Reviewed, UniProtKB/Swiss-Prot O25883 (FUMC_HELPY)

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:	HP_1325

Organism

Helicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]

Taxonomic identifier

210 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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 – 463	463	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161280
Regions
	Region	128 – 131	4	B site By similarity
	Region	138 – 140	3	Substrate binding By similarity
Sites
	Binding site	99	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O25883-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: D5798ADBC0EA0260	FASTA	463	50,975
	10 20 30 40 50 60 MQFRIEHDTM GEIKVNDSQY WGAQTQRSLE NFKIGTEKMP KELIGAFAKL KRSLAVVNHK 70 80 90 100 110 120 LGKLSLEKSQ AIIKACDCIL KGELCGEFPL AIWQTGSGTQ TNMNLNEVIA NKATEILGGN 130 140 150 160 170 180 FREKKLIHPN DDVNMSQSSN DTFPTAMHIV SVLEITHRLL PSLENLLKTF KEKSQQFKEI 190 200 210 220 230 240 VKIGRTHLQD ATPLTLGQEF SGYASMLEHS KQQILESLEH LRELAIGGTA VGTGLNAHKE 250 260 270 280 290 300 LSEKVAEELS QFSGVKFVSA PNKFHALTSH DAIAYAHGAF KALAANLMKI ANDIRWLASG 310 320 330 340 350 360 PRCGLGELNI PENEPGSSIM PGKVNPTQCE AMTMVAVQVM GNDTAIGIAA SQGNFELNVF 370 380 390 400 410 420 KPVIIYNFLQ SLRLLSDSME SFNIHCASGI EPNREKIDYY LHHSLMLVTA LNPHVGYENA 430 440 450 460 AKIAKNAHKK GISLKESALE LKLLSAEDFD KFVVPEKMIG PKA

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000511 Genomic DNA. Translation: AAD08368.1.
PIR	E64685.
RefSeq	NP_208117.1.
3D structure databases
HSSP	HSSP built from PDB template 1FUR based on UniProtKB P05042.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3320N.
Genome annotation databases
GeneID	898748.
GenomeReviews	Gene locus HP_1325 in contig AE000511_GR.
KEGG	hpy:HP1325.
NMPDR	fig|85962.1.peg.1313.
TIGR	HP_1325.
Phylogenomic databases
HOGENOM	O25883.
OMA	GSQGHFE.
Enzyme and pathway databases
BRENDA	4.2.1.2. 1131.
Family and domain databases
HAMAP	MF_00743. [Tree]
InterPro	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	PR00149. FUMRATELYASE.
TIGRFAMs	TIGR00979. fumC_II. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_HELPY

Accession

Primary (citable) accession number: O25883

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 63 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)