 EKCDL-LTGPGVVDgprRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADDVPETPPPT 218
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
41-270 5.81e-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: 246.60  E-value: 5.81e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  41 KFYTDPVEAVKDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGCDNFGLGLLLQSKQIKRMVSSY--VGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 119 NAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHFI 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1823847314 199 LEEAITGDFALVKAWKADQAGNIIFRKSARNFNLPMCKAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 4.82e-77

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 241.44  E-value: 4.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  43 YTDPVEAV-KDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGcdNFGLGLLLQSKQIKRMVSSYVGE--N 119
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAG--VLGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 120 AEFERQYLAGELEVELTPQGTLAERIRAGGAGVP--AFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHF 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPK------------------KRVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823847314 198 ILEEAITGDFALVKAWKADQAGNIIFRKSARNFNLPMC-KAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKG 272
Cdd:pfam01144 141 LLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
48-270 1.36e-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: 1.36e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314   48 EAVKDIPDGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGcdnFGLGLLLQSKQIKRMVSSYVGENAEFERQYL 127
Cdd:smart00882   4 EAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  128 AGELEVELTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGGSPikynkdgsiaiaskPKEVKEFNGQHFILEEAITGDF 207
Cdd:smart00882  81 DGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYEG--------------GKVRPFGMGGAYLLVPAIRPDV 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1823847314  208 ALVKAWKADQAGNIIFRKSARNFNLP-MCKAAETSVVEVEEIVDIGSFAPEDIH--IPKIYVHRLI 270
Cdd:smart00882 147 ALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
CoA_trans pfam01144
Coenzyme A transferase;
302-501 1.39e-59

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 195.98  E-value: 1.39e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 302 RERIIRRAALEFEDGMYANLG----IGIP-LLASNFISPNMT--VHLQSENGVLGLGPYPLQNEVDADLINAGKETVTVL 374
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 375 PGASYFSSDESFA-MIRGGHVNLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGN 448
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1823847314 449 AHKIMEKCTLPLTGKQCVS--RIITEKAVFDVDSK-KGLTLIELWEGLTVDDIKKS 501
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVEKgELLPLTVHTPGVLVDAVVEA 216
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-274 1.68e-58

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 193.43  E-value: 1.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  55 DGAKILVGGFGLCGIPENLIGALLKTGVKGLTAISNNAGCDNFGLGLLLQSKQIKRMVSSYVGENAEFERQYLAGELEVE 134
Cdd:PRK09920   17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 135 LTPQGTLAERIRAGGAGVPAFYTRTGYGTLVQEGgspikynkdgsiaiaskpKEVKEFNGQHFILEEAITGDFALVKAWK 214
Cdd:PRK09920   97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 215 ADQAGNIIFRKSARNFNLPMCKAAETSVVEVEEIVDIGSFAPEDIHIPKIYVHRLIKGEK 274
Cdd:PRK09920  159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQE 218
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
305-499 2.83e-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: 2.83e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  305 IIRRAALEFEDGMYANLGIG--IPLLASNFI----SPNMTVHLQSENGVLGLGPYPLqnEVDADLINAGKETVTVLPGAS 378
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILalirQGPKDLTLISENGGLGLGLLAG--EGDVKKIIAGHVGLTPLLGRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  379 YFSSD-ESFAMIRGGHVNLTMLGAMQVSKYGDLANWM-------IPGKMVK-GMGGAMDLVSSAKTKVVVTMEHSAK--G 447
Cdd:smart00882  79 YFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADefG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1823847314  448 NA--HKIMEKCTLPLTGKQ-----CVSRIITEKAVFDVDSKKGLTlielwEGLTVDDIK 499
Cdd:smart00882 159 NLvyEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRLLI-----PGVLVDAVV 212
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
41-514 2.43e-38

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 146.80  E-value: 2.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314  41 KFYTdPVEAVKDIPDGAKILVGGFGLCGIPENLIGAL----LKTGV-KGLTAISnNAGC---DNFGLGLLLQSKQIKRMV 112
Cdd:COG4670     2 KIIS-AEEAAALIKDGDTVATSGFVGAGVPEELLKALeerfLETGHpRDLTLIH-AAGQgdgKGRGLDHLAHEGLVKRVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 113 SSYVGENAEFERQYLAGELEVELTPQGTLAERIRAGGAGVPAFYTRTGYGTLV---QEGGspiKYNkdgsiAIASKPK-E 188
Cdd:COG4670    80 GGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVdprLEGG---KLN-----ERTTEDLvE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 189 VKEFNGQHFILEEAITGDFALVKAWKADQAGNIIF-RKSARNFNLPMCKAAETS----VVEVEEIVDIGSFAPEDIHIPK 263
Cdd:COG4670   152 LVEIDGEEYLFYKAFPIDVALIRGTTADEDGNLSMeHEALTLEVLAIAQAAKNSggivIAQVERIVKRGSLHPKDVKVPG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 264 IYV----------HRLIKGEKYEKRIerlsirkEGDVKT--KSGKPGE-NVRERIIRRAALEFEDGMYANLGIGIPLLAS 330
Cdd:COG4670   232 ILVdyvvvappedHMQTFSTQYNPAY-------SGEIRVplSSLPPLPlDERKVIARRAAMELRPGAVVNLGIGIPEGVA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 331 NF-----ISPNMTvhLQSENGVLGlGpYPLQnevDADLinagketvtvlpGASY-----FSSDESFAMIRGGHVNLTMLG 400
Cdd:COG4670   305 AVaaeegISDLIT--LTVESGPIG-G-VPAG---GLDF------------GAAVnaeaiIDQPDQFDFYDGGGLDIAFLG 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1823847314 401 AMQVSKYGDLANWMIPGKMVkGMGGAMDLVSSAKT-------------------KVVVTMEhsakGNAHKIM---EKCTl 458
Cdd:COG4670   366 FAQVDRHGNVNVSKFGGRIA-GCGGFINITQNAKKvvfcgtftagglkvevedgKLRILQE----GKIKKFVkkvEQIT- 439
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1823847314 459 pLTGKQCVSR-----IITEKAVFDVdSKKGLTLIELWEGLTVD-DI--KkstgCDFAV----SPKLMP 514
Cdd:COG4670   440 -FSGKYARERgqevlYVTERAVFEL-TPEGLELTEIAPGIDLErDIlaQ----MEFRPiiadDLKLMD 501
 
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