Q83CL8 (FUMC_COXBU) 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:	CBU_1096

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	459 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 Reference 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 – 459	459	Fumarate hydratase class II HAMAP-Rule MF_00743		PRO_0000161273
Regions
	Region	95 – 97	3	Substrate binding By similarity
	Region	126 – 129	4	B site By similarity
	Region	136 – 138	3	Substrate binding By similarity
	Region	184 – 185	2	Substrate binding By similarity
	Region	321 – 323	3	Substrate binding By similarity
Sites
	Active site	185	1	Proton donor/acceptor By similarity
	Active site	315	1	By similarity
	Binding site	316	1	Substrate By similarity
	Site	328	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q83CL8 [UniParc]. Last modified December 15, 2003. Version 2. Checksum: 15153802D24B2359	FASTA	459	49,850
	10 20 30 40 50 60 MRKESDSMGT IEVPSEKYYG AQSQRSLINF AIGRETMPPE LIRAFGVLKK AAVLTNVELG 70 80 90 100 110 120 KVSQEKANFI LKACEELIAG KLNDHFPLKI WQTGSGTQTN MNVNEVISNR AIELAGGKLG 130 140 150 160 170 180 SKEPVHPNDH VNMSQSSNDT FPTAMHITAA EMITHQLIPN LTVLRDTLEK KSKEFSEIIK 190 200 210 220 230 240 IGRTHLQDAV PLTLGQEFSG YVAQLNHNLE AINDVLPTLY RLALGGTAVG TGLNTHPQFA 250 260 270 280 290 300 KKAADHIAEL TGIPFYSASN KFAALAANDE IVLVSGVLKT LACSLMKIAN DIRWLASGPR 310 320 330 340 350 360 CGIGEIVIPE NEPGSSIMPG KVNPTQSEAM TMVCVQVIGN DTTITIAGSQ GNFELNVYKP 370 380 390 400 410 420 VMAYNLIQSI YLLSDACRSF NDHCAVGIKP NQEKINDYLN NSLMLVTALN QIIGYDKASE 430 440 450 IAKKAYKEGT TLKEAALQLG YLTASEFDKA VDPKKMVAI

References

[1]

"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016828 Genomic DNA. Translation: AAO90609.2.
RefSeq	NP_820095.2. NC_002971.3.
3D structure databases
ProteinModelPortal	Q83CL8.
SMR	Q83CL8. Positions 1-457.
ModBase	Search...
Protein-protein interaction databases
STRING	227377.CBU_1096.
Proteomic databases
PRIDE	Q83CL8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO90609; AAO90609; CBU_1096.
GeneID	1208998.
KEGG	cbu:CBU_1096.
PATRIC	17930925. VBICoxBur82552_1090.
Phylogenomic databases
eggNOG	COG0114.
HOGENOM	HOG000061736.
KO	K01679.
OMA	KDTMGEV.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	CBUR227377:GJ7S-1090-MONOMER.
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_COXBU

Accession

Primary (citable) accession number: Q83CL8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	May 1, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program