Q7W0A2 (FUMC_BORPE) 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:	BP0248

Organism

Bordetella pertussis

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

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_0000161258
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)
	Q7W0A2 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: F3A3E9FE37BC9532	FASTA	463	49,506
	10 20 30 40 50 60 MKTRTEKDTF GPIEVPEQHL WGAQTQRSLH FFAISTEKMP VPLVAAMARL KRAAAKVNAE 70 80 90 100 110 120 LGELDPQVAD AIMRAADEVI AGKWPDEFPL SVWQTGSGTQ SNMNMNEVLA NRASELLGGE 130 140 150 160 170 180 RGEGRKVHPN DHVNRGQSSN DTFPTAMHVA AAVEVEHRVL PALKALRGTL AAKSAAFYDI 190 200 210 220 230 240 VKIGRTHLQD ATPLTLGQEI SGYVAQLDLA EQQIRATLAG LHQLAIGGTA VGTGLNAHPQ 250 260 270 280 290 300 FSAKVSAELA HDTGSAFVSA PNKFQALASH EALLFAHGAL KTLAAGLMKI ANDVRWLASG 310 320 330 340 350 360 PRSGLGEISI PENEPGSSIM PGKVNPTQCE AVTMLAAQVM GNDVAINVGG ASGNFELNVF 370 380 390 400 410 420 KPLVIHNFLQ SVRLLADGMV SFDKHCAAGI EPNRERITEL VERSLMLVTA LNPHIGYDKA 430 440 450 460 AQIAKKAHKE NLSLKEAALA LGHLTEAQFA EWVVPGDMTN ARR

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640411 Genomic DNA. Translation: CAE40628.1.
RefSeq	NP_879133.1. NC_002929.2.
3D structure databases
ProteinModelPortal	Q7W0A2.
SMR	Q7W0A2. Positions 4-458.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2664150.
GenomeReviews	Gene locus BP0248 in contig BX470248_GR.
KEGG	bpe:BP0248.
NMPDR	fig|257313.1.peg.213.
PATRIC	21153526. VBIBorPer7866_0270.
Phylogenomic databases
HOGENOM	HBG284369.
OMA	RIEKDTM.
PhylomeDB	Q7W0A2.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	BPER257313:BP0248-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_BORPE

Accession

Primary (citable) accession number: Q7W0A2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program