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Reviewed, UniProtKB/Swiss-Prot A7ZPI2 (FCTA_ECO24)

Last modified July 13, 2010. Version 20. 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:EcE24377A_2662
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [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_1000062168

Sites

Active site1691Nucleophile By similarity
Binding site961Coenzyme A By similarity
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SequencesHide

Sequence LengthMass (Da)Tools
A7ZPI2-1 [UniParc].

Last modified October 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 pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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Cross-referencesHide

Sequence databases

EMBL
GenBank
DDBJ
CP000800 Genomic DNA. Translation: ABV18483.1.
RefSeqYP_001463711.1.

3D structure databases

SMRA7ZPI2. Positions 1-416.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZPI2.

Genome annotation databases

EnsemblBacteriaEBESCT00000021347; EBESCP00000020409; EBESCG00000020401.
GeneID5586087.
GenomeReviewsGene locus EcE24377A_2662 in contig CP000800_GR.
KEGGecw:EcE24377A_2662.

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_ECO24
AccessionPrimary (citable) accession number: A7ZPI2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: July 13, 2010
This is version 20 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