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Reviewed, UniProtKB/Swiss-Prot A1ADQ1 (FCTA_ECOK1)

Last modified July 13, 2010. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
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Names and originHide

Protein namesRecommended name:
Formyl-coenzyme A transferase

Short name=Formyl-CoA transferase
EC=2.8.3.16
Gene names
Name:frc
Ordered Locus Names:Ecok1_22970
ORF Names:APECO1_4162
OrganismEscherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]
Taxonomic identifier405955 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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Protein attributesHide

Sequence length416 AA.
Sequence statusComplete.
Protein existenceInferred from homology.
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General annotation (Comments)Hide

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

Subunit structure

Homodimer By similarity. HAMAP MF_00742

Sequence similarities

Belongs to the caiB/baiF CoA-transferase family.

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OntologiesHide

Keywords
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionformyl-CoA transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...
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Sequence annotation (Features)Hide

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Formyl-coenzyme A transferase HAMAP MF_00742
PRO_0000300988

Sites

Active site1691Nucleophile By similarity
Binding site961Coenzyme A By similarity
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SequencesHide

Sequence LengthMass (Da)Tools
A1ADQ1-1 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 97F7FA4001073301

FASTA41645,828
        10         20         30         40         50         60 
MSTPLQGIKV LDFTGVQSGP SCTQMLAWFG ADVIKIERPG VGDVTRHQLR DIPDIDALYF 

        70         80         90        100        110        120 
TMLNSNKRSI ELNTKTAEGK EVMEKLIREA DILVENFHPG AIDHMGFTWE HIQEINPRLI 

       130        140        150        160        170        180 
FGSIKGFDEC SPYVNVKAYE NVAQAAGGAA STTGFWDGPP LVSAAALGDS NTGMHLLIGL 

       190        200        210        220        230        240 
LAALLHREKT GRGQRVTMSM QDAVLNLCRV KLRDQQRLDK LGYLEEYPQY PNGTFGDAVP 

       250        260        270        280        290        300 
RGGNAGGGGQ PGWILKCKGW ETDPNAYIYF TIQEQNWENT CKAIGKPEWI TDPAYSTAHA 

       310        320        330        340        350        360 
RQPHIFDIFA EIEKYTVTID KHEAVAYLTQ FDIPCAPVLS MKEISLDPSL RQSGSVVEVE 

       370        380        390        400        410 
QPLRGKYLTV GCPMKFSAFT PDIKAAPLLG EHTAAVLQEL GYSDDEIAAM KQNHAI 

« Hide

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ReferencesHide

[1]"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
J. Bacteriol. 189:3228-3236(2007) [PubMed: 17293413] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
CP000468 Genomic DNA. Translation: ABJ01791.1.
RefSeqYP_853505.1.

3D structure databases

SMRA1ADQ1. Positions 1-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1ADQ1.

Genome annotation databases

EnsemblBacteriaEBESCT00000038761; EBESCP00000037278; EBESCG00000037811.
GeneID4492491.
GenomeReviewsGene locus Ecok1_22970 in contig CP000468_GR.
KEGGecv:APECO1_4162.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1804.
HOGENOMHBG659028.
OMADEWANDP.
ProtClustDBPRK05398.

Family and domain databases

HAMAPMF_00742. Formyl-CoA_transfer.
[Tree]
InterProIPR003673. CoA-Trfase_fam_III.
IPR017659. Formyl-CoA_transferase.
[Graphical view]
Gene3DG3DSA:3.40.50.10540. CoA-Trfase_fam_III. 1 hit.
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...
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Entry informationHide

Entry nameFCTA_ECOK1
AccessionPrimary (citable) accession number: A1ADQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 23, 2007
Last modified: July 13, 2010
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
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Relevant documentsHide

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents