Q81SA0 (FUMC_BACAN) 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:	BA_1767, GBAA_1767, BAS1637

Organism

Bacillus anthracis [Reference proteome] [HAMAP]

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	462 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 – 462	462	Fumarate hydratase class II HAMAP-Rule MF_00743		PRO_0000161252
Regions
	Region	97 – 99	3	Substrate binding By similarity
	Region	127 – 130	4	B site By similarity
	Region	137 – 139	3	Substrate binding By similarity
	Region	185 – 186	2	Substrate binding By similarity
	Region	322 – 324	3	Substrate binding By similarity
Sites
	Active site	186	1	Proton donor/acceptor By similarity
	Active site	316	1	By similarity
	Binding site	317	1	Substrate By similarity
	Site	329	1	Important for catalytic activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81SA0 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 0FB897C31FAC981D	FASTA	462	50,345
	10 20 30 40 50 60 MEYRIERDTL GEIKVPADKL WAAQTQRSKE NFPIGTEQMP LEIVKAFAIL KKSAALSNQK 70 80 90 100 110 120 LGKLSEEKAE AIVVAADEII AGKWNEHFPL VVWQTGSGTQ SNMNVNEVIA NRGNQILKEK 130 140 150 160 170 180 GSDVHIHPND DVNMSQSSND TFPTALHVAC VLAVENHVLP AITKLKETLA EKVTAFEHII 190 200 210 220 230 240 KIGRTHLQDA TPLTLGQEIS GWHRMLEKTE RMIAESNTYM KELAIGGTAV GTGINAHPKF 250 260 270 280 290 300 GEMVSEEISQ FTGKQFISAP NKFHALTSHD EVVYTHGALK ALAADLMKIA NDVRWLASGP 310 320 330 340 350 360 RSGLGEIIIP ANEPGSSIMP GKVNPTQSEA LTMVVAQVMG NDATIGFAAS QGNFELNVFK 370 380 390 400 410 420 PVIAYNFLQS AHLLADAIVS FNDNCAVGIE ADEEIIKENV NRSLMLVTAL NPHIGYENAA 430 440 450 460 KIAKHAHKEG LTLKEAALQS GLLTEEQFNE IVDPKKMIAP KE

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'." Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A. J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP25681.1. AE017334 Genomic DNA. Translation: AAT30883.1. AE017225 Genomic DNA. Translation: AAT53954.1.
RefSeq	NP_844195.1. NC_003997.3. YP_018408.1. NC_007530.2. YP_027903.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81SA0.
SMR	Q81SA0. Positions 4-458.
ModBase	Search...
Protein-protein interaction databases
STRING	198094.BA_1767.
Protocols and materials databases
DNASU	1086574.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAP25681; AAP25681; BA_1767. AAT30883; AAT30883; GBAA_1767. AAT53954; AAT53954; BAS1637.
GeneID	1086574. 2818045. 2851297.
KEGG	ban:BA_1767. bar:GBAA_1767. bat:BAS1637.
Phylogenomic databases
eggNOG	COG0114.
HOGENOM	HOG000061736.
KO	K01679.
OMA	KDTMGEV.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	BANT260799:GJAJ-1708-MONOMER. BANT261594:GJ7F-1779-MONOMER.
UniPathway	UPA00223; UER01007.
Family and domain databases
Gene3D	1.10.275.10. 1 hit.
HAMAP	MF_00743. FumaraseC.
InterPro	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	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_BACAN

Accession

Primary (citable) accession number: Q81SA0
Secondary accession number(s): Q6I0I3, Q6KUE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program