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Conserved domains on  [gi|1401585371|ref|NP_001351231|]
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succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial isoform 5 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

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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 1.36e-114

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


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 337.06  E-value: 1.36e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDnfGLGLLLRSKQIKRMVSSY---VG 117
Cdd:COG1788     3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 118 ENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788    81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK--Y 275
Cdd:COG1788   143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                  ....
gi 1401585371 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 ...
300-478 1.74e-85

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: 261.84  E-value: 1.74e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 380 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGN-----------------------------AHKIMEKCTLPL 430
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKlvpgmggamdlvagakrvivamehttkdgESKILKECTLPL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1401585371 431 TGKQCVNRIITEKAVFDVDkKKGLTLIELWEGLTVDDVQKSTGCDFAV 478
Cdd:TIGR02428 161 TGAKCVDRIVTELAVFEVT-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 1.36e-114

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 337.06  E-value: 1.36e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDnfGLGLLLRSKQIKRMVSSY---VG 117
Cdd:COG1788     3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 118 ENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788    81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK--Y 275
Cdd:COG1788   143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                  ....
gi 1401585371 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 ...
300-478 1.74e-85

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: 261.84  E-value: 1.74e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 380 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGN-----------------------------AHKIMEKCTLPL 430
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKlvpgmggamdlvagakrvivamehttkdgESKILKECTLPL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1401585371 431 TGKQCVNRIITEKAVFDVDkKKGLTLIELWEGLTVDDVQKSTGCDFAV 478
Cdd:TIGR02428 161 TGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
41-270 6.03e-83

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: 255.84  E-value: 6.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSY--VGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 119 NAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFI 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1401585371 199 LEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 6.11e-81

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 250.30  E-value: 6.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  43 YTDPVEAV-KDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVdnFGLGLLLRSKQIKRMVSSYVGE--N 119
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 120 AEFERQYLSGELEVELTPQGTLAERIRAGGAGVP--AFYTPTGYGTLVQEGGspikynkdgsvaiaskprEVREFNGQHF 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK------------------RVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401585371 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 5.69e-76

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: 237.49  E-value: 5.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371   48 EAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGvdnFGLGLLLRSKQIKRMVSSYVGENAEFERQYL 127
Cdd:smart00882   4 EAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  128 SGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSpikynkdgsvaiaskPREVREFN-GQHFILEEAITGD 206
Cdd:smart00882  81 DGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYE---------------GGKVRPFGmGGAYLLVPAIRPD 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1401585371  207 FALVKAWKADRAGNVIFRKSARNFNLP-MCKAAETTVVEVEEIVDIGAFAPEDIH--IPQIYVHRLI 270
Cdd:smart00882 146 VALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
302-486 2.02e-71

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 226.58  E-value: 2.02e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 302 RERIIKRAALEFEDGMYANLGIGIPLLASNFI--SPNITVHLQSENGVLGLGPYPRQ-HEADADLINAGKEtvtilpgas 378
Cdd:COG2057     5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPgSVGDPDLINAGKQ--------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 379 FFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMI----------------PGNAH--------------KIMEKCTL 428
Cdd:COG2057    76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkpgkrlpgmggaMDLAAgakrvivvmehskrKFVEKCDL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401585371 429 pLTGKQCVN---RIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQ 486
Cdd:COG2057   156 -LTGPGVVDgprRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADDVPETP 215
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-274 1.38e-60

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 198.05  E-value: 1.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  55 DGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVE 134
Cdd:PRK09920   17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 135 LTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFILEEAITGDFALVKAWK 214
Cdd:PRK09920   97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 215 ADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK 274
Cdd:PRK09920  159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQE 218
CoA_trans pfam01144
Coenzyme A transferase;
302-471 5.74e-41

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 146.29  E-value: 5.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 302 RERIIKRAALEFEDGMYANLG----IGIP-LLASNFISPNIT--VHLQSENGVLGLGPYPRQHEADADLINAGKETVTIL 374
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 375 PGASFFSSDESFA-MIRGGHVDLTMLGAMQVSKYGDLANWMIP-----------------------------------GN 418
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIGtyvapkkrvpgfggamyllepalradvalikaskaDG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1401585371 419 AHKIMEKCTLPLTGKQCVN--RIITEKAVFDVD-KKKGLTLIELWEGLTVDDVQKS 471
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVeKGELLPLTVHTPGVLVDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
305-469 5.29e-33

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: 124.63  E-value: 5.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  305 IIKRAALEFEDGMYANLGIG--IPLLASNFIS------PNITvhLQSENGVLGLGPYPrqHEADADLINAGKETVTILPG 376
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILAlirqgpKDLT--LISENGGLGLGLLA--GEGDVKKIIAGHVGLTPLLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  377 ASFFSSD-ESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIP--------------------------------------- 416
Cdd:smart00882  77 RLYFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDvdpryeggkvrpfgmggayllvpairpdvalirahtade 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401585371  417 -GNA--HKIMEKCTLPLTGKQ-----CVNRIITEKAVFDVDKKKGLTlielwEGLTVDDVQ 469
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 1.36e-114

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 337.06  E-value: 1.36e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDnfGLGLLLRSKQIKRMVSSY---VG 117
Cdd:COG1788     3 KVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvggVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 118 ENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHF 197
Cdd:COG1788    81 LNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------KETREIDGEEY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 198 ILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK--Y 275
Cdd:COG1788   143 VLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGgaR 222

                  ....
gi 1401585371 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 ...
300-478 1.74e-85

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: 261.84  E-value: 1.74e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 300 DVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASF 379
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 380 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGN-----------------------------AHKIMEKCTLPL 430
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKlvpgmggamdlvagakrvivamehttkdgESKILKECTLPL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1401585371 431 TGKQCVNRIITEKAVFDVDkKKGLTLIELWEGLTVDDVQKSTGCDFAV 478
Cdd:TIGR02428 161 TGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
41-270 6.03e-83

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: 255.84  E-value: 6.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  41 KFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSY--VGE 118
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 119 NAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFI 198
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREFDGKGYV 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1401585371 199 LEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLI 270
Cdd:TIGR02429 146 LEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
43-272 6.11e-81

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 250.30  E-value: 6.11e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  43 YTDPVEAV-KDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVdnFGLGLLLRSKQIKRMVSSYVGE--N 119
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 120 AEFERQYLSGELEVELTPQGTLAERIRAGGAGVP--AFYTPTGYGTLVQEGGspikynkdgsvaiaskprEVREFNGQHF 197
Cdd:pfam01144  79 PEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK------------------RVPGFGGAMY 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401585371 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 5.69e-76

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: 237.49  E-value: 5.69e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371   48 EAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGvdnFGLGLLLRSKQIKRMVSSYVGENAEFERQYL 127
Cdd:smart00882   4 EAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  128 SGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSpikynkdgsvaiaskPREVREFN-GQHFILEEAITGD 206
Cdd:smart00882  81 DGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYE---------------GGKVRPFGmGGAYLLVPAIRPD 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1401585371  207 FALVKAWKADRAGNVIFRKSARNFNLP-MCKAAETTVVEVEEIVDIGAFAPEDIH--IPQIYVHRLI 270
Cdd:smart00882 146 VALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
302-486 2.02e-71

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 226.58  E-value: 2.02e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 302 RERIIKRAALEFEDGMYANLGIGIPLLASNFI--SPNITVHLQSENGVLGLGPYPRQ-HEADADLINAGKEtvtilpgas 378
Cdd:COG2057     5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPgSVGDPDLINAGKQ--------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 379 FFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMI----------------PGNAH--------------KIMEKCTL 428
Cdd:COG2057    76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkpgkrlpgmggaMDLAAgakrvivvmehskrKFVEKCDL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401585371 429 pLTGKQCVN---RIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQ 486
Cdd:COG2057   156 -LTGPGVVDgprRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADDVPETP 215
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
55-274 1.38e-60

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 198.05  E-value: 1.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  55 DGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVE 134
Cdd:PRK09920   17 DGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNPETGRRMISGEMDVE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 135 LTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGgspikynkdgsvaiaskpREVREFNGQHFILEEAITGDFALVKAWK 214
Cdd:PRK09920   97 LVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTLTLDGKTWLLERPLRADLALIRAHR 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 215 ADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEK 274
Cdd:PRK09920  159 ADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQE 218
CoA_trans pfam01144
Coenzyme A transferase;
302-471 5.74e-41

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 146.29  E-value: 5.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 302 RERIIKRAALEFEDGMYANLG----IGIP-LLASNFISPNIT--VHLQSENGVLGLGPYPRQHEADADLINAGKETVTIL 374
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 375 PGASFFSSDESFA-MIRGGHVDLTMLGAMQVSKYGDLANWMIP-----------------------------------GN 418
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIGtyvapkkrvpgfggamyllepalradvalikaskaDG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1401585371 419 AHKIMEKCTLPLTGKQCVN--RIITEKAVFDVD-KKKGLTLIELWEGLTVDDVQKS 471
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVeKGELLPLTVHTPGVLVDAVVEA 216
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
41-409 1.33e-33

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 132.93  E-value: 1.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  41 KFYTdPVEAVKDIPDGATVLVGGFGLCGIPENLIDAL----LKTGV-KGLTAVSNNA-------GVDNFGL-GLllrskq 107
Cdd:COG4670     2 KIIS-AEEAAALIKDGDTVATSGFVGAGVPEELLKALeerfLETGHpRDLTLIHAAGqgdgkgrGLDHLAHeGL------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 108 IKRMVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLV---QEGGspiKYNkdgsvAIAS 184
Cdd:COG4670    75 VKRVIGGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVdprLEGG---KLN-----ERTT 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 185 KPR-EVREFNGQHFILEEAITGDFALVKAWKADRAGNVIF-RKSARNFNLPMCKAAE----TTVVEVEEIVDIGAFAPED 258
Cdd:COG4670   147 EDLvELVEIDGEEYLFYKAFPIDVALIRGTTADEDGNLSMeHEALTLEVLAIAQAAKnsggIVIAQVERIVKRGSLHPKD 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 259 IHIPQIYV----------HRLIKGEKYEKRIErlsirkegdGEAK-----SAKPGDDVRERIIKRAALEFEDGMYANLGI 323
Cdd:COG4670   227 VKVPGILVdyvvvappedHMQTFSTQYNPAYS---------GEIRvplssLPPLPLDERKVIARRAAMELRPGAVVNLGI 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371 324 GIPLLASNF-----ISPNITvhLQSENGVLGlGpyprqheadadlinagketvTILPGASFFSSDESFAMIR-------- 390
Cdd:COG4670   298 GIPEGVAAVaaeegISDLIT--LTVESGPIG-G--------------------VPAGGLDFGAAVNAEAIIDqpdqfdfy 354
                         410       420
                  ....*....|....*....|
gi 1401585371 391 -GGHVDLTMLGAMQVSKYGD 409
Cdd:COG4670   355 dGGGLDIAFLGFAQVDRHGN 374
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
305-469 5.29e-33

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: 124.63  E-value: 5.29e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  305 IIKRAALEFEDGMYANLGIG--IPLLASNFIS------PNITvhLQSENGVLGLGPYPrqHEADADLINAGKETVTILPG 376
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILAlirqgpKDLT--LISENGGLGLGLLA--GEGDVKKIIAGHVGLTPLLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401585371  377 ASFFSSD-ESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIP--------------------------------------- 416
Cdd:smart00882  77 RLYFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDvdpryeggkvrpfgmggayllvpairpdvalirahtade 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401585371  417 -GNA--HKIMEKCTLPLTGKQ-----CVNRIITEKAVFDVDKKKGLTlielwEGLTVDDVQ 469
Cdd:smart00882 157 fGNLvyEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRLLI-----PGVLVDAVV 212
 
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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