Q6G884 (FUMC_STAAS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fumarate hydratase class II
Short name=Fumarase C
EC=4.2.1.2

Gene names

Name:	fumC
Synonyms:	citG
Ordered Locus Names:	SAS1772

Organism

Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]

Taxonomic identifier

282459 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-malate = fumarate + H2O. HAMAP MF_00743
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP MF_00743
Subunit structure	Homotetramer By similarity. HAMAP MF_00743
Subcellular location	Cytoplasm By similarity HAMAP 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. HAMAP MF_00743
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular function	fumarate hydratase 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
	Chain	1 – 461	461	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161315
Regions
	Region	127 – 130	4	B site By similarity
	Region	137 – 139	3	Substrate binding By similarity
Sites
	Binding site	99	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6G884 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 74BBF16CB7C3A638	FASTA	461	51,146
	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

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MSSA476.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571857 Genomic DNA. Translation: CAG43577.1.
RefSeq	YP_043889.1. NC_002953.3.
3D structure databases
ProteinModelPortal	Q6G884.
SMR	Q6G884. Positions 3-458.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6G884.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000023239; EBSTAP00000022406; EBSTAG00000023238.
GeneID	2863681.
GenomeReviews	Gene locus SAS1772 in contig BX571857_GR.
KEGG	sas:SAS1772.
PATRIC	19553067. VBIStaAur96780_1844.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0114.
GeneTree	EBGT00050000024474.
HOGENOM	HBG284369.
OMA	RIEKDTM.
PhylomeDB	Q6G884.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	SAUR282459:SAS1772-MONOMER.
Family and domain databases
HAMAP	MF_00743. FumaraseC. [Tree]
InterPro	IPR003031. D_crystallin. IPR005677. Fum_hydII. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR022761. Lyase1_N. [Graphical view]
Gene3D	G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KO	K01679.
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
SUPFAM	SSF48557. L-Aspartase-like. 1 hit.
TIGRFAMs	TIGR00979. FumC_II. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_STAAS

Accession

Primary (citable) accession number: Q6G884

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program