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Conserved domains on  [gi|446728378|ref|WP_000805691|]
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MULTISPECIES: acyl CoA:acetate/3-ketoacid CoA transferase [Enterobacteriaceae]

Protein Classification

acyl CoA:acetate/3-ketoacid CoA transferase( domain architecture ID 11468716)

acyl CoA:acetate/3-ketoacid CoA transferase similar to Escherichia coli acetate CoA-transferase YdiF, which has broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
13-523 0e+00

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


:

Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 808.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  13 VPVLSAQEAVNYIPDEATLCVLGAGGgILEATTLITALADKYKQTQTPRNLSIISPTGLGDRADRGISPLAQEGLVKWAL 92
Cdd:COG4670    1 SKIISAEEAAALIKDGDTVATSGFVG-AGVPEELLKALEERFLETGHPRDLTLIHAAGQGDGKGRGLDHLAHEGLVKRVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  93 CGHWGQSPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGKLNEVTKEDLIKLVEFDNKE 172
Cdd:COG4670   80 GGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVDPRLEGGKLNERTTEDLVELVEIDGEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 173 YLYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAVHNNGGIVMMQVQKMVKKATLHPKSVRIPGYLVDIVVV 252
Cdd:COG4670  160 YLFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLAIAQAAKNSGGIVIAQVERIVKRGSLHPKDVKVPGILVDYVVV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 253 DP--DQSQLYGGaPVNRFISGDFTLDDSTKLSLPLNQRKLVARRALFEMRKGAVGNVGVGIADGIGLVAREEGCADDFIL 330
Cdd:COG4670  240 APpeDHMQTFST-QYNPAYSGEIRVPLSSLPPLPLDERKVIARRAAMELRPGAVVNLGIGIPEGVAAVAAEEGISDLITL 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 331 TVETGPIGGITSQGIAFGANVNTRAILDMTSQFDFYHGGGLDVCYLSFAEVDQHGNVGVHKFNGKIMGTGGFIDISATSK 410
Cdd:COG4670  319 TVESGPIGGVPAGGLDFGAAVNAEAIIDQPDQFDFYDGGGLDIAFLGFAQVDRHGNVNVSKFGGRIAGCGGFINITQNAK 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 411 KIIFCGTLTAGSLKTEIADGKLHIVQEGRVNKFIRELPEITFSGKIALERGLDVRYITERAVFTLKEDGLHLIEIAPGVD 490
Cdd:COG4670  399 KVVFCGTFTAGGLKVEVEDGKLRILQEGKIKKFVKKVEQITFSGKYARERGQEVLYVTERAVFELTPEGLELTEIAPGID 478
                        490       500       510
                 ....*....|....*....|....*....|...
gi 446728378 491 LQKDILDKMDFTPVISPELKLMDERLFIDAAMG 523
Cdd:COG4670  479 LERDILAQMEFRPIIADDLKLMDARIFRDEPMG 511
 
Name Accession Description Interval E-value
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
13-523 0e+00

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 808.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  13 VPVLSAQEAVNYIPDEATLCVLGAGGgILEATTLITALADKYKQTQTPRNLSIISPTGLGDRADRGISPLAQEGLVKWAL 92
Cdd:COG4670    1 SKIISAEEAAALIKDGDTVATSGFVG-AGVPEELLKALEERFLETGHPRDLTLIHAAGQGDGKGRGLDHLAHEGLVKRVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  93 CGHWGQSPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGKLNEVTKEDLIKLVEFDNKE 172
Cdd:COG4670   80 GGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVDPRLEGGKLNERTTEDLVELVEIDGEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 173 YLYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAVHNNGGIVMMQVQKMVKKATLHPKSVRIPGYLVDIVVV 252
Cdd:COG4670  160 YLFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLAIAQAAKNSGGIVIAQVERIVKRGSLHPKDVKVPGILVDYVVV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 253 DP--DQSQLYGGaPVNRFISGDFTLDDSTKLSLPLNQRKLVARRALFEMRKGAVGNVGVGIADGIGLVAREEGCADDFIL 330
Cdd:COG4670  240 APpeDHMQTFST-QYNPAYSGEIRVPLSSLPPLPLDERKVIARRAAMELRPGAVVNLGIGIPEGVAAVAAEEGISDLITL 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 331 TVETGPIGGITSQGIAFGANVNTRAILDMTSQFDFYHGGGLDVCYLSFAEVDQHGNVGVHKFNGKIMGTGGFIDISATSK 410
Cdd:COG4670  319 TVESGPIGGVPAGGLDFGAAVNAEAIIDQPDQFDFYDGGGLDIAFLGFAQVDRHGNVNVSKFGGRIAGCGGFINITQNAK 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 411 KIIFCGTLTAGSLKTEIADGKLHIVQEGRVNKFIRELPEITFSGKIALERGLDVRYITERAVFTLKEDGLHLIEIAPGVD 490
Cdd:COG4670  399 KVVFCGTFTAGGLKVEVEDGKLRILQEGKIKKFVKKVEQITFSGKYARERGQEVLYVTERAVFELTPEGLELTEIAPGID 478
                        490       500       510
                 ....*....|....*....|....*....|...
gi 446728378 491 LQKDILDKMDFTPVISPELKLMDERLFIDAAMG 523
Cdd:COG4670  479 LERDILAQMEFRPIIADDLKLMDARIFRDEPMG 511
CoA_trans pfam01144
Coenzyme A transferase;
15-252 7.47e-48

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 165.17  E-value: 7.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378   15 VLSAQEAV-NYIPDEATLCVLGAGGGILeATTLITALADKYkqtqtPRNLSIISPTGlgdrADRGISPLAQEGLVKWALC 93
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGI-PETLIAALARSG-----VKDLTVISNEA----GVLGLGPLLLNGSVKKVIA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378   94 GHWGQ--SPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQP--GIISDIGIGTFVDPRqqggklnevtkedlIKLVEFD 169
Cdd:pfam01144  71 SYGGEtaNPEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPK--------------KRVPGFG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  170 NKEYLYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAvhnnGGIVMMQVQKMVKKATLHPKSVRIPGYLVDI 249
Cdd:pfam01144 137 GAMYLLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVAAA----AKVTILEVEEIVEKGELLPLTVHTPGVLVDA 212

                  ...
gi 446728378  250 VVV 252
Cdd:pfam01144 213 VVE 215
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
17-251 7.39e-47

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: 162.38  E-value: 7.39e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378    17 SAQEAVNYIPDEATLCVlGAGGGILEATTLITALADkykqtQTPRNLSIISPTGLGdradrGISPLAQEGLVKWALCGHW 96
Cdd:smart00882   1 SAAEAAREIKDGDTVAL-GGFGGLPTPAALILALIR-----QGPKDLTLISENGGL-----GLGLLAGEGDVKKIIAGHV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378    97 GQSPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGKLNEVTkedliklvefDNKEYLYY 176
Cdd:smart00882  70 GLTPLLGRLYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYEGGKVRPFG----------MGGAYLLV 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446728378   177 KAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAVHNNGGivmmQVQKMVKKATLHPKSVR--IPGYLVDIVV 251
Cdd:smart00882 140 PAIRPDVALIRAHTADEFGNLVYEKEATSCGLPLTAAAAKKVIV----QVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
17-251 5.78e-15

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: 74.03  E-value: 5.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378   17 SAQEAVNYIPDEATLCVlGAGGGILEATTLITALADkykqtQTPRNLSIISPT-GLGDRadrGISPLAQEGLVKWALCGH 95
Cdd:TIGR02429   8 SAAEAVSVIPDGATIMI-GGFGTAGQPFELIDALID-----TGAKDLTIVSNNaGNGEI---GLAALLKAGQVRKLICSF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378   96 WGQS-PRI-SELAEQNKIIAYNYPQGVLTQTLRAAAAhqpgiisdiGIGTFVDPRQQGGKLNEvTKEDLiklvEFDNKEY 173
Cdd:TIGR02429  79 PRQSdSYVfDELYRAGKIELELVPQGTLAERIRAAGA---------GLGAFFTPTGYGTLLAE-GKETR----EFDGKGY 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  174 LYYKAIAPDIAFIRATTCDSEGYATFEdevmyldalviaQAVHNNGGIVMM-------QVQKMVKKATLHPKSVRIPGYL 246
Cdd:TIGR02429 145 VLEYPLPADFALIKAHKADRWGNLTYR------------KAARNFGPIMAMaakttiaQVSQVVELGELDPEDVITPGIF 212

                  ....*
gi 446728378  247 VDIVV 251
Cdd:TIGR02429 213 VQRVV 217
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
15-252 2.18e-12

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 66.70  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  15 VLSAQEAVNYIPDEATLCVlGAGGGILEATTLITALADkykqtQTPRNLSIIS-PTGlgdRADRGISPLAQEGLVKWALC 93
Cdd:PRK09920   5 LMTLQDATGFFRDGMTIMV-GGFMGIGTPSRLVEALLE-----SGVRDLTLIAnDTA---FVDTGIGPLIVNGRVKKVIA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  94 GHWGQSPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQggklnevtkedlikLVEFDNKEY 173
Cdd:PRK09920  76 SHIGTNPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEGKQ--------------TLTLDGKTW 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446728378 174 LYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAvhnngGIVMMQVQKMVKKATLHPKSVRIPGYLVDIVVV 252
Cdd:PRK09920 142 LLERPLRADLALIRAHRADTLGNLTYQLSARNFNPLIALAA-----DITLVEPDELVETGELQPDHIVTPGAVIDHIIV 215
 
Name Accession Description Interval E-value
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
13-523 0e+00

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 808.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  13 VPVLSAQEAVNYIPDEATLCVLGAGGgILEATTLITALADKYKQTQTPRNLSIISPTGLGDRADRGISPLAQEGLVKWAL 92
Cdd:COG4670    1 SKIISAEEAAALIKDGDTVATSGFVG-AGVPEELLKALEERFLETGHPRDLTLIHAAGQGDGKGRGLDHLAHEGLVKRVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  93 CGHWGQSPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGKLNEVTKEDLIKLVEFDNKE 172
Cdd:COG4670   80 GGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVDPRLEGGKLNERTTEDLVELVEIDGEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 173 YLYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAVHNNGGIVMMQVQKMVKKATLHPKSVRIPGYLVDIVVV 252
Cdd:COG4670  160 YLFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLAIAQAAKNSGGIVIAQVERIVKRGSLHPKDVKVPGILVDYVVV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 253 DP--DQSQLYGGaPVNRFISGDFTLDDSTKLSLPLNQRKLVARRALFEMRKGAVGNVGVGIADGIGLVAREEGCADDFIL 330
Cdd:COG4670  240 APpeDHMQTFST-QYNPAYSGEIRVPLSSLPPLPLDERKVIARRAAMELRPGAVVNLGIGIPEGVAAVAAEEGISDLITL 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 331 TVETGPIGGITSQGIAFGANVNTRAILDMTSQFDFYHGGGLDVCYLSFAEVDQHGNVGVHKFNGKIMGTGGFIDISATSK 410
Cdd:COG4670  319 TVESGPIGGVPAGGLDFGAAVNAEAIIDQPDQFDFYDGGGLDIAFLGFAQVDRHGNVNVSKFGGRIAGCGGFINITQNAK 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 411 KIIFCGTLTAGSLKTEIADGKLHIVQEGRVNKFIRELPEITFSGKIALERGLDVRYITERAVFTLKEDGLHLIEIAPGVD 490
Cdd:COG4670  399 KVVFCGTFTAGGLKVEVEDGKLRILQEGKIKKFVKKVEQITFSGKYARERGQEVLYVTERAVFELTPEGLELTEIAPGID 478
                        490       500       510
                 ....*....|....*....|....*....|...
gi 446728378 491 LQKDILDKMDFTPVISPELKLMDERLFIDAAMG 523
Cdd:COG4670  479 LERDILAQMEFRPIIADDLKLMDARIFRDEPMG 511
CoA_trans pfam01144
Coenzyme A transferase;
15-252 7.47e-48

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 165.17  E-value: 7.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378   15 VLSAQEAV-NYIPDEATLCVLGAGGGILeATTLITALADKYkqtqtPRNLSIISPTGlgdrADRGISPLAQEGLVKWALC 93
Cdd:pfam01144   1 VESAAEAVaKEIKDGMTVNVGGFGLIGI-PETLIAALARSG-----VKDLTVISNEA----GVLGLGPLLLNGSVKKVIA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378   94 GHWGQ--SPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQP--GIISDIGIGTFVDPRqqggklnevtkedlIKLVEFD 169
Cdd:pfam01144  71 SYGGEtaNPEFGRQYFSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPK--------------KRVPGFG 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  170 NKEYLYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAvhnnGGIVMMQVQKMVKKATLHPKSVRIPGYLVDI 249
Cdd:pfam01144 137 GAMYLLEPALRADVALIKASKADGEGNLVFRTTAPNFNGPAVAAA----AKVTILEVEEIVEKGELLPLTVHTPGVLVDA 212

                  ...
gi 446728378  250 VVV 252
Cdd:pfam01144 213 VVE 215
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
17-251 7.39e-47

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: 162.38  E-value: 7.39e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378    17 SAQEAVNYIPDEATLCVlGAGGGILEATTLITALADkykqtQTPRNLSIISPTGLGdradrGISPLAQEGLVKWALCGHW 96
Cdd:smart00882   1 SAAEAAREIKDGDTVAL-GGFGGLPTPAALILALIR-----QGPKDLTLISENGGL-----GLGLLAGEGDVKKIIAGHV 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378    97 GQSPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGKLNEVTkedliklvefDNKEYLYY 176
Cdd:smart00882  70 GLTPLLGRLYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYEGGKVRPFG----------MGGAYLLV 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446728378   177 KAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAVHNNGGivmmQVQKMVKKATLHPKSVR--IPGYLVDIVV 251
Cdd:smart00882 140 PAIRPDVALIRAHTADEFGNLVYEKEATSCGLPLTAAAAKKVIV----QVEEIVDLGVLDPDPVRllIPGVLVDAVV 212
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
15-268 9.50e-27

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 107.86  E-value: 9.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  15 VLSAQEAVNYIPDEATLCVLGAGG-GILEAttLITALADkykqtQTPRNLSIISPTGLGDradrGISPLAQEGLVKWALC 93
Cdd:COG1788    5 VISLAEAVADVKDGMTIAIGGFGLcGIPMA--LIDELIR-----QGVKDLTLISNNAGVD----GLGLLIGAGQVKKVIA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  94 GHWGQ---SPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTfvdprqqggklnEVTKEDliKLVEFDN 170
Cdd:COG1788   74 SYVGGvglNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGT------------DVAEGK--ETREIDG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 171 KEYLYYKAIAPDIAFIRATTCDSEG------YATFEDEVMyldalviAQAvhnnGGIVMMQVQKMVKKATLHPKSVRIPG 244
Cdd:COG1788  140 EEYVLEPALRADVALIHAQKADRAGnlvyrgTARNFNPLM-------AMA----AKRVIVEVEEIVEVGELDPDAVVTPG 208
                        250       260
                 ....*....|....*....|....
gi 446728378 245 YLVDIVVVDPdqsqlyGGAPVNRF 268
Cdd:COG1788  209 IFVDAVVEVP------GGARDKRI 226
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
288-514 1.01e-15

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


Pssm-ID: 441660  Cd Length: 235  Bit Score: 76.74  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 288 RKLVARRALFEMRKGAVGNVGVGIADGIGLVAREEgCADDFILTVETGPIGgITSQGIAFGAN----VNTR-AILDMTSQ 362
Cdd:COG2057    5 RELMAVRAARELRDGEVVNLGIGLPTLAANLAPLT-HAPDVTLQSENGLLG-PGPAPLPGSVGdpdlINAGkQFFDSADS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378 363 FDFYHGGGLDVCYLSFAEVDQHGN-----VGVHKFNGKIM-GTGGFIDISATSKKIIFCGTLTAgslkteiadgklhivq 436
Cdd:COG2057   83 FAMIRGGHIDVGFLGAAQVDRYGNlnnwmIGDYDKPGKRLpGMGGAMDLAAGAKRVIVVMEHSK---------------- 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446728378 437 egrvNKFIRELPEITFSGKIaleRGLdVRYITERAVFTLKED-GLHLIEIAPGVDLQkDILDKMDFTPVISPELKLMDE 514
Cdd:COG2057  147 ----RKFVEKCDLLTGPGVV---DGP-RRVITDLAVFDFDPEkGLVLRELHPGVTVE-EVQENTGFELIVADDVPETPP 216
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
17-251 5.78e-15

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: 74.03  E-value: 5.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378   17 SAQEAVNYIPDEATLCVlGAGGGILEATTLITALADkykqtQTPRNLSIISPT-GLGDRadrGISPLAQEGLVKWALCGH 95
Cdd:TIGR02429   8 SAAEAVSVIPDGATIMI-GGFGTAGQPFELIDALID-----TGAKDLTIVSNNaGNGEI---GLAALLKAGQVRKLICSF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378   96 WGQS-PRI-SELAEQNKIIAYNYPQGVLTQTLRAAAAhqpgiisdiGIGTFVDPRQQGGKLNEvTKEDLiklvEFDNKEY 173
Cdd:TIGR02429  79 PRQSdSYVfDELYRAGKIELELVPQGTLAERIRAAGA---------GLGAFFTPTGYGTLLAE-GKETR----EFDGKGY 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  174 LYYKAIAPDIAFIRATTCDSEGYATFEdevmyldalviaQAVHNNGGIVMM-------QVQKMVKKATLHPKSVRIPGYL 246
Cdd:TIGR02429 145 VLEYPLPADFALIKAHKADRWGNLTYR------------KAARNFGPIMAMaakttiaQVSQVVELGELDPEDVITPGIF 212

                  ....*
gi 446728378  247 VDIVV 251
Cdd:TIGR02429 213 VQRVV 217
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
15-252 2.18e-12

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 66.70  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  15 VLSAQEAVNYIPDEATLCVlGAGGGILEATTLITALADkykqtQTPRNLSIIS-PTGlgdRADRGISPLAQEGLVKWALC 93
Cdd:PRK09920   5 LMTLQDATGFFRDGMTIMV-GGFMGIGTPSRLVEALLE-----SGVRDLTLIAnDTA---FVDTGIGPLIVNGRVKKVIA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446728378  94 GHWGQSPRISELAEQNKIIAYNYPQGVLTQTLRAAAAHQPGIISDIGIGTFVDPRQQggklnevtkedlikLVEFDNKEY 173
Cdd:PRK09920  76 SHIGTNPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEGKQ--------------TLTLDGKTW 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446728378 174 LYYKAIAPDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAvhnngGIVMMQVQKMVKKATLHPKSVRIPGYLVDIVVV 252
Cdd:PRK09920 142 LLERPLRADLALIRAHRADTLGNLTYQLSARNFNPLIALAA-----DITLVEPDELVETGELQPDHIVTPGAVIDHIIV 215
 
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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