Reviewed, UniProtKB/Swiss-Prot P69902 (FCTA_ECOLI)

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
Synonyms:	yfdW
Ordered Locus Names:	b2374, JW2371

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. 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. HAMAP MF_00742
Sequence similarities	Belongs to the caiB/baiF CoA-transferase family.

Ontologies

Keywords
Molecular function	Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	formyl-CoA transferase activity Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-1128607,EBI-548960

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_0000194716

Regions

Region

17 – 18

2

Coenzyme A binding HAMAP MF_00742

Region

137 – 140

4

Coenzyme A binding HAMAP MF_00742

Sites

Active site

169

1

Nucleophile HAMAP MF_00742

Binding site

75

1

Coenzyme A HAMAP MF_00742

Binding site

96

1

Coenzyme A HAMAP MF_00742

Binding site

98

1

Coenzyme A HAMAP MF_00742

Secondary structure

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416

Helix Strand Turn

Details...

Turn

4 – 7

4

Beta strand

9 – 12

4

Helix

18 – 28

11

Beta strand

32 – 37

6

Turn

39 – 41

3

Helix

44 – 46

3

Turn

47 – 49

3

Helix

58 – 61

4

Beta strand

68 – 71

4

Helix

77 – 89

13

Beta strand

91 – 95

5

Helix

109 – 115

7

Beta strand

120 – 127

8

Turn

132 – 135

4

Helix

140 – 146

7

Helix

149 – 152

4

Turn

167 – 169

3

Helix

170 – 190

21

Beta strand

195 – 199

5

Helix

200 – 207

8

Helix

209 – 221

13

Turn

228 – 232

5

Beta strand

247 – 250

4

Beta strand

252 – 256

5

Turn

258 – 262

5

Beta strand

267 – 271

5

Helix

274 – 276

3

Helix

277 – 283

7

Helix

287 – 290

4

Turn

293 – 295

3

Helix

298 – 301

4

Helix

302 – 304

3

Helix

305 – 316

12

Helix

321 – 328

8

Helix

329 – 331

3

Beta strand

335 – 337

3

Helix

341 – 346

6

Helix

348 – 352

5

Beta strand

355 – 361

7

Turn

362 – 364

3

Beta strand

365 – 370

6

Beta strand

373 – 378

6

Turn

389 – 392

4

Helix

393 – 399

7

Helix

404 – 416

13

Sequences

	Sequence		Length	Mass (Da)
	P69902-1 [UniParc]. Last modified January 4, 2005. 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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The crystal structure of the Escherichia coli YfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases." Gruez A., Roig-Zamboni V., Valencia C., Campanacci V., Cambillau C. J. Biol. Chem. 278:34582-34586(2003) [PubMed: 12844490] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF APOENZYME AND OF COMPLEX WITH COENZYME A AND OXALATE. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC75433.1.
AP009048 Genomic DNA. Translation: BAA16247.1.

PIR

C65011.

RefSeq

AP_002974.1.
NP_416875.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PQY	X-ray	2.35	A	2-416	[»]
1PT5	X-ray	2.00	A/B	1-416	[»]
1PT7	X-ray	1.80	A/B	1-416	[»]
1PT8	X-ray	2.20	A/B	1-416	[»]
1Q6Y	X-ray	1.99	A	2-416	[»]
1Q7E	X-ray	1.60	A	2-416	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P69902. 1 interaction.

STRING

P69902.

Genome annotation databases

GeneID

946842.

GenomeReviews

Gene locus JW2371 in contig AP009048_GR.
Gene locus b2374 in contig U00096_GR.

KEGG

ecj:JW2371.
eco:b2374.

Organism-specific databases

EchoBASE

EB3897.

EcoGene

EG14145. frc.

CMR

Search...

Phylogenomic databases

eggNOG

COG1804.

HOGENOM

HBG659028.

OMA

KFDIPCA.

Enzyme and pathway databases

BioCyc

EcoCyc:G7237-MONOMER.
ECOL168927:B2374-MONOMER.
MetaCyc:G7237-MONOMER.

Gene expression databases

Genevestigator

P69902.

Family and domain databases

HAMAP

MF_00742. Formyl-CoA_transfer.
[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_ECOLI

Accession

Primary (citable) accession number: P69902
Secondary accession number(s): P77407

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	January 4, 2005
Last modified:	February 9, 2010
This is version 49 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)