Reviewed, UniProtKB/Swiss-Prot Q9RR70 (FUMC_DEIRA)

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:	DR_2627

Organism

Deinococcus radiodurans [Complete proteome] [HAMAP]

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	464 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: 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 – 464	464	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161274
Regions
	Region	131 – 134	4	B site By similarity
	Region	141 – 143	3	Substrate binding By similarity
Sites
	Binding site	102	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9RR70-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6CE8DC9A8D90A07E	FASTA	464	49,876
	10 20 30 40 50 60 MTKTRQETDT MGKMDVDASR YWGAQTERSI HNFPIGRDTF VWGRPVIRAL GILKKGAAQA 70 80 90 100 110 120 NAELGELPAD VADLIVKAAD EVIAGKLDEH FPLVVFQTGS GTQSNMNANE VISNRAIELA 130 140 150 160 170 180 GGEMGSKKPV HPNDHVNRGQ SSNDTFPTAM HIAVVLELNE RLYGAVGKLR DTLHAKAEQY 190 200 210 220 230 240 KDLVKVGRTH LQDATPITLG QEIGGWVAQL DYALSEVKHA GEGLLDLAIG GTAVGTGLNA 250 260 270 280 290 300 HPKFGDLAAK KYEEETGYHF RSAENKFAAL SAHDALVQTS AALRTLAGAL MKMANDVRWL 310 320 330 340 350 360 ASGPRNGIGE ITIPENEPGS SIMPGKVNPT QSEAMTMVAT RVFGNDATVA FAGSQGNFQL 370 380 390 400 410 420 NVFKPVMVHA VLESIRLISD ACLAFNDHCA VGIQPNEAKI KENLDKNLMQ VTALNRHIGY 430 440 450 460 DKAAAIAKKA HKEGTSLKDA ALALGYVTED EFAQWVVPLG MTHN

References

[1]

"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000513 Genomic DNA. Translation: AAF12164.1.
PIR	B75250.
RefSeq	NP_296346.1.
3D structure databases
SMR	Q9RR70. Positions 5-459.
ModBase	Search...
Genome annotation databases
GeneID	1797634.
GenomeReviews	Gene locus DR_2627 in contig AE000513_GR.
KEGG	dra:DR_2627.
NMPDR	fig|243230.1.peg.2805.
TIGR	DR_2627.
Phylogenomic databases
HOGENOM	HBG284369.
OMA	RIEKDTM.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_2627-MONOMER.
BRENDA	4.2.1.2. 96172.
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. [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_DEIRA

Accession

Primary (citable) accession number: Q9RR70

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 60 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)