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Conserved domains on  [gi|2024431117|ref|XP_040511456|]
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succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial isoform X1 [Gallus gallus]

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 ...
189-397 6.79e-110

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: 321.16  E-value: 6.79e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 189 NVRERIIRRAALEFEDGMYANLGIGIPLLASNFISPDITVHLQSENGVLGLGPYPLESEVDPDLINAGKETVTVLPGSSY 268
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 269 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAQtKVVVTMEHSAKGNVHKILEKCNLP 348
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2024431117 349 LTGKQCVNRIITEKAVFDVDkKKGLTLVEIWEGLSVDDIKKSTGCDFAV 397
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
1-169 6.92e-76

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


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 234.98  E-value: 6.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   1 MVSSY---VGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGgapikynsdgtiaiasqpR 77
Cdd:COG1788    71 VIASYvggVGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------K 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  78 EVREFDGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMCKAAKTTVVEVEEIVDIGAFAPEDIHVPKIYVD 157
Cdd:COG1788   133 ETREIDGEEYVLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVD 212
                         170
                  ....*....|....
gi 2024431117 158 RLIQGEK--FEKRI 169
Cdd:COG1788   213 AVVEVPGgaRDKRI 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 ...
189-397 6.79e-110

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: 321.16  E-value: 6.79e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 189 NVRERIIRRAALEFEDGMYANLGIGIPLLASNFISPDITVHLQSENGVLGLGPYPLESEVDPDLINAGKETVTVLPGSSY 268
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 269 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAQtKVVVTMEHSAKGNVHKILEKCNLP 348
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2024431117 349 LTGKQCVNRIITEKAVFDVDkKKGLTLVEIWEGLSVDDIKKSTGCDFAV 397
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
191-405 3.12e-96

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 287.44  E-value: 3.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 191 RERIIRRAALEFEDGMYANLGIGIPLLASNFI--SPDITVHLQSENGVLGLGPYPLE-SEVDPDLINAGKEtvtvlpgss 267
Cdd:COG2057     5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPgSVGDPDLINAGKQ--------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 268 YFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAQtKVVVTMEHSAKgnvhKIL 342
Cdd:COG2057    76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024431117 343 EKCNLpLTGKQCVN---RIITEKAVFDVDKKKGLTLVEIWEGLSVDDIKKSTGCDFAVSPKLIPMR 405
Cdd:COG2057   151 EKCDL-LTGPGVVDgprRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADDVPETP 215
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
1-169 6.92e-76

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 234.98  E-value: 6.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   1 MVSSY---VGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGgapikynsdgtiaiasqpR 77
Cdd:COG1788    71 VIASYvggVGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------K 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  78 EVREFDGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMCKAAKTTVVEVEEIVDIGAFAPEDIHVPKIYVD 157
Cdd:COG1788   133 ETREIDGEEYVLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVD 212
                         170
                  ....*....|....
gi 2024431117 158 RLIQGEK--FEKRI 169
Cdd:COG1788   213 AVVEVPGgaRDKRI 226
CoA_trans pfam01144
Coenzyme A transferase;
191-390 8.94e-59

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 190.59  E-value: 8.94e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 191 RERIIRRAALEFEDGMYANLG----IGIP-LLASNFISPDIT--VHLQSENGVLGLGPYPLESEVDPDLINAGKETVTVL 263
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 264 PGSSYFSSDESFA-MIRGGHVDLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAQTKVVVTMEHSAKGN 337
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024431117 338 VHKILEKCNLPLTGKQCVN--RIITEKAVFDVD-KKKGLTLVEIWEGLSVDDIKKS 390
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVeKGELLPLTVHTPGVLVDAVVEA 216
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
3-160 3.70e-54

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: 179.19  E-value: 3.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   3 SSYVgenaeFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGgapikynsdgtiaiasqpREVREF 82
Cdd:TIGR02429  83 DSYV-----FDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREF 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024431117  83 DGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMCKAAKTTVVEVEEIVDIGAFAPEDIHVPKIYVDRLI 160
Cdd:TIGR02429 140 DGKGYVLEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
1-162 2.26e-51

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 171.71  E-value: 2.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   1 MVSSYVGE--NAEFERQYLSGELEVELTPQGTLAERIRAGGAGIP--AFYTSTGYGTLVQEGGapikynsdgtiaiasqp 76
Cdd:pfam01144  68 VIASYGGEtaNPEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK----------------- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  77 rEVREFDGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMC-KAAKTTVVEVEEIVDIGAFAPEDIHVPKIY 155
Cdd:pfam01144 131 -RVPGFGGAMYLLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVL 209

                  ....*..
gi 2024431117 156 VDRLIQG 162
Cdd:pfam01144 210 VDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
194-388 2.38e-51

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: 2.38e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  194 IIRRAALEFEDGMYANLGIG--IPLLASNFISPDIT----VHLQSENGVLGLGPYPleSEVDPDLINAGKETVTVLPGSS 267
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILALIRQgpkdLTLISENGGLGLGLLA--GEGDVKKIIAGHVGLTPLLGRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  268 YFSSD-ESFAMIRGGHVDLTMLGAMQVSKYGDLANWM-------IPGKMVK-GMGGAMDLVSSAQTKVVVTMEHSAK--G 336
Cdd:smart00882  79 YFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADefG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024431117  337 NV--HKILEKCNLPLTGKQ-----CVNRIITEKAVFDVDKKKGLTlveiwEGLSVDDIK 388
Cdd:smart00882 159 NLvyEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRLLI-----PGVLVDAVV 212
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
1-160 4.17e-49

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: 165.46  E-value: 4.17e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117    1 MVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGGapikynsdgtiaiasQPREVR 80
Cdd:smart00882  64 IIAGHVGLTPLLGRLYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRY---------------EGGKVR 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   81 EF-DGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQP-MCKAAKTTVVEVEEIVDIGAFAPEDIH--VPKIYV 156
Cdd:smart00882 129 PFgMGGAYLLVPAIRPDVALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLV 208

                   ....
gi 2024431117  157 DRLI 160
Cdd:smart00882 209 DAVV 212
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
1-164 4.26e-42

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 147.59  E-value: 4.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   1 MVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGgapikynsdgtiaiasqpREVR 80
Cdd:PRK09920   73 VIASHIGTNPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  81 EFDGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMCKAAKTTVVEVEEIVDIGAFAPEDIHVPKIYVDRLI 160
Cdd:PRK09920  135 TLDGKTWLLERPLRADLALIRAHRADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHII 214

                  ....
gi 2024431117 161 QGEK 164
Cdd:PRK09920  215 VSQE 218
 
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 ...
189-397 6.79e-110

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: 321.16  E-value: 6.79e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 189 NVRERIIRRAALEFEDGMYANLGIGIPLLASNFISPDITVHLQSENGVLGLGPYPLESEVDPDLINAGKETVTVLPGSSY 268
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEPGEEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 269 FSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAQtKVVVTMEHSAKGNVHKILEKCNLP 348
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAK-RVIVAMEHTTKDGESKILKECTLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2024431117 349 LTGKQCVNRIITEKAVFDVDkKKGLTLVEIWEGLSVDDIKKSTGCDFAV 397
Cdd:TIGR02428 160 LTGAKCVDRIVTELAVFEVT-DGGLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
191-405 3.12e-96

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 287.44  E-value: 3.12e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 191 RERIIRRAALEFEDGMYANLGIGIPLLASNFI--SPDITVHLQSENGVLGLGPYPLE-SEVDPDLINAGKEtvtvlpgss 267
Cdd:COG2057     5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAplTHAPDVTLQSENGLLGPGPAPLPgSVGDPDLINAGKQ--------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 268 YFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAQtKVVVTMEHSAKgnvhKIL 342
Cdd:COG2057    76 FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAK-RVIVVMEHSKR----KFV 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024431117 343 EKCNLpLTGKQCVN---RIITEKAVFDVDKKKGLTLVEIWEGLSVDDIKKSTGCDFAVSPKLIPMR 405
Cdd:COG2057   151 EKCDL-LTGPGVVDgprRVITDLAVFDFDPEKGLVLRELHPGVTVEEVQENTGFELIVADDVPETP 215
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
1-169 6.92e-76

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 234.98  E-value: 6.92e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   1 MVSSY---VGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGgapikynsdgtiaiasqpR 77
Cdd:COG1788    71 VIASYvggVGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEG------------------K 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  78 EVREFDGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMCKAAKTTVVEVEEIVDIGAFAPEDIHVPKIYVD 157
Cdd:COG1788   133 ETREIDGEEYVLEPALRADVALIHAQKADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVD 212
                         170
                  ....*....|....
gi 2024431117 158 RLIQGEK--FEKRI 169
Cdd:COG1788   213 AVVEVPGgaRDKRI 226
CoA_trans pfam01144
Coenzyme A transferase;
191-390 8.94e-59

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 190.59  E-value: 8.94e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 191 RERIIRRAALEFEDGMYANLG----IGIP-LLASNFISPDIT--VHLQSENGVLGLGPYPLESEVDPDLINAGKETVTVL 263
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVKdlTVISNEAGVLGLGPLLLNGSVKKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 264 PGSSYFSSDESFA-MIRGGHVDLTMLGAMQVSKYGDLANWMI-----PGKMVKGMGGAMDLVSSAQTKVVVTMEHSAKGN 337
Cdd:pfam01144  81 FGRQYFSGELEFElWPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPALRADVALIKASKADG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024431117 338 VHKILEKCNLPLTGKQCVN--RIITEKAVFDVD-KKKGLTLVEIWEGLSVDDIKKS 390
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAaaAKVTILEVEEIVeKGELLPLTVHTPGVLVDAVVEA 216
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
3-160 3.70e-54

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: 179.19  E-value: 3.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   3 SSYVgenaeFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGgapikynsdgtiaiasqpREVREF 82
Cdd:TIGR02429  83 DSYV-----FDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEG------------------KETREF 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024431117  83 DGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMCKAAKTTVVEVEEIVDIGAFAPEDIHVPKIYVDRLI 160
Cdd:TIGR02429 140 DGKGYVLEYPLPADFALIKAHKADRWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVV 217
CoA_trans pfam01144
Coenzyme A transferase;
1-162 2.26e-51

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 171.71  E-value: 2.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   1 MVSSYVGE--NAEFERQYLSGELEVELTPQGTLAERIRAGGAGIP--AFYTSTGYGTLVQEGGapikynsdgtiaiasqp 76
Cdd:pfam01144  68 VIASYGGEtaNPEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKK----------------- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  77 rEVREFDGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMC-KAAKTTVVEVEEIVDIGAFAPEDIHVPKIY 155
Cdd:pfam01144 131 -RVPGFGGAMYLLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVaAAAKVTILEVEEIVEKGELLPLTVHTPGVL 209

                  ....*..
gi 2024431117 156 VDRLIQG 162
Cdd:pfam01144 210 VDAVVEA 216
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
194-388 2.38e-51

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: 2.38e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  194 IIRRAALEFEDGMYANLGIG--IPLLASNFISPDIT----VHLQSENGVLGLGPYPleSEVDPDLINAGKETVTVLPGSS 267
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFggLPTPAALILALIRQgpkdLTLISENGGLGLGLLA--GEGDVKKIIAGHVGLTPLLGRL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  268 YFSSD-ESFAMIRGGHVDLTMLGAMQVSKYGDLANWM-------IPGKMVK-GMGGAMDLVSSAQTKVVVTMEHSAK--G 336
Cdd:smart00882  79 YFDGEiESFLLPQGGLADRLRAGAAGVPGFGTLAGLGtdvdpryEGGKVRPfGMGGAYLLVPAIRPDVALIRAHTADefG 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024431117  337 NV--HKILEKCNLPLTGKQ-----CVNRIITEKAVFDVDKKKGLTlveiwEGLSVDDIK 388
Cdd:smart00882 159 NLvyEKEATSCGLPLTAAAakkviVQVEEIVDLGVLDPDPVRLLI-----PGVLVDAVV 212
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
1-160 4.17e-49

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: 165.46  E-value: 4.17e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117    1 MVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGGapikynsdgtiaiasQPREVR 80
Cdd:smart00882  64 IIAGHVGLTPLLGRLYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRY---------------EGGKVR 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   81 EF-DGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQP-MCKAAKTTVVEVEEIVDIGAFAPEDIH--VPKIYV 156
Cdd:smart00882 129 PFgMGGAYLLVPAIRPDVALIRAHTADEFGNLVYEKEATSCGLPlTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLV 208

                   ....
gi 2024431117  157 DRLI 160
Cdd:smart00882 209 DAVV 212
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
1-164 4.26e-42

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 147.59  E-value: 4.26e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117   1 MVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGIPAFYTSTGYGTLVQEGgapikynsdgtiaiasqpREVR 80
Cdd:PRK09920   73 VIASHIGTNPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEG------------------KQTL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  81 EFDGRHFILEKSITGDFALVKAWKADRAGNIIFRKTARNFNQPMCKAAKTTVVEVEEIVDIGAFAPEDIHVPKIYVDRLI 160
Cdd:PRK09920  135 TLDGKTWLLERPLRADLALIRAHRADTLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHII 214

                  ....
gi 2024431117 161 QGEK 164
Cdd:PRK09920  215 VSQE 218
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
27-404 8.63e-27

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 111.74  E-value: 8.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117  27 PQGTLAERIRAGGAGIPAFYTSTGYGTLV---QEGGapiKYNsdgtiAIASQPR-EVREFDGRHFILEKSITGDFALVKA 102
Cdd:COG4670   104 PQGVISHLFREIAAGRPGVLTKVGLGTFVdprLEGG---KLN-----ERTTEDLvELVEIDGEEYLFYKAFPIDVALIRG 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 103 WKADRAGNIIFRKTARNFNQ-PMCKAAK----TTVVEVEEIVDIGAFAPEDIHVPKIYVDRLIQGEKFEKRI-------E 170
Cdd:COG4670   176 TTADEDGNLSMEHEALTLEVlAIAQAAKnsggIVIAQVERIVKRGSLHPKDVKVPGILVDYVVVAPPEDHMQtfstqynP 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 171 RLS--IRKPEDSKAKQKPgdNVRERIIRRAALEFEDGMYANLGIGIPLLASNF-----ISPDITvhLQSENGVLGlGpYP 243
Cdd:COG4670   256 AYSgeIRVPLSSLPPLPL--DERKVIARRAAMELRPGAVVNLGIGIPEGVAAVaaeegISDLIT--LTVESGPIG-G-VP 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 244 LEsevDPDL---INAgketvtvlpgSSYFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVkGMGGAMDLVS 320
Cdd:COG4670   330 AG---GLDFgaaVNA----------EAIIDQPDQFDFYDGGGLDIAFLGFAQVDRHGNVNVSKFGGRIA-GCGGFINITQ 395
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024431117 321 SAQT-------------------KVVVTMEhsakGNVHKILEK-----CNLPL---TGKQCVnrIITEKAVFDVdKKKGL 373
Cdd:COG4670   396 NAKKvvfcgtftagglkvevedgKLRILQE----GKIKKFVKKveqitFSGKYareRGQEVL--YVTERAVFEL-TPEGL 468
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2024431117 374 TLVEIWEGLSVD-DI--KkstgCDF--AVSPKLIPM 404
Cdd:COG4670   469 ELTEIAPGIDLErDIlaQ----MEFrpIIADDLKLM 500
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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