Q7VKC9 (FUMC_HAEDU) 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:	HD_1986

Organism

Haemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]

Taxonomic identifier

233412 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus ducreyi

Protein attributes

Sequence length	464 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
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 – 464	464	Fumarate hydratase class II HAMAP-Rule MF_00743		PRO_0000161278
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)
	Q7VKC9 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 7FC2E242353C1DEC	FASTA	464	50,483
	10 20 30 40 50 60 MEYRIEKDTM GEVKVPADRY WAAQTERSRN NFRIGPEASM PVEIIEAFAY LKKAAAFANA 70 80 90 100 110 120 ELGALTTEKR DLIAMVCDEI LANKLADEFP LVIWQTGSGT QSNMNLNEVI ANRAHVLQGG 130 140 150 160 170 180 ALGEKSIIHP NDDVNKSQSS NDTYPTAMHI AAYKKVVEVT IPAIERLQKT FAIKSEAFKD 190 200 210 220 230 240 VVKIGRTHLM DATPLTLGQE FSAYAAQLQF GLLALKNTLP HLAQLALGGT AVGTGLNTPK 250 260 270 280 290 300 GYDVKVAEYI AQFTQLPFIT AENKFEALAT HDAIIETHGA LKQIAMSLFK IANDIRLLAS 310 320 330 340 350 360 GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EAMTMVAAQV LGNDTTISFA GSQGHFQLNV 370 380 390 400 410 420 FKPVMAANFL QSAQLLADVC ISFDEHCASG IEPNYPRIQQ QLENSLMLVT ALNTHIGYEN 430 440 450 460 AAKIAKTAHK NGTTLKEEAI NLGLVTAEQF DQWVRPQNMV GSLK

References

[1]

"The complete genome sequence of Haemophilus ducreyi." Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017143 Genomic DNA. Translation: AAP96703.1.
RefSeq	NP_874314.1. NC_002940.2.
3D structure databases
ProteinModelPortal	Q7VKC9.
SMR	Q7VKC9. Positions 4-460.
ModBase	Search...
Protein-protein interaction databases
STRING	233412.HD1986.
Proteomic databases
PRIDE	Q7VKC9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAP96703; AAP96703; HD_1986.
GeneID	1491818.
KEGG	hdu:HD1986.
PATRIC	20180098. VBIHaeDuc133973_1664.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0114.
KO	K01679.
OMA	KDTMGEV.
ProtClustDB	PRK00485.
Enzyme and pathway databases
BioCyc	HDUC233412:GH5F-1727-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_HAEDU

Accession

Primary (citable) accession number: Q7VKC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program