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Reviewed, UniProtKB/Swiss-Prot Q5HES4 (FUMC_STAAC)

Last modified November 3, 2009. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fumarate hydratase class II
      Short name=Fumarase C
    EC=4.2.1.2
Gene names
Name: fumC
Synonyms: citG
Ordered Locus Names: SACOL1908
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle. HAMAP MF_00743

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

There are 2 substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Fumarate hydratase class II HAMAP MF_00743
PRO_0000161311

Regions

Region127 – 1304B site By similarity
Region137 – 1393Substrate binding By similarity

Sites

Binding site991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HES4-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: FA5B0EB76BBD4185

FASTA46151,108
        10         20         30         40         50         60 
MSVRIEHDTF GEIEVPADKY WGAQTERSKR NFPVGKERMP IEVVYGFAQL KRAAAIANFD 

        70         80         90        100        110        120 
LGKLSEAKKD AIVYACDQIL SGELDEHFPL VVWQTGSGTQ SNMNVNEVVS YVANMYLKDH 

       130        140        150        160        170        180 
QSDESIHPND DVNKSQSSND TFPTAMHVAL YQEVETKLEP ALKLLRNTLK EKEDKFDSII 

       190        200        210        220        230        240 
KIGRTHLQDA TPIKLGQEIS GWRYMLDRCE TMLSESKKHI LNLAIGGTAV GTGINAHPEF 

       250        260        270        280        290        300 
GDKVAHYISE NTGYPFVSSE NKFHALTAHD EVVQLHGTLK ALAGDLMKIA NDVRWLASGP 

       310        320        330        340        350        360 
RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTVVGFASS QGNFELNVYK 

       370        380        390        400        410        420 
PVIMHNTLQS IYLLADGMET FNNNCAVGIE PIEENIDNYL NQSLMLVTAL NPHIGYEKAA 

       430        440        450        460 
QIAKKAHKEG LTLKESAIQT GYVTEEQFEA WIKPEDMVDP H 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000046 Genomic DNA. Translation: AAW36920.1.
RefSeqYP_186733.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HES4.

Genome annotation databases

GeneID3237674.
GenomeReviewsGene locus SACOL1908 in contig CP000046_GR.
KEGGsac:SACOL1908.
TIGRSACOL1908.

Phylogenomic databases

HOGENOMQ5HES4.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycSAUR93062:SACOL1908-MON.

Family and domain databases

HAMAPMF_00743.
[Tree]
InterProIPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_STAAC
AccessionPrimary (citable) accession number: Q5HES4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents