Reviewed, UniProtKB/Swiss-Prot Q7W4N9 (FUMC_BORPA)

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:	BPP3619

Organism

Bordetella parapertussis [Complete proteome] [HAMAP]

Taxonomic identifier

519 [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
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 MF_00743		PRO_0000161257
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)
	Q7W4N9-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 8D96DAFACB625AE1	FASTA	463	49,491
	10 20 30 40 50 60 MKTRTEKDTF GPIEVPEQHL WGAQTQRSLH FFAISTEKMP VPLVAAMARL KRAAAKVNAE 70 80 90 100 110 120 LGELDPQVAD AIMRAADEVV 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: 12822 / ATCC BAA-587 / NCTC 13253.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640434 Genomic DNA. Translation: CAE38903.1.
RefSeq	NP_885778.1.
3D structure databases
SMR	Q7W4N9. Positions 4-458.
ModBase	Search...
Genome annotation databases
GeneID	1666559.
KEGG	bpa:BPP3619.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284369.
OMA	RIEKDTM.
PhylomeDB	Q7W4N9.
Enzyme and pathway databases
BioCyc	BPAR257311:BPP3619-MONOMER.
BRENDA	4.2.1.2. 263123.
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. [Graphical view]
Pfam	PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view]
PRINTS	PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE.
TIGRFAMs	TIGR00979. fumC_II. 1 hit.
PROSITE	PS00163. FUMARATE_LYASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FUMC_BORPA

Accession

Primary (citable) accession number: Q7W4N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)