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Q82M40 (FCTA_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Formyl-coenzyme A transferase

Short name=Formyl-CoA transferase
EC=2.8.3.16
Gene names
Name:frc
Ordered Locus Names:SAV_1820
OrganismStreptomyces avermitilis [Complete proteome] [HAMAP]
Taxonomic identifier33903 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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

Sequence similarities

Belongs to the CaiB/BaiF CoA-transferase family.

Ontologies

Keywords
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionformyl-CoA transferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Formyl-coenzyme A transferase HAMAP MF_00742
PRO_0000194723

Sites

Active site1671Nucleophile By similarity
Binding site951Coenzyme A By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82M40 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8204C8A684585A7B

FASTA40944,360
        10         20         30         40         50         60 
MTKALEGIRV LDMTHVQSGP SATQLLAWLG ADVVKLEAPT GDITRGQLRD LPDVDSLYFT 

        70         80         90        100        110        120 
MLNCNKRSIT LNTKTERGKE ILTELIRRSD VMVENFGPGA VDRMGFTWDR IRDINPRIVY 

       130        140        150        160        170        180 
ASIKGFGDGP YTDFKAYEVV AQAMGGSMST TGFEDGPPLA TGAQIGDSGT GIHAVAGILA 

       190        200        210        220        230        240 
ALYQRENTGR GQRVNVAMQH AVLNLCRVKL RDQQRLAHGP LAEYPNDDFG DEVPRSGNAS 

       250        260        270        280        290        300 
GGGQPGWAVK CAPGGPNDYV YVIVQPVGWK PLSELIGRPE LADDPEWATP EARLPQLTKM 

       310        320        330        340        350        360 
FQLIEEWSAT LPKWEVLEKL NAHNIPCGPI LSTKEIVEDA SLVANEMVVT VPHPERGEFV 

       370        380        390        400 
TVGSPLKLSD SPVDVTSSPL LGEHNAEVYV GELGLGDEEL RLLKSNGVI 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC69531.1.
RefSeqNP_822996.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ82M40.
SMRQ82M40. Positions 1-409.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1213305.
GenomeReviewsGene locus SAV_1820 in contig BA000030_GR.
KEGGsma:SAV_1820.
NMPDRfig|227882.1.peg.1822.
PATRIC23717055. VBIStrAve112782_1941.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG659028.
OMANDYVYVI.
ProtClustDBPRK05398.

Enzyme and pathway databases

BioCycSAVE227882:SAV1820-MONOMER.

Family and domain databases

HAMAPMF_00742. Formyl-CoA_transfer.
[Tree]
InterProIPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
IPR017659. Formyl-CoA_transferase.
[Graphical view]
Gene3DG3DSA:3.40.50.10540. CoA-Trfase_fam_III. 1 hit.
KOK07749.
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...

Entry information

Entry nameFCTA_STRAW
AccessionPrimary (citable) accession number: Q82M40
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families