NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1026527348|gb|ANC98172|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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. ...
1-160 3.56e-132

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: 375.08  E-value: 3.56e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLK 80
Cdd:PRK05398   58 LYFTMLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMGFTWERIQEINPRLIVASIKGFGPGSPYEDVK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348  81 VYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNLCRVKLRDQQR 160
Cdd:PRK05398  138 AYENVAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQQR 217
 
Name Accession Description Interval E-value
PRK05398 PRK05398
formyl-coenzyme A transferase; Provisional
1-160 3.56e-132

formyl-coenzyme A transferase; Provisional


Pssm-ID: 180055  Cd Length: 416  Bit Score: 375.08  E-value: 3.56e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLK 80
Cdd:PRK05398   58 LYFTMLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMGFTWERIQEINPRLIVASIKGFGPGSPYEDVK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348  81 VYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNLCRVKLRDQQR 160
Cdd:PRK05398  138 AYENVAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQQR 217
oxalate_frc TIGR03253
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from ...
1-160 2.70e-110

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: 319.83  E-value: 2.70e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLK 80
Cdd:TIGR03253  57 LYFTMLNCNKRSITLNTKTPEGKEVLEELIKKADVMVENFGPGALDRMGFTWEYIQEINPRLILASIKGFGEGSPYENVK 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348  81 VYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNLCRVKLRDQQR 160
Cdd:TIGR03253 137 AYENVAQAAGGAASTTGFWDGPPLVSGAALGDSNTGMHLMIGILAALYQREHTGRGQRVTVAMQDAVLNLCRVKLRDQQR 216
CaiB COG1804
Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid ...
1-150 1.83e-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: 1.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFsdGHH--YED 78
Cdd:COG1804    59 AYFLSLNRNKRSITLDLKSPEGRELLRRLVARADVLVENFRPGVLERLGLGYEALRAINPRLIYCSISGF--GQTgpYAD 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1026527348  79 LKVYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNL 150
Cdd:COG1804   137 RPGYDLIAQAMSGLMSLTGEPDGPPVRVGVSVADIAAGLYAAIGILAALLHRERTGRGQVVDVSLLDAALAL 208
CoA_transf_3 pfam02515
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
1-151 3.38e-50

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: 164.32  E-value: 3.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLK 80
Cdd:pfam02515  53 AYFLSVNRNKRSVALDLKSEEGREVLRRLVARADVVIENFRPGVLERLGLGYEDLRAINPRLIYCSVSGYGQTGPYADRP 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1026527348  81 VYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNLC 151
Cdd:pfam02515 133 GYDLIAQAMSGLMSLTGEPGGPPVKVGTPVGDIVTGLLAAIAILAALLARERTGKGQVIDVSLLEAALALM 203
 
Name Accession Description Interval E-value
PRK05398 PRK05398
formyl-coenzyme A transferase; Provisional
1-160 3.56e-132

formyl-coenzyme A transferase; Provisional


Pssm-ID: 180055  Cd Length: 416  Bit Score: 375.08  E-value: 3.56e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLK 80
Cdd:PRK05398   58 LYFTMLNSNKRSITLDTKTPEGKEVLEKLIREADVLVENFGPGALDRMGFTWERIQEINPRLIVASIKGFGPGSPYEDVK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348  81 VYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNLCRVKLRDQQR 160
Cdd:PRK05398  138 AYENVAQCAGGAASTTGFWDGPPTVSGAALGDSNTGMHLAIGILAALLQREKTGRGQRVTVSMQDAVLNLCRVKLRDQQR 217
oxalate_frc TIGR03253
formyl-CoA transferase; This enzyme, formyl-CoA transferase, transfers coenzyme A from ...
1-160 2.70e-110

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: 319.83  E-value: 2.70e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLK 80
Cdd:TIGR03253  57 LYFTMLNCNKRSITLNTKTPEGKEVLEELIKKADVMVENFGPGALDRMGFTWEYIQEINPRLILASIKGFGEGSPYENVK 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348  81 VYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNLCRVKLRDQQR 160
Cdd:TIGR03253 137 AYENVAQAAGGAASTTGFWDGPPLVSGAALGDSNTGMHLMIGILAALYQREHTGRGQRVTVAMQDAVLNLCRVKLRDQQR 216
CaiB COG1804
Crotonobetainyl-CoA:carnitine CoA-transferase CaiB and related acyl-CoA transferases [Lipid ...
1-150 1.83e-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: 1.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFsdGHH--YED 78
Cdd:COG1804    59 AYFLSLNRNKRSITLDLKSPEGRELLRRLVARADVLVENFRPGVLERLGLGYEALRAINPRLIYCSISGF--GQTgpYAD 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1026527348  79 LKVYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNL 150
Cdd:COG1804   137 RPGYDLIAQAMSGLMSLTGEPDGPPVRVGVSVADIAAGLYAAIGILAALLHRERTGRGQVVDVSLLDAALAL 208
CoA_transf_3 pfam02515
CoA-transferase family III; CoA-transferases are found in organizms from all lines of descent. ...
1-151 3.38e-50

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: 164.32  E-value: 3.38e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLK 80
Cdd:pfam02515  53 AYFLSVNRNKRSVALDLKSEEGREVLRRLVARADVVIENFRPGVLERLGLGYEDLRAINPRLIYCSVSGYGQTGPYADRP 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1026527348  81 VYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNLC 151
Cdd:pfam02515 133 GYDLIAQAMSGLMSLTGEPGGPPVKVGTPVGDIVTGLLAAIAILAALLARERTGKGQVIDVSLLEAALALM 203
PRK11430 PRK11430
putative CoA-transferase; Provisional
1-148 4.23e-38

putative CoA-transferase; Provisional


Pssm-ID: 183132 [Multi-domain]  Cd Length: 381  Bit Score: 133.57  E-value: 4.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFSDGHHYEDLK 80
Cdd:PRK11430   62 LYYSFINHGKESVVLDLKNDHDKSIFINMLKQADVLAENFRPGTMEKLGFSWETLQEINPRLIYASSSGFGHTGPLKDAP 141
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1026527348  81 VYENVAQCAGGAASTSGFWDGPPTVSGAALGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVL 148
Cdd:PRK11430  142 AYDTIIQAMSGIMMETGYPDAPPVRVGTSLADLCGGVYLFSGIVSALYGREKSQRGAHVDIAMFDATL 209
PRK03525 PRK03525
L-carnitine CoA-transferase;
9-148 2.88e-16

L-carnitine CoA-transferase;


Pssm-ID: 179589  Cd Length: 405  Bit Score: 74.41  E-value: 2.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   9 NKRSLTLDTKTQEGKDVLTKLIKESDVMVENFGPGALDRMGFSWDNIQKINPGMILASVKGFsdGHH----YEDLKVYEN 84
Cdd:PRK03525   65 NLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWEHNPKLVIAHLSGF--GQYgteeYTNLPAYNT 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026527348  85 VAQCAGGAASTSGFWDGPPTVSGAAlGDSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVL 148
Cdd:PRK03525  143 IAQAFSGYLIQNGDVDQPMPAFPYT-ADYFSGLTATTAALAALHKARETGKGESIDIAMYEVML 205
mesacon_CoA_iso TIGR04253
mesaconyl-CoA isomerase; Members of this protein family belong by homology to the family of ...
1-150 1.19e-07

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: 49.96  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026527348   1 LYFTMLNSNKRSLTLDTKTQEGKDVLTKLI----KESDVMVENFgPGaldRMGFSWDNIQKINPGMILASVKGFSDGHHY 76
Cdd:TIGR04253  56 LFWAGLNKGKRSIAIDIRHPRGQELLTQLIcapgDHAGLFITNF-PA---KGWLAYDALKAHRADLIMVNLTGRRDGGSE 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1026527348  77 EDLKVYENVaqcagGAASTSGFWDGPPTVSGAALG-DSNTGMHLAIGILTALHAKNKTGKGQKVAVSMQDSVLNL 150
Cdd:TIGR04253 132 VDYTLNPQL-----GLPFMTGPTSSPDVVNHVFPAwDFISGQMIALGLLAAERHRRLTGEGQLVKIALKDVALAM 201
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH