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Q6G884 (FUMC_STAAS) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 69. 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:
Fumarate hydratase class II

Short name=Fumarase C
EC=4.2.1.2
Gene names
Name:fumC
Synonyms:citG
Ordered Locus Names:SAS1772
OrganismStaphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]
Taxonomic identifier282459 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743

Catalytic activity

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00743

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00743.

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 termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161315

Regions

Region97 – 993Substrate binding By similarity
Region127 – 1304B site By similarity
Region137 – 1393Substrate binding By similarity
Region185 – 1862Substrate binding By similarity
Region322 – 3243Substrate binding By similarity

Sites

Active site1861Proton donor/acceptor By similarity
Active site3161 By similarity
Binding site3171Substrate By similarity
Site3291Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G884 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 74BBF16CB7C3A638

FASTA46151,146
        10         20         30         40         50         60 
MSVRIEHDTF GEIEVPADKY WGAQTERSKR NFPVGKERMP IEVVYGFAQL KRAAALANFD 

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

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

       190        200        210        220        230        240 
KIGRTHLQDA TPIKLGQEIS GWRYMLDRCE IMLSESKKHI 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571857 Genomic DNA. Translation: CAG43577.1.
RefSeqYP_043889.1. NC_002953.3.

3D structure databases

ProteinModelPortalQ6G884.
SMRQ6G884. Positions 3-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING282459.SAS1772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2863681.
KEGGsas:SAS1772.
PATRIC19553067. VBIStaAur96780_1844.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_STAAS
AccessionPrimary (citable) accession number: Q6G884
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 19, 2004
Last modified: March 19, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways