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Conserved domains on  [gi|1026527390|gb|ANC98193|]
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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. ...
 1-154 4.81e-127

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: 361.98  E-value: 4.81e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKVYEN 80
Cdd:PRK05398   62 MLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMGFTWERIQEINPRLIVASIKGFGPGSPYEDVKAYEN 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527390  81 VAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINLCRVKLRDQ 154
Cdd:PRK05398  142 VAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQ 215
 
Name Accession Description Interval E-value
PRK05398 PRK05398
formyl-coenzyme A transferase; Provisional
 1-154 4.81e-127

formyl-coenzyme A transferase; Provisional


Pssm-ID: 180055  Cd Length: 416  Bit Score: 361.98  E-value: 4.81e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKVYEN 80
Cdd:PRK05398   62 MLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMGFTWERIQEINPRLIVASIKGFGPGSPYEDVKAYEN 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527390  81 VAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINLCRVKLRDQ 154
Cdd:PRK05398  142 VAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQ 215
oxalate_frc TIGR03253
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from ...
 1-154 3.97e-106

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: 308.66  E-value: 3.97e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKVYEN 80
Cdd:TIGR03253  61 MLNCNKRSITLNTKTPEGKEVLEELIKKADVMVENFGPGALDRMGFTWEYIQEINPRLILASIKGFGEGSPYENVKAYEN 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527390  81 VAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINLCRVKLRDQ 154
Cdd:TIGR03253 141 VAQAAGGAASTTGFWDGPPLVSGAALGDSNTGMHLMIGILAALYQREHTGRGQRVTVAMQDAVLNLCRVKLRDQ 214
CaiB COG1804
Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid ...
 1-146 1.45e-60

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


Pssm-ID: 441409  Cd Length: 397  Bit Score: 191.86  E-value: 1.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFsdGHH--YEDLKVY 78
Cdd:COG1804    63 SLNRNKRSITLDLKSPEGRELLRRLVARADVLVENFRPGVLERLGLGYEALRAINPRLIYCSISGF--GQTgpYADRPGY 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1026527390  79 ENVAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINL 146
Cdd:COG1804   141 DLIAQAMSGLMSLTGEPDGPPVRVGVSVADIAAGLYAAIGILAALLHRERTGRGQVVDVSLLDAALAL 208
CoA_transf_3 pfam02515
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
 1-147 1.36e-49

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: 162.77  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKVYEN 80
Cdd:pfam02515  57 SVNRNKRSVALDLKSEEGREVLRRLVARADVVIENFRPGVLERLGLGYEDLRAINPRLIYCSVSGYGQTGPYADRPGYDL 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1026527390  81 VAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINLC 147
Cdd:pfam02515 137 IAQAMSGLMSLTGEPGGPPVKVGTPVGDIVTGLLAAIAILAALLARERTGKGQVIDVSLLEAALALM 203
 
Name Accession Description Interval E-value
PRK05398 PRK05398
formyl-coenzyme A transferase; Provisional
 1-154 4.81e-127

formyl-coenzyme A transferase; Provisional


Pssm-ID: 180055  Cd Length: 416  Bit Score: 361.98  E-value: 4.81e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKVYEN 80
Cdd:PRK05398   62 MLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMGFTWERIQEINPRLIVASIKGFGPGSPYEDVKAYEN 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527390  81 VAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINLCRVKLRDQ 154
Cdd:PRK05398  142 VAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQ 215
oxalate_frc TIGR03253
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from ...
 1-154 3.97e-106

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: 308.66  E-value: 3.97e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKVYEN 80
Cdd:TIGR03253  61 MLNCNKRSITLNTKTPEGKEVLEELIKKADVMVENFGPGALDRMGFTWEYIQEINPRLILASIKGFGEGSPYENVKAYEN 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527390  81 VAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINLCRVKLRDQ 154
Cdd:TIGR03253 141 VAQAAGGAASTTGFWDGPPLVSGAALGDSNTGMHLMIGILAALYQREHTGRGQRVTVAMQDAVLNLCRVKLRDQ 214
CaiB COG1804
Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid ...
 1-146 1.45e-60

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


Pssm-ID: 441409  Cd Length: 397  Bit Score: 191.86  E-value: 1.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFsdGHH--YEDLKVY 78
Cdd:COG1804    63 SLNRNKRSITLDLKSPEGRELLRRLVARADVLVENFRPGVLERLGLGYEALRAINPRLIYCSISGF--GQTgpYADRPGY 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1026527390  79 ENVAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINL 146
Cdd:COG1804   141 DLIAQAMSGLMSLTGEPDGPPVRVGVSVADIAAGLYAAIGILAALLHRERTGRGQVVDVSLLDAALAL 208
CoA_transf_3 pfam02515
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
 1-147 1.36e-49

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: 162.77  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   1 MLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKVYEN 80
Cdd:pfam02515  57 SVNRNKRSVALDLKSEEGREVLRRLVARADVVIENFRPGVLERLGLGYEDLRAINPRLIYCSVSGYGQTGPYADRPGYDL 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1026527390  81 VAQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVINLC 147
Cdd:pfam02515 137 IAQAMSGLMSLTGEPGGPPVKVGTPVGDIVTGLLAAIAILAALLARERTGKGQVIDVSLLEAALALM 203
PRK11430 PRK11430
putative CoA-transferase; Provisional
 2-144 2.06e-34

putative CoA-transferase; Provisional


Pssm-ID: 183132 [Multi-domain]  Cd Length: 381  Bit Score: 123.56  E-value: 2.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   2 LNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKVYENV 81
Cdd:PRK11430   67 INHGKESVVLDLKNDHDKSIFINMLKQADVLAENFRPGTMEKLGFSWETLQEINPRLIYASSSGFGHTGPLKDAPAYDTI 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1026527390  82 AQCAGGAASTTGFWDGPPTVSAAALGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQDSVI 144
Cdd:PRK11430  147 IQAMSGIMMETGYPDAPPVRVGTSLADLCGGVYLFSGIVSALYGREKSQRGAHVDIAMFDATL 209
PRK03525 PRK03525
L-carnitine CoA-transferase;
5-139 5.66e-16

L-carnitine CoA-transferase;


Pssm-ID: 179589  Cd Length: 405  Bit Score: 73.64  E-value: 5.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   5 NKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFsdGHH----YEDLKVYEN 80
Cdd:PRK03525   65 NLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWEHNPKLVIAHLSGF--GQYgteeYTNLPAYNT 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1026527390  81 VAQCAGGAASTTGFWDGPPTVSAAAlGDSNTGMHLAIGILTALHHRNKTGKGQKVAVSM 139
Cdd:PRK03525  143 IAQAFSGYLIQNGDVDQPMPAFPYT-ADYFSGLTATTAALAALHKARETGKGESIDIAM 200
mesacon_CoA_iso TIGR04253
mesaconyl-CoA isomerase; Members of this protein family belong by homology to the family of ...
 2-141 1.90e-09

mesaconyl-CoA isomerase; Members of this protein family belong by homology to the family of CoA transferases. However, the characterized member from Chloroflexus aurantiacus appears to perform an intramolecular transfer, making it an isomerase. The enzyme converts mesaconyl-C1-CoA to mesaconyl-C4-CoA as part of the bicyclic 3-hydroxyproprionate pathway for carbon fixation.


Pssm-ID: 211976  Cd Length: 403  Bit Score: 54.97  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527390   2 LNSNKRSLTLDTKTQEGKDVLTKLI----KESDVMVENFgPGaldRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLKV 77
Cdd:TIGR04253  61 LNKGKRSIAIDIRHPRGQELLTQLIcapgDHAGLFITNF-PA---KGWLAYDALKAHRADLIMVNLTGRRDGGSEVDYTL 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1026527390  78 YENVaqcagGAASTTGFWDGPPTVSAAALG-DSNTGMHLAIGILTALHHRNKTGKGQKVAVSMQD 141
Cdd:TIGR04253 137 NPQL-----GLPFMTGPTSSPDVVNHVFPAwDFISGQMIALGLLAAERHRRLTGEGQLVKIALKD 196
 
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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