O06644 (FCTA_OXAFO) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Oxalobacter formigenes

Taxonomic identifier

847 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Oxalobacteraceae › Oxalobacter

Protein attributes

Sequence length	428 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. HAMAP-Rule MF_00742
Catalytic activity	Formyl-CoA + oxalate = formate + oxalyl-CoA. Ref.1
Pathway	Metabolic intermediate degradation; oxalate degradation; CO(2) and formate from oxalate: step 1/2. HAMAP-Rule MF_00742
Subunit structure	Dimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00742.
Sequence similarities	Belongs to the CaiB/BaiF CoA-transferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	oxalate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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

Initiator methionine

1

1

Removed HAMAP-Rule MF_00742

Chain

2 – 428

427

Formyl-coenzyme A transferase HAMAP-Rule MF_00742

PRO_0000194720

Regions

Region

15 – 17

3

Coenzyme A binding HAMAP-Rule MF_00742

Sites

Active site

169

1

Nucleophile

Binding site

96

1

Coenzyme A

Binding site

137

1

Coenzyme A

Secondary structure

1

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428

Helix Strand Turn

Details...

Turn

4 – 7

4

Beta strand

9 – 12

4

Helix

18 – 28

11

Beta strand

32 – 38

7

Turn

39 – 41

3

Helix

44 – 47

4

Helix

58 – 61

4

Turn

62 – 65

4

Beta strand

68 – 72

5

Beta strand

74 – 76

3

Helix

77 – 89

13

Beta strand

91 – 95

5

Helix

101 – 104

4

Helix

109 – 115

7

Beta strand

120 – 127

8

Turn

132 – 135

4

Helix

140 – 146

7

Turn

147 – 149

3

Helix

150 – 152

3

Helix

169 – 190

22

Beta strand

195 – 199

5

Helix

200 – 207

8

Helix

209 – 221

13

Helix

228 – 230

3

Turn

232 – 234

3

Helix

245 – 247

3

Beta strand

261 – 268

8

Turn

270 – 274

5

Beta strand

279 – 283

5

Helix

286 – 288

3

Helix

289 – 295

7

Helix

299 – 301

3

Turn

305 – 307

3

Helix

310 – 313

4

Turn

314 – 316

3

Helix

317 – 326

10

Turn

327 – 330

4

Helix

333 – 342

10

Beta strand

347 – 349

3

Helix

353 – 357

5

Helix

360 – 364

5

Beta strand

367 – 371

5

Turn

374 – 376

3

Beta strand

379 – 382

4

Beta strand

385 – 390

6

Turn

401 – 404

4

Helix

405 – 411

7

Helix

416 – 424

9

Sequences

	Sequence		Length	Mass (Da)
	O06644 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 386E87C19EA0C8AC	FASTA	428	47,327
	10 20 30 40 50 60 MTKPLDGINV LDFTHVQAGP ACTQMMGFLG ANVIKIERRG SGDMTRGWLQ DKPNVDSLYF 70 80 90 100 110 120 TMFNCNKRSI ELDMKTPEGK ELLEQMIKKA DVMVENFGPG ALDRMGFTWE YIQELNPRVI 130 140 150 160 170 180 LASVKGYAEG HANEHLKVYE NVAQCSGGAA ATTGFWDGPP TVSGAALGDS NSGMHLMIGI 190 200 210 220 230 240 LAALEMRHKT GRGQKVAVAM QDAVLNLVRI KLRDQQRLER TGILAEYPQA QPNFAFDRDG 250 260 270 280 290 300 NPLSFDNITS VPRGGNAGGG GQPGWMLKCK GWETDADSYV YFTIAANMWP QICDMIDKPE 310 320 330 340 350 360 WKDDPAYNTF EGRVDKLMDI FSFIETKFAD KDKFEVTEWA AQYGIPCGPV MSMKELAHDP 370 380 390 400 410 420 SLQKVGTVVE VVDEIRGNHL TVGAPFKFSG FQPEITRAPL LGEHTDEVLK ELGLDDAKIK ELHAKQVV

References

[1]	"DNA sequencing and expression of the formyl coenzyme A transferase gene, frc, from Oxalobacter formigenes." Sidhu H., Ogden S.D., Lung H.-Y., Luttge B.G., Baetz A.L., Peck A.B. J. Bacteriol. 179:3378-3381(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, CATALYTIC ACTIVITY. Strain: OxB.
[2]	"Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes." Baetz A.L., Allison M.J. J. Bacteriol. 172:3537-3540(1990) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: OxB.
[3]	"Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer." Ricagno S., Jonsson S., Richards N., Lindqvist Y. EMBO J. 22:3210-3219(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH COENZYME A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U82167 Genomic DNA. Translation: AAC45298.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P5H	X-ray	2.20	A/B	1-428	[»]
1P5R	X-ray	2.50	A/B	1-428	[»]
1T3Z	X-ray	2.30	A/B	2-427	[»]
1T4C	X-ray	2.61	A/B	2-427	[»]
1VGQ	X-ray	2.13	A/B	2-427	[»]
1VGR	X-ray	2.10	A/B	2-427	[»]
2VJK	X-ray	1.97	A/B	1-428	[»]
2VJL	X-ray	2.00	A/B	1-428	[»]
2VJM	X-ray	1.89	A/B	1-428	[»]
2VJN	X-ray	2.00	A/B	1-428	[»]
2VJO	X-ray	2.20	A/B	1-428	[»]
2VJP	X-ray	1.95	A/B	1-428	[»]
2VJQ	X-ray	1.80	A/B/C/D	1-428	[»]

ProteinModelPortal

O06644.

SMR

O06644. Positions 2-428.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16179.

BRENDA

2.8.3.16. 4478.

UniPathway

UPA00540; UER00598.

Family and domain databases

Gene3D

3.40.50.10540. 2 hits.

HAMAP

MF_00742. Formyl-CoA_transfer.

InterPro

IPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
IPR017659. Formyl-CoA_transferase.
[Graphical view]

PANTHER

PTHR11837. PTHR11837. 1 hit.

Pfam

PF02515. CoA_transf_3. 1 hit.
[Graphical view]

SUPFAM

SSF89796. CoA-Trfase_fam_III. 1 hit.

TIGRFAMs

TIGR03253. oxalate_frc. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

O06644.

Entry information

Entry name

FCTA_OXAFO

Accession

Primary (citable) accession number: O06644

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program