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Conserved domains on  [gi|58866010|ref|NP_001012221|]
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succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial precursor [Rattus norvegicus]

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

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List of domain hits

Name Accession Description Interval E-value
SugarP_isomerase super family cl00339
SugarP_isomerase: Sugar Phosphate Isomerase family; includes type A ribose 5-phosphate ...
300-506 6.07e-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: 322.70  E-value: 6.07e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   300 RTRIIKRAALEFKDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKKEVDPDIINAGKQTVTVIPGGCFFA 379
Cdd:TIGR02428   3 RDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASYFD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   380 SDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMVPGKKVKGMGGAMDLVSSKKtKVVVTMEHCTKTKQPKILEKCTMPLT 459
Cdd:TIGR02428  83 SADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLPLT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 58866010   460 GKSCVDLIITEKAVFEVDrSKGLKLVELWEGSSLDEVKATTGCSFKV 506
Cdd:TIGR02428 162 GAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
41-279 1.52e-92

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


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 281.59  E-value: 1.52e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010  41 KFYTDPVKAVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDdfGLGILLASKQVRRVVCSYL---G 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYVggvG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 118 ENKLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGgvpiryspeghlitlsqpREVREFEGQHH 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 198 LLERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVIKGPR--F 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 58866010 276 EKRI 279
Cdd:COG1788 223 DKRI 226
 
Name Accession Description Interval E-value
pcaJ_scoB_fam TIGR02428
3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the ...
300-506 6.07e-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: 322.70  E-value: 6.07e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   300 RTRIIKRAALEFKDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKKEVDPDIINAGKQTVTVIPGGCFFA 379
Cdd:TIGR02428   3 RDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASYFD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   380 SDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMVPGKKVKGMGGAMDLVSSKKtKVVVTMEHCTKTKQPKILEKCTMPLT 459
Cdd:TIGR02428  83 SADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLPLT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 58866010   460 GKSCVDLIITEKAVFEVDrSKGLKLVELWEGSSLDEVKATTGCSFKV 506
Cdd:TIGR02428 162 GAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
41-279 1.52e-92

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 281.59  E-value: 1.52e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010  41 KFYTDPVKAVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDdfGLGILLASKQVRRVVCSYL---G 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYVggvG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 118 ENKLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGgvpiryspeghlitlsqpREVREFEGQHH 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 198 LLERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVIKGPR--F 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 58866010 276 EKRI 279
Cdd:COG1788 223 DKRI 226
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
300-514 1.39e-89

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 274.35  E-value: 1.39e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 300 RTRIIKRAALEFKDGMYANLGIGIPVLASNYI--SPKMTVYLHSENGILGLGPFPLKKEV-DPDIINAGKQtvtvipggc 376
Cdd:COG2057   5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPGSVgDPDLINAGKQ--------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 377 FFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMV-----PGKKVKGMGGAMDLVSSKKtKVVVTMEHCTKtkqpKIL 451
Cdd:COG2057  76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58866010 452 EKCTMpLTGKSCVD---LIITEKAVFEVDRSKGLKLVELWEGSSLDEVKATTGCSFKVCPNLKPMQ 514
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 6.23e-72

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: 228.49  E-value: 6.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    41 KFYTDPVKAVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDDFGLGILLASKQVRRVVCSY--LGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   119 NKLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGgvpiryspeghlitlsqpREVREFEGQHHL 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58866010   199 LERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 9.20e-62

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 201.76  E-value: 9.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    43 YTDPVKAVEG-IKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVddFGLGILLASKQVRRVVCSYLGE--N 119
Cdd:pfam01144   1 VESAAEAVAKeIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   120 KLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVP--AFYTPTGYGTQVQEGGvpiryspeghlitlsqprEVREFEGQHH 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK------------------RVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58866010   198 LLERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMC-KAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVIKG 272
Cdd:pfam01144 141 LLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
49-270 9.14e-61

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: 198.97  E-value: 9.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010     49 AVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGvddFGLGILLASKQVRRVVCSYLGENKLCEQLYLA 128
Cdd:smart00882   5 AAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYFD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    129 GKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGGvpiryspeghlitlsQPREVREF-EGQHHLLERAIRADF 207
Cdd:smart00882  82 GEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRY---------------EGGKVRPFgMGGAYLLVPAIRPDV 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58866010    208 ALIKGWKADRSGNVIFRGSARNFNVP-MCKAADISVVEVEEIVDVGTFAPEDIH--IPNIYVKRVI 270
Cdd:smart00882 147 ALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
CoA_trans pfam01144
Coenzyme A transferase;
300-498 1.47e-55

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 185.58  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   300 RTRIIKRAALEFKDGMYANLG----IGIPV-LASNYIS--PKMTVYLHSENGILGLGPFPLKKEVDPDIINAGKQTVTVI 372
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPEtLIAALARsgVKDLTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   373 PGGCFFASDDSFA-MIRGGHIQLTMLGAMQVSKYGDLANWMV-----PGKKVKGMGGAMDLVSSKKTKVVVTMEHCTKTK 446
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 58866010   447 QPKILEKCTMPLTGKSCVDL--IITEKAVFEVDR-SKGLKLVELWEGSSLDEVKA 498
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAAaaKVTILEVEEIVEkGELLPLTVHTPGVLVDAVVE 215
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-270 3.00e-50

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 171.47  E-value: 3.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   55 DGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDDFGLGILLASKQVRRVVCSYLGENKLCEQLYLAGKLELE 134
Cdd:PRK09920  17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010  135 MTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGgvpiryspeghlitlsqpREVREFEGQHHLLERAIRADFALIKGWK 214
Cdd:PRK09920  97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 58866010  215 ADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVI 270
Cdd:PRK09920 159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHII 214
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
303-497 4.39e-46

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: 160.06  E-value: 4.39e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    303 IIKRAALEFKDGMYANLGIG--IPVLASNYISPKMT----VYLHSENGILGLGPFPlkKEVDPDIINAGKQTVTVIPGGC 376
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILALIRQgpkdLTLISENGGLGLGLLA--GEGDVKKIIAGHVGLTPLLGRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    377 FFASD-DSFAMIRGGHIQLTMLGAMQVSKYGDLANWM-------VPGKKVK-GMGGAMDLVSSKKTKVVVTMEHCTKTK- 446
Cdd:smart00882  79 YFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADEFg 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 58866010    447 ---QPKILEKCTMPLTGKS-----CVDLIITEKAVFEVDRSKGlklveLWEGSSLDEVK 497
Cdd:smart00882 159 nlvYEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRL-----LIPGVLVDAVV 212
 
Name Accession Description Interval E-value
pcaJ_scoB_fam TIGR02428
3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the ...
300-506 6.07e-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: 322.70  E-value: 6.07e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   300 RTRIIKRAALEFKDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKKEVDPDIINAGKQTVTVIPGGCFFA 379
Cdd:TIGR02428   3 RDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASYFD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   380 SDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMVPGKKVKGMGGAMDLVSSKKtKVVVTMEHCTKTKQPKILEKCTMPLT 459
Cdd:TIGR02428  83 SADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLPLT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 58866010   460 GKSCVDLIITEKAVFEVDrSKGLKLVELWEGSSLDEVKATTGCSFKV 506
Cdd:TIGR02428 162 GAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
41-279 1.52e-92

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 281.59  E-value: 1.52e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010  41 KFYTDPVKAVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDdfGLGILLASKQVRRVVCSYL---G 117
Cdd:COG1788   3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYVggvG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 118 ENKLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGgvpiryspeghlitlsqpREVREFEGQHH 197
Cdd:COG1788  81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 198 LLERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVIKGPR--F 275
Cdd:COG1788 143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                ....
gi 58866010 276 EKRI 279
Cdd:COG1788 223 DKRI 226
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
300-514 1.39e-89

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 274.35  E-value: 1.39e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 300 RTRIIKRAALEFKDGMYANLGIGIPVLASNYI--SPKMTVYLHSENGILGLGPFPLKKEV-DPDIINAGKQtvtvipggc 376
Cdd:COG2057   5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPGSVgDPDLINAGKQ--------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 377 FFASDDSFAMIRGGHIQLTMLGAMQVSKYGDLANWMV-----PGKKVKGMGGAMDLVSSKKtKVVVTMEHCTKtkqpKIL 451
Cdd:COG2057  76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58866010 452 EKCTMpLTGKSCVD---LIITEKAVFEVDRSKGLKLVELWEGSSLDEVKATTGCSFKVCPNLKPMQ 514
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 6.23e-72

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: 228.49  E-value: 6.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    41 KFYTDPVKAVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDDFGLGILLASKQVRRVVCSY--LGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   119 NKLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGgvpiryspeghlitlsqpREVREFEGQHHL 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58866010   199 LERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 9.20e-62

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 201.76  E-value: 9.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    43 YTDPVKAVEG-IKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVddFGLGILLASKQVRRVVCSYLGE--N 119
Cdd:pfam01144   1 VESAAEAVAKeIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   120 KLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVP--AFYTPTGYGTQVQEGGvpiryspeghlitlsqprEVREFEGQHH 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK------------------RVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58866010   198 LLERAIRADFALIKGWKADRSGNVIFRGSARNFNVPMC-KAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVIKG 272
Cdd:pfam01144 141 LLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
49-270 9.14e-61

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: 198.97  E-value: 9.14e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010     49 AVEGIKDGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGvddFGLGILLASKQVRRVVCSYLGENKLCEQLYLA 128
Cdd:smart00882   5 AAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYFD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    129 GKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGGvpiryspeghlitlsQPREVREF-EGQHHLLERAIRADF 207
Cdd:smart00882  82 GEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRY---------------EGGKVRPFgMGGAYLLVPAIRPDV 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58866010    208 ALIKGWKADRSGNVIFRGSARNFNVP-MCKAADISVVEVEEIVDVGTFAPEDIH--IPNIYVKRVI 270
Cdd:smart00882 147 ALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
CoA_trans pfam01144
Coenzyme A transferase;
300-498 1.47e-55

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 185.58  E-value: 1.47e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   300 RTRIIKRAALEFKDGMYANLG----IGIPV-LASNYIS--PKMTVYLHSENGILGLGPFPLKKEVDPDIINAGKQTVTVI 372
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPEtLIAALARsgVKDLTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   373 PGGCFFASDDSFA-MIRGGHIQLTMLGAMQVSKYGDLANWMV-----PGKKVKGMGGAMDLVSSKKTKVVVTMEHCTKTK 446
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 58866010   447 QPKILEKCTMPLTGKSCVDL--IITEKAVFEVDR-SKGLKLVELWEGSSLDEVKA 498
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAAaaKVTILEVEEIVEkGELLPLTVHTPGVLVDAVVE 215
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-270 3.00e-50

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 171.47  E-value: 3.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010   55 DGASVMLGGFGLCGIPENLIGALKTKGVKDLKIISSNVGVDDFGLGILLASKQVRRVVCSYLGENKLCEQLYLAGKLELE 134
Cdd:PRK09920  17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010  135 MTPQGTLAERIRAGGTGVPAFYTPTGYGTQVQEGgvpiryspeghlitlsqpREVREFEGQHHLLERAIRADFALIKGWK 214
Cdd:PRK09920  97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 58866010  215 ADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHIPNIYVKRVI 270
Cdd:PRK09920 159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHII 214
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
303-497 4.39e-46

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: 160.06  E-value: 4.39e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    303 IIKRAALEFKDGMYANLGIG--IPVLASNYISPKMT----VYLHSENGILGLGPFPlkKEVDPDIINAGKQTVTVIPGGC 376
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILALIRQgpkdLTLISENGGLGLGLLA--GEGDVKKIIAGHVGLTPLLGRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010    377 FFASD-DSFAMIRGGHIQLTMLGAMQVSKYGDLANWM-------VPGKKVK-GMGGAMDLVSSKKTKVVVTMEHCTKTK- 446
Cdd:smart00882  79 YFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADEFg 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 58866010    447 ---QPKILEKCTMPLTGKS-----CVDLIITEKAVFEVDRSKGlklveLWEGSSLDEVK 497
Cdd:smart00882 159 nlvYEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRL-----LIPGVLVDAVV 212
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
40-486 2.62e-24

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 105.97  E-value: 2.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010  40 VKFYTdPVKAVEGIKDGASVMLGGFGLCGIPENLIGAL-----KTKGVKDLKIISSN-VGV-DDFGLGILLASKQVRRVV 112
Cdd:COG4670   1 SKIIS-AEEAAALIKDGDTVATSGFVGAGVPEELLKALeerflETGHPRDLTLIHAAgQGDgKGRGLDHLAHEGLVKRVI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 113 CSYLGENKLCEQLYLAGKLELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTQV---QEGG----------Vpiryspegh 179
Cdd:COG4670  80 GGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVdprLEGGklnerttedlV--------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 180 litlsqprEVREFEGQHHLLERAIRADFALIKGWKADRSGNVIF-RGSARNFNVPMCKAA------------DISVVeve 246
Cdd:COG4670 151 --------ELVEIDGEEYLFYKAFPIDVALIRGTTADEDGNLSMeHEALTLEVLAIAQAAknsggiviaqveRIVKR--- 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 247 eivdvGTFAPEDIHIPNIYVKRVIKGPR----------FEKRI---ERLTTRDSPPAPgskdQDPkRTRIIKRAALEFKD 313
Cdd:COG4670 220 -----GSLHPKDVKVPGILVDYVVVAPPedhmqtfstqYNPAYsgeIRVPLSSLPPLP----LDE-RKVIARRAAMELRP 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 314 GMYANLGIGIP-----VLASNYISPKMTvyLHSENGILGlGpFPLkkeVDPDI---INAgkqtvtvipgGCFFASDDSFA 385
Cdd:COG4670 290 GAVVNLGIGIPegvaaVAAEEGISDLIT--LTVESGPIG-G-VPA---GGLDFgaaVNA----------EAIIDQPDQFD 352
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 386 MIRGGHIQLTMLGAMQVSKYGDLaNwmVP--GKKVKGMGGAMDLVSS------------------------------KKT 433
Cdd:COG4670 353 FYDGGGLDIAFLGFAQVDRHGNV-N--VSkfGGRIAGCGGFINITQNakkvvfcgtftagglkvevedgklrilqegKIK 429
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58866010 434 KVVVTMEHCT-------KTKQPkilekctmpltgkscVdLIITEKAVFEVdRSKGLKLVE 486
Cdd:COG4670 430 KFVKKVEQITfsgkyarERGQE---------------V-LYVTERAVFEL-TPEGLELTE 472
 
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.
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