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A5EGD7 (FCTA_BRASB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formyl-coenzyme A transferase

Short name=Formyl-CoA transferase
EC=2.8.3.16
Gene names
Name:frc
Ordered Locus Names:BBta_3113
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate By similarity. HAMAP MF_00742

Catalytic activity

Formyl-CoA + oxalate = formate + oxalyl-CoA. HAMAP MF_00742

Pathway

Metabolic intermediate degradation; oxalate degradation; CO(2) and formate from oxalate: step 1/2. HAMAP MF_00742

Sequence similarities

Belongs to the CaiB/BaiF CoA-transferase family.

Ontologies

Keywords
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionformyl-CoA transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Formyl-coenzyme A transferase HAMAP MF_00742
PRO_0000300985

Sites

Active site1681Nucleophile By similarity
Binding site961Coenzyme A By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EGD7 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 23FA62E1131A035F

FASTA42546,639
        10         20         30         40         50         60 
MTKALEGVRI LDFTHVQSGP TCTQLLAWFG ADVIKVERPG VGDITRGQLQ DIPNVDSLYF 

        70         80         90        100        110        120 
TMLNHNKRSI TLDTKNPKGK EVLTELIKKC DVLVENFGPG VLDRMGFPWE KIQAINPKMI 

       130        140        150        160        170        180 
VASIKGFGPG PYEDCKVYEN VAQCTGGAAS TTGFRDGLPL VTGAQIGDSG TGLHLALGIV 

       190        200        210        220        230        240 
TALYQRTHTG KGQRVTAAMQ DGVLNLCRVK LRDQQRLERG PLKEYSQFGE GVPFGDAVPR 

       250        260        270        280        290        300 
AGNDSGGGQP GRILKCKGWE TDPNAYIYFI TQAPVWEKIC DVIGEPTWKT DPNYAKPAAR 

       310        320        330        340        350        360 
LPRLNEIFGR IEQWTMTKTK FEAMDILNEF DIPCGPILSM KEIAEDESLR KTGTLVEVDH 

       370        380        390        400        410        420 
PTRGKYLSVG NPIKLSDSPA EVTRSPLLGE HTDEILRQVL GFSDHQVAEI HDSGALDPPR 


KEAAE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000494 Genomic DNA. Translation: ABQ35231.1.
RefSeqYP_001239137.1. NC_009485.1.

3D structure databases

ProteinModelPortalA5EGD7.
SMRA5EGD7. Positions 1-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5EGD7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5149017.
GenomeReviewsGene locus BBta_3113 in contig CP000494_GR.
KEGGbbt:BBta_3113.
PATRIC21207053. VBIBraSp29847_3209.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1804.
HOGENOMHBG659028.
OMAQFGEGIP.
ProtClustDBPRK05398.

Family and domain databases

HAMAPMF_00742. Formyl-CoA_transfer.
[Tree]
InterProIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
IPR017659. Formyl-CoA_transferase.
[Graphical view]
Gene3DG3DSA:3.40.50.10540. CoA-Trfase_fam_III. 1 hit.
KOK07749.
PANTHERPTHR11837. CAIB_BAIF. 1 hit.
PfamPF02515. CoA_transf_3. 1 hit.
[Graphical view]
SUPFAMSSF89796. CoA-Trfase_fam_III. 1 hit.
TIGRFAMsTIGR03253. Oxalate_frc. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFCTA_BRASB
AccessionPrimary (citable) accession number: A5EGD7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families