Q8YB50 (FUMC_BRUME) 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:	BMEII1051

Organism

Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]

Taxonomic identifier

224914 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella melitensis › Brucella melitensis bv. 1

Protein attributes

Sequence length	463 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. HAMAP-Rule MF_00743
Subcellular location	Cytoplasm By similarity HAMAP-Rule 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-Rule MF_00743
Sequence similarities	Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
Sequence caution	The sequence AAL54293.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Molecular function	Lyase
Technical term	Allosteric enzyme 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-Rule MF_00743		PRO_0000161261
Regions
	Region	98 – 100	3	Substrate binding By similarity
	Region	129 – 132	4	B site By similarity
	Region	139 – 141	3	Substrate binding By similarity
	Region	187 – 188	2	Substrate binding By similarity
	Region	324 – 326	3	Substrate binding By similarity
Sites
	Active site	188	1	Proton donor/acceptor By similarity
	Active site	318	1	By similarity
	Binding site	319	1	Substrate By similarity
	Site	331	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8YB50 [UniParc]. Last modified December 15, 2003. Version 2. Checksum: C2F6DD271F19B4F8	FASTA	463	49,624
	10 20 30 40 50 60 MAATRTETDT FGPIDVPADR YWGAQTQRSL QNFRIGGERM PLPLVHALGV VKRAAAETNI 70 80 90 100 110 120 ALGKLDPVLG QVIAVAASEV IEGKLDDHFP LVVWQTGSGT QSNMNANEVI SNRAIELLGG 130 140 150 160 170 180 EMGSKKPIHP NDHVNMSQSS NDSFPTAIHI ATAVETVNRL YPALEHLTKA LKVKEEAFKD 190 200 210 220 230 240 IIKIGRTHTQ DATPVTLGQE FSGYRAALEY ARHRLEQSLA DVFLLAQGGT AVGTGLNAPV 250 260 270 280 290 300 GFDKGFAEAV SEITGLSFKT APNKFEALAS HGAVLNFHGS LNALAADLFK IANDIRFLGS 310 320 330 340 350 360 GPRSGLGELS LPENEPGSSI MPGKVNPTQA EAMTMVATQV FGNQTAVTVA ASQGHFELNV 370 380 390 400 410 420 FKPVIAYNVL QSIRLLSDTM VSFADHCVEG IEPNTARIKE LLERSLMLVT ALAPAIGYDN 430 440 450 460 AARIAKTAHK NGTTLREEAL ASGLVSEEDY DRLVRAERMI APQ

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008918 Genomic DNA. Translation: AAL54293.1. Different initiation.
PIR	AB3641.
RefSeq	NP_542029.2. NC_003318.1.
3D structure databases
ProteinModelPortal	Q8YB50.
SMR	Q8YB50. Positions 5-463.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8YB50. 1 interaction.
STRING	224914.BMEII1051.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL54293; AAL54293; BMEII1051.
GeneID	1198823.
KEGG	bme:BMEII1051.
PATRIC	17856895. VBIBruMel92729_3406.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000061736.
KO	K01679.
OMA	KDTMGEV.
ProtClustDB	PRK00485.
Enzyme and pathway databases
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_BRUME

Accession

Primary (citable) accession number: Q8YB50

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	December 15, 2003
Last modified:	May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program