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Protein

Formyl-CoA:oxalate CoA-transferase

Gene

frc

Organism
Oxalobacter formigenes
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. It can also use succinate as acceptor.5 Publications

Catalytic activityi

Formyl-CoA + oxalate = formate + oxalyl-CoA.UniRule annotation5 Publications

Enzyme regulationi

Inhibited by the sulfhydryl reagents N-ethylmaleimide and p-chloromercuribenzoate, and by chloride. Competitively inhibited by acetyl-CoA.3 Publications

Kineticsi

Kcat is 5.3 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius. Kcat is 149 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with succinate as acceptor at pH 6.7 and 30 degrees Celsius.PubMed:18245280).

  1. KM=2 µM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius. PubMed:18245280 and 18162462)4 Publications
  2. KM=8 µM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius. PubMed:15213226)4 Publications
  3. KM=16 µM for formyl-CoA (with succinate as acceptor at pH 6.7 and 30 degrees Celsius. PubMed:18245280)4 Publications
  4. KM=0.32 mM for succinate (with formyl-CoA as donor at pH 6.7 and 30 degrees Celsius. PubMed:18245280)4 Publications
  5. KM=2.3 mM for succinate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius. PubMed:2361939)4 Publications
  6. KM=3 mM for formyl-CoA (with oxalate as acceptor at pH 6.8 and 25 degrees Celsius. PubMed:2361939)4 Publications
  7. KM=3.9 mM for oxalate (with formyl-CoA as donor at pH 6.7 and 30 degrees Celsius. PubMed:18245280 and 15213226)4 Publications
  8. KM=5.1 mM for oxalate4 Publications
  1. Vmax=6.4 µmol/min/mg enzyme with oxalate as substrate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius. PubMed:2361939)4 Publications
  2. Vmax=19.2 µmol/min/mg enzyme with succinate as substrate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius. PubMed:2361939)4 Publications
  3. Vmax=29.6 µmol/min/mg enzyme with formyl-CoA as substrate (with oxalate as acceptor at pH 6.8 and 25 degrees Celsius. PubMed:2361939)4 Publications

pH dependencei

Optimum pH is between 6.5 and 7.5.4 Publications

Pathwayi: oxalate degradation

This protein is involved in step 1 of the subpathway that synthesizes CO(2) and formate from oxalate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Formyl-CoA:oxalate CoA-transferase (frc)
  2. Oxalyl-CoA decarboxylase (oxc)
This subpathway is part of the pathway oxalate degradation, which is itself part of Metabolic intermediate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and formate from oxalate, the pathway oxalate degradation and in Metabolic intermediate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei38Coenzyme AUniRule annotation3 Publications1
Binding sitei104Coenzyme AUniRule annotation3 Publications1
Active sitei169NucleophileUniRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16179.
BRENDAi2.8.3.16. 4478.
UniPathwayiUPA00540; UER00598.

Names & Taxonomyi

Protein namesi
Recommended name:
Formyl-CoA:oxalate CoA-transferase (EC:2.8.3.16UniRule annotation)
Short name:
FCOCT
Alternative name(s):
Formyl-coenzyme A transferaseUniRule annotation
Gene namesi
Name:frcUniRule annotation
OrganismiOxalobacter formigenes
Taxonomic identifieri847 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeOxalobacter

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17Q → A: 45-fold decrease of the catalytic effiency. 1 Publication1
Mutagenesisi48W → F: Little change in the affinity binding and catalytic efficiency, and it does not display major structural changes. 1 Publication1
Mutagenesisi48W → P: Little change in the affinity binding and catalytic efficiency. It exhibits substrate inhibition with oxalate. It does not display major structural changes. 1 Publication1
Mutagenesisi169D → A: Loss of CoA-transferase activity. 1 Publication1
Mutagenesisi169D → E: Loss of CoA-transferase activity. 1 Publication1
Mutagenesisi169D → S: Loss of CoA-transferase activity. 1 Publication1
Mutagenesisi259G → A: 2.5-fold decrease of the catalytic effiency. 1 Publication1
Mutagenesisi260G → A: 25-fold decrease of the catalytic effiency. Reduction of the affinity binding for both formyl-CoA and oxalate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001947202 – 428Formyl-CoA:oxalate CoA-transferaseAdd BLAST427

Interactioni

Subunit structurei

Homodimer.UniRule annotation5 Publications

Protein-protein interaction databases

STRINGi556269.OFBG_01036.

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 7Combined sources4
Beta strandi9 – 12Combined sources4
Helixi18 – 28Combined sources11
Beta strandi32 – 38Combined sources7
Turni39 – 41Combined sources3
Helixi44 – 47Combined sources4
Helixi58 – 61Combined sources4
Turni62 – 66Combined sources5
Beta strandi68 – 72Combined sources5
Beta strandi74 – 76Combined sources3
Helixi77 – 89Combined sources13
Beta strandi91 – 95Combined sources5
Helixi101 – 104Combined sources4
Helixi109 – 115Combined sources7
Beta strandi120 – 127Combined sources8
Turni132 – 135Combined sources4
Helixi140 – 146Combined sources7
Turni147 – 149Combined sources3
Helixi150 – 152Combined sources3
Helixi169 – 190Combined sources22
Beta strandi195 – 199Combined sources5
Helixi200 – 207Combined sources8
Helixi209 – 221Combined sources13
Helixi228 – 230Combined sources3
Turni232 – 234Combined sources3
Turni238 – 240Combined sources3
Helixi245 – 247Combined sources3
Beta strandi261 – 268Combined sources8
Turni270 – 274Combined sources5
Beta strandi279 – 283Combined sources5
Helixi286 – 288Combined sources3
Helixi289 – 295Combined sources7
Helixi299 – 301Combined sources3
Turni305 – 307Combined sources3
Helixi310 – 313Combined sources4
Turni314 – 316Combined sources3
Helixi317 – 326Combined sources10
Turni327 – 330Combined sources4
Helixi333 – 342Combined sources10
Beta strandi347 – 349Combined sources3
Helixi353 – 357Combined sources5
Helixi360 – 364Combined sources5
Beta strandi367 – 371Combined sources5
Turni374 – 376Combined sources3
Beta strandi379 – 382Combined sources4
Beta strandi385 – 390Combined sources6
Turni401 – 404Combined sources4
Helixi405 – 411Combined sources7
Helixi416 – 424Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P5HX-ray2.20A/B1-428[»]
1P5RX-ray2.50A/B1-428[»]
1T3ZX-ray2.30A/B2-428[»]
1T4CX-ray2.61A/B2-428[»]
1VGQX-ray2.13A/B2-428[»]
1VGRX-ray2.10A/B2-428[»]
2VJKX-ray1.97A/B1-428[»]
2VJLX-ray2.00A/B1-428[»]
2VJMX-ray1.89A/B1-428[»]
2VJNX-ray2.00A/B1-428[»]
2VJOX-ray2.20A/B1-428[»]
2VJPX-ray1.95A/B1-428[»]
2VJQX-ray1.80A/B/C/D1-428[»]
ProteinModelPortaliO06644.
SMRiO06644.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO06644.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni15 – 18Coenzyme A binding4
Regioni72 – 75Coenzyme A binding4
Regioni96 – 98Coenzyme A binding3
Regioni137 – 140Coenzyme A binding4
Regioni260 – 262Substrate binding3

Sequence similaritiesi

Belongs to the CaiB/BaiF CoA-transferase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C04. Bacteria.
COG1804. LUCA.
KOiK07749.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
HAMAPiMF_00742. Formyl_CoA_transfer. 1 hit.
InterProiIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
IPR017659. Formyl_CoA_transfer.
[Graphical view]
PfamiPF02515. CoA_transf_3. 2 hits.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.
TIGRFAMsiTIGR03253. oxalate_frc. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O06644-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKPLDGINV LDFTHVQAGP ACTQMMGFLG ANVIKIERRG SGDMTRGWLQ
60 70 80 90 100
DKPNVDSLYF TMFNCNKRSI ELDMKTPEGK ELLEQMIKKA DVMVENFGPG
110 120 130 140 150
ALDRMGFTWE YIQELNPRVI LASVKGYAEG HANEHLKVYE NVAQCSGGAA
160 170 180 190 200
ATTGFWDGPP TVSGAALGDS NSGMHLMIGI LAALEMRHKT GRGQKVAVAM
210 220 230 240 250
QDAVLNLVRI KLRDQQRLER TGILAEYPQA QPNFAFDRDG NPLSFDNITS
260 270 280 290 300
VPRGGNAGGG GQPGWMLKCK GWETDADSYV YFTIAANMWP QICDMIDKPE
310 320 330 340 350
WKDDPAYNTF EGRVDKLMDI FSFIETKFAD KDKFEVTEWA AQYGIPCGPV
360 370 380 390 400
MSMKELAHDP SLQKVGTVVE VVDEIRGNHL TVGAPFKFSG FQPEITRAPL
410 420
LGEHTDEVLK ELGLDDAKIK ELHAKQVV
Length:428
Mass (Da):47,327
Last modified:January 23, 2007 - v3
Checksum:i386E87C19EA0C8AC
GO

Mass spectrometryi

Molecular mass is 47196 Da from positions 1 - 428. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82167 Genomic DNA. Translation: AAC45298.1.

Genome annotation databases

KEGGiag:AAC45298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82167 Genomic DNA. Translation: AAC45298.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P5HX-ray2.20A/B1-428[»]
1P5RX-ray2.50A/B1-428[»]
1T3ZX-ray2.30A/B2-428[»]
1T4CX-ray2.61A/B2-428[»]
1VGQX-ray2.13A/B2-428[»]
1VGRX-ray2.10A/B2-428[»]
2VJKX-ray1.97A/B1-428[»]
2VJLX-ray2.00A/B1-428[»]
2VJMX-ray1.89A/B1-428[»]
2VJNX-ray2.00A/B1-428[»]
2VJOX-ray2.20A/B1-428[»]
2VJPX-ray1.95A/B1-428[»]
2VJQX-ray1.80A/B/C/D1-428[»]
ProteinModelPortaliO06644.
SMRiO06644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi556269.OFBG_01036.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC45298.

Phylogenomic databases

eggNOGiENOG4105C04. Bacteria.
COG1804. LUCA.
KOiK07749.

Enzyme and pathway databases

UniPathwayiUPA00540; UER00598.
BioCyciMetaCyc:MONOMER-16179.
BRENDAi2.8.3.16. 4478.

Miscellaneous databases

EvolutionaryTraceiO06644.

Family and domain databases

Gene3Di3.40.50.10540. 2 hits.
HAMAPiMF_00742. Formyl_CoA_transfer. 1 hit.
InterProiIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
IPR017659. Formyl_CoA_transfer.
[Graphical view]
PfamiPF02515. CoA_transf_3. 2 hits.
[Graphical view]
SUPFAMiSSF89796. SSF89796. 1 hit.
TIGRFAMsiTIGR03253. oxalate_frc. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFCTA_OXAFO
AccessioniPrimary (citable) accession number: O06644
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.