O69294 (FUMC_CAMJE) 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:	Cj1364c

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	463 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 Reference 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 – 463	463	Fumarate hydratase class II HAMAP MF_00743		PRO_0000161263
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)
	O69294 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: E281B37B5791FFC0	FASTA	463	50,710
	10 20 30 40 50 60 MEYRVEHDTM GEVKVPNDKY WGAQTERSFE NFKIGCEKMP KVLIYAFANL KKSLALVNNK 70 80 90 100 110 120 LGKLDDAKKN AIVQACDEII AGKFDDNFPL AIWQTGSGTQ SNMNMNEVIA NRATEIMGGD 130 140 150 160 170 180 FRKEKLVHPN DHVNMSQSSN DTFPTAMSIV AVEQVEKKLI PALDELIATF EKKVKEFDGI 190 200 210 220 230 240 IKIGRTHLQD ATPLTLAQEF SGYLSMLLHS KEQIIASLPT LRELAIGGTA VGTGLNAHPE 250 260 270 280 290 300 LSQKVSEELT QLIGTKFISS PNKFHALTSH DAINFTHGAM KGLAANLMKI ANDIRWLASG 310 320 330 340 350 360 PRCGLGELII PENEPGSSIM PGKVNPTQCE AVTMVAVQVM GNDVAIGFAA SQGNFELNVF 370 380 390 400 410 420 KPVIIYNFLQ SLDLLADSMH SFNIHCAVGI EPNRAKIDHN LHNSLMLVTA LNPHIGYENA 430 440 450 460 AKVAKNAHKK GISLKESTME LGLVSEEDFN KFVDPTKMIG PKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Griffiths P.L., Connerton I.F. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.
[2]	"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y16882 Genomic DNA. Translation: CAA76499.1. AL111168 Genomic DNA. Translation: CAL35476.1.
PIR	A81281.
RefSeq	YP_002344752.1. NC_002163.1.
3D structure databases
ProteinModelPortal	O69294.
SMR	O69294. Positions 4-459.
ModBase	Search...
Protein-protein interaction databases
IntAct	O69294. 11 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	905657.
GenomeReviews	Gene locus Cj1364c in contig AL111168_GR.
KEGG	cje:Cj1364c.
PATRIC	20059693. VBICamJej33762_1345.
Phylogenomic databases
HOGENOM	HBG284369.
OMA	RIEKDTM.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1364C-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_CAMJE

Accession

Primary (citable) accession number: O69294
Secondary accession number(s): Q0P8P5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program