Q8CNR1 (FUMC_STAES) 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
Ordered Locus Names:	SE_1532

Organism

Staphylococcus epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP]

Taxonomic identifier

176280 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus epidermidis

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
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. HAMAP-Rule 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	Allosteric enzyme Complete proteome
Gene Ontology (GO)
Biological_process	fumarate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: HAMAP
Cellular_component	tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro
Molecular_function	fumarate hydratase activity Inferred from electronic annotation. Source: HAMAP
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-Rule MF_00743		PRO_0000161317
Regions
	Region	97 – 99	3	Substrate binding By similarity
	Region	127 – 130	4	B site By similarity
	Region	137 – 139	3	Substrate binding By similarity
	Region	185 – 186	2	Substrate binding By similarity
	Region	322 – 324	3	Substrate binding By similarity
Sites
	Active site	186	1	Proton donor/acceptor By similarity
	Active site	316	1	By similarity
	Binding site	317	1	Substrate By similarity
	Site	329	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8CNR1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 478E748E9F13827A	FASTA	461	51,329
	10 20 30 40 50 60 MSVRIEHDTF GEIEVPEDKY WGAQTERSKR NFPVGKEHMP IQVIYGFAQL KRGAALANHE 70 80 90 100 110 120 LGKLSDEKKN AIVYACDRIL NGELDNHFPL VIWQTGSGTQ SNMNVNEVVS YVANEYLKKH 130 140 150 160 170 180 GSKETIHPND DVNKSQSSND TFPTAMHVAL FHEVETKLEP ALNHLRQTFK EKEDQYQSII 190 200 210 220 230 240 KIGRTHLQDA TPIKLGQEIS GWRYMLEKCE QLLSESKKHI LNLAIGGTAV GTGINAHPEF 250 260 270 280 290 300 GHKVAKYISQ NTGYAFVSSE NKFHALTSHD EIVQLHGTLK ALATDLMKIA NDIRWLASGP 310 320 330 340 350 360 RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTTVGIASS QGNFELNVFK 370 380 390 400 410 420 PVIMHNTLQS IYLLADGMNT FNKNCAIGIQ PIEENINNYL NQSLMLVTAL NPHIGYEKAA 430 440 450 460 QIAKKAHKEG LTLKESAIES GYVTESQFEE WIKPEDMVDP H

References

[1]

"Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)." Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M. Mol. Microbiol. 49:1577-1593(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12228.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE015929 Genomic DNA. Translation: AAO05131.1.
RefSeq	NP_765087.1. NC_004461.1.
3D structure databases
ProteinModelPortal	Q8CNR1.
SMR	Q8CNR1. Positions 3-457.
ModBase	Search...
Protein-protein interaction databases
STRING	176280.SE1532.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO05131; AAO05131; SE_1532.
GeneID	1056804.
KEGG	sep:SE1532.
PATRIC	19608864. VBIStaEpi113981_1497.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0114.
KO	K01679.
OMA	KDTMGEV.
ProtClustDB	PRK00485.
Enzyme and pathway databases
UniPathway	UPA00223; UER01007.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
HAMAP	MF_00743. FumaraseC.
InterPro	IPR003031. D_crystallin. IPR005677. Fum_hydII. IPR024083. Fumarase/histidase_N. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. [Graphical view]
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_STAES

Accession

Primary (citable) accession number: Q8CNR1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program