Reviewed, UniProtKB/Swiss-Prot P64172 (FUMC_STAAM)

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:	SAV1851

Organism

Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP]

Taxonomic identifier

158878 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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 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: 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 MF_00743		PRO_0000161312
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)
	P64172-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 5FB7439BBE7A559E	FASTA	461	51,161
	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 DVNESQSSND TFPTAMHVAL YQEVETKLEP ALKLLRNTLK EKEDKFESII 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]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000017 Genomic DNA. Translation: BAB58013.1.
RefSeq	NP_372375.1.
3D structure databases
HSSP	HSSP built from PDB template 1FUR based on UniProtKB P05042.
ModBase	Search...
Protein-protein interaction databases
STRING	P64172.
2-D gel databases
World-2DPAGE	0002:P64172.
Genome annotation databases
GeneID	1121833.
GenomeReviews	Gene locus SAV1851 in contig BA000017_GR.
KEGG	sav:SAV1851.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P64172.
OMA	GSQGHFE.
Enzyme and pathway databases
BioCyc	SAUR158878:SAV1851-MON.
Family and domain databases
HAMAP	MF_00743. [Tree]
InterPro	IPR003031. D_crystallin. IPR005677. Fum_hydII. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. [Graphical view]
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
TIGRFAMs	TIGR00979. fumC_II. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_STAAM

Accession

Primary (citable) accession number: P64172
Secondary accession number(s): Q99T27

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)