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Conserved domains on  [gi|1026527368|gb|ANC98182|]
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formyl-coenzyme A transferase, partial [uncultured Hyphomicrobiales bacterium]

Protein Classification

CoA transferase family protein( domain architecture ID 139588)

CoA transferase belonging to the CaiB family catalyzes the reversible transfer of the CoA moiety from a fatty acid CoA ester to a fatty acid acceptor, might also act as an acyl-CoA racemase

EC:  2.-.-.-
Gene Ontology:  GO:0016740
PubMed:  11749953
SCOP:  4000567

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CoA_transf_3 super family cl19215
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
 1-152 3.45e-117

CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.


The actual alignment was detected with superfamily member PRK05398:

Pssm-ID: 450273  Cd Length: 416  Bit Score: 336.94  E-value: 3.45e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGPG-PYADCKVYEN 78
Cdd:PRK05398   62 MLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMgFTWERIQEINPRLIVASIKGFGPGsPYEDVKAYEN 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNLARVKLRDQ 152
Cdd:PRK05398  142 VAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQ 215
 
Name Accession Description Interval E-value
PRK05398 PRK05398
formyl-coenzyme A transferase; Provisional
 1-152 3.45e-117

formyl-coenzyme A transferase; Provisional


Pssm-ID: 180055  Cd Length: 416  Bit Score: 336.94  E-value: 3.45e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGPG-PYADCKVYEN 78
Cdd:PRK05398   62 MLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMgFTWERIQEINPRLIVASIKGFGPGsPYEDVKAYEN 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNLARVKLRDQ 152
Cdd:PRK05398  142 VAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQ 215
oxalate_frc TIGR03253
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from ...
 1-152 1.07e-99

formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from formyl-CoA to oxalate. It forms a pathway, together with oxalyl-CoA decarboxylase, for oxalate degradation; decarboxylation by the latter gene regenerates formyl-CoA. The two enzymes typically are encoded by a two-gene operon. [Cellular processes, Detoxification]


Pssm-ID: 211800  Cd Length: 415  Bit Score: 292.49  E-value: 1.07e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGPG-PYADCKVYEN 78
Cdd:TIGR03253  61 MLNCNKRSITLNTKTPEGKEVLEELIKKADVMVENFGPGALDRMgFTWEYIQEINPRLILASIKGFGEGsPYENVKAYEN 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNLARVKLRDQ 152
Cdd:TIGR03253 141 VAQAAGGAASTTGFWDGPPLVSGAALGDSNTGMHLMIGILAALYQREHTGRGQRVTVAMQDAVLNLCRVKLRDQ 214
CaiB COG1804
Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid ...
 1-144 2.92e-62

Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid transport and metabolism];


Pssm-ID: 441409  Cd Length: 397  Bit Score: 196.10  E-value: 2.92e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGP-GPYADCKVYEN 78
Cdd:COG1804    63 SLNRNKRSITLDLKSPEGRELLRRLVARADVLVENFRPGVLERLgLGYEALRAINPRLIYCSISGFGQtGPYADRPGYDL 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNL 144
Cdd:COG1804   143 IAQAMSGLMSLTGEPDGPPVRVGVSVADIAAGLYAAIGILAALLHRERTGRGQVVDVSLLDAALAL 208
CoA_transf_3 pfam02515
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
 1-144 1.38e-51

CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.


Pssm-ID: 426810 [Multi-domain]  Cd Length: 367  Bit Score: 167.78  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGP-GPYADCKVYEN 78
Cdd:pfam02515  57 SVNRNKRSVALDLKSEEGREVLRRLVARADVVIENFRPGVLERLgLGYEDLRAINPRLIYCSVSGYGQtGPYADRPGYDL 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNL 144
Cdd:pfam02515 137 IAQAMSGLMSLTGEPGGPPVKVGTPVGDIVTGLLAAIAILAALLARERTGKGQVIDVSLLEAALAL 202
 
Name Accession Description Interval E-value
PRK05398 PRK05398
formyl-coenzyme A transferase; Provisional
 1-152 3.45e-117

formyl-coenzyme A transferase; Provisional


Pssm-ID: 180055  Cd Length: 416  Bit Score: 336.94  E-value: 3.45e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGPG-PYADCKVYEN 78
Cdd:PRK05398   62 MLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMgFTWERIQEINPRLIVASIKGFGPGsPYEDVKAYEN 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNLARVKLRDQ 152
Cdd:PRK05398  142 VAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQ 215
oxalate_frc TIGR03253
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from ...
 1-152 1.07e-99

formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from formyl-CoA to oxalate. It forms a pathway, together with oxalyl-CoA decarboxylase, for oxalate degradation; decarboxylation by the latter gene regenerates formyl-CoA. The two enzymes typically are encoded by a two-gene operon. [Cellular processes, Detoxification]


Pssm-ID: 211800  Cd Length: 415  Bit Score: 292.49  E-value: 1.07e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGPG-PYADCKVYEN 78
Cdd:TIGR03253  61 MLNCNKRSITLNTKTPEGKEVLEELIKKADVMVENFGPGALDRMgFTWEYIQEINPRLILASIKGFGEGsPYENVKAYEN 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNLARVKLRDQ 152
Cdd:TIGR03253 141 VAQAAGGAASTTGFWDGPPLVSGAALGDSNTGMHLMIGILAALYQREHTGRGQRVTVAMQDAVLNLCRVKLRDQ 214
CaiB COG1804
Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid ...
 1-144 2.92e-62

Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid transport and metabolism];


Pssm-ID: 441409  Cd Length: 397  Bit Score: 196.10  E-value: 2.92e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGP-GPYADCKVYEN 78
Cdd:COG1804    63 SLNRNKRSITLDLKSPEGRELLRRLVARADVLVENFRPGVLERLgLGYEALRAINPRLIYCSISGFGQtGPYADRPGYDL 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNL 144
Cdd:COG1804   143 IAQAMSGLMSLTGEPDGPPVRVGVSVADIAAGLYAAIGILAALLHRERTGRGQVVDVSLLDAALAL 208
CoA_transf_3 pfam02515
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
 1-144 1.38e-51

CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.


Pssm-ID: 426810 [Multi-domain]  Cd Length: 367  Bit Score: 167.78  E-value: 1.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   1 MLNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFGP-GPYADCKVYEN 78
Cdd:pfam02515  57 SVNRNKRSVALDLKSEEGREVLRRLVARADVVIENFRPGVLERLgLGYEDLRAINPRLIYCSVSGYGQtGPYADRPGYDL 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1026527368  79 VAQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVLNL 144
Cdd:pfam02515 137 IAQAMSGLMSLTGEPGGPPVKVGTPVGDIVTGLLAAIAILAALLARERTGKGQVIDVSLLEAALAL 202
PRK11430 PRK11430
putative CoA-transferase; Provisional
 2-142 1.14e-37

putative CoA-transferase; Provisional


Pssm-ID: 183132 [Multi-domain]  Cd Length: 381  Bit Score: 132.03  E-value: 1.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   2 LNHNKRSITLDTKNPKGREVLEALVKTCDVLVENFAPGVLDRM-LPWARIQELNPRMIVASIKGFG-PGPYADCKVYENV 79
Cdd:PRK11430   67 INHGKESVVLDLKNDHDKSIFINMLKQADVLAENFRPGTMEKLgFSWETLQEINPRLIYASSSGFGhTGPLKDAPAYDTI 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1026527368  80 AQCAGGSASTTGFRDGLPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVL 142
Cdd:PRK11430  147 IQAMSGIMMETGYPDAPPVRVGTSLADLCGGVYLFSGIVSALYGREKSQRGAHVDIAMFDATL 209
PRK03525 PRK03525
L-carnitine CoA-transferase;
5-142 6.08e-13

L-carnitine CoA-transferase;


Pssm-ID: 179589  Cd Length: 405  Bit Score: 64.78  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527368   5 NKRSITLDTKNPKGREVLEALVKTCDVLVEN-----FA-PGVLDRMLpWariqELNPRMIVASIKGFG---PGPYADCKV 75
Cdd:PRK03525   65 NLHALSLNIFKDEGREAFLKLMETTDIFIEAskgpaFArRGITDEVL-W----EHNPKLVIAHLSGFGqygTEEYTNLPA 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1026527368  76 YENVAQCAGGSASTTGFRDGlPLVTGAQIGDSGTGLHLALGIVTALYQRTRTGRGQRVDCAMQDGVL 142
Cdd:PRK03525  140 YNTIAQAFSGYLIQNGDVDQ-PMPAFPYTADYFSGLTATTAALAALHKARETGKGESIDIAMYEVML 205
 
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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