Reviewed, UniProtKB/Swiss-Prot A7ZPI2 (FCTA_ECO24)

Names and origin

Protein names

Recommended name:
    Formyl-coenzyme A transferase
      Short name=Formyl-CoA transferase
    EC=2.8.3.16

Gene names

Name:	frc
Ordered Locus Names:	EcE24377A_2662

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate By similarity.
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.
Sequence similarities	Belongs to the caiB/baiF CoA-transferase family.

Ontologies

Keywords
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	formyl-CoA transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 416	416	Formyl-coenzyme A transferase HAMAP MF_00742		PRO_1000062168
Sites
	Active site	169	1	Nucleophile By similarity
	Binding site	96	1	Coenzyme A By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ZPI2-1 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 97F7FA4001073301	FASTA	416	45,828
	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

References

[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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000800 Genomic DNA. Translation: ABV18483.1.
RefSeq	YP_001463711.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZPI2.
Genome annotation databases
GeneID	5586087.
GenomeReviews	Gene locus EcE24377A_2662 in contig CP000800_GR.
KEGG	ecw:EcE24377A_2662.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	GWVLKCK.
Family and domain databases
HAMAP	MF_00742. [Tree]
InterPro	IPR003673. CoA-Trfase_fam_III. IPR017659. Formyl-CoA_transferase. [Graphical view]
Gene3D	G3DSA:3.40.50.10540. CoA-Trfase_fam_III. 1 hit.
PANTHER	PTHR11837. CAIB_BAIF. 1 hit.
Pfam	PF02515. CoA_transf_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR03253. oxalate_frc. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FCTA_ECO24

Accession

Primary (citable) accession number: A7ZPI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	November 3, 2009
This is version 13 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)