P71384 (FUMC_HAEIN) 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:	HI_1398

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

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

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. 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.

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 – 464	464	Fumarate hydratase class II HAMAP-Rule MF_00743		PRO_0000161279
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)
	P71384 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: AC836336DA7457CE	FASTA	464	50,482
	10 20 30 40 50 60 MAFRIEKDTM GEVQVLADKY WAAQTERSRN NFKIGPAASM PHEIIEAFGY LKKAAAFANH 70 80 90 100 110 120 DLGVLPLEKR DLIALACDEI LANKLDDQFP LVIWQTGSGT QSNMNVNEVV ANRAHVLNGG 130 140 150 160 170 180 KLGEKSIIHP NDDVNKSQSS NDTFPTAMHI AAYKKVVEHT IPCVERLQKT FAAKSEAFKN 190 200 210 220 230 240 VVKIGRTHLM DATPLTLGQE FSAYAAQLDF GLKALKNTLP HLSQLALGGT AVGTGLNTPK 250 260 270 280 290 300 GYDLKVVDYI AKFTALPFVT ADNKFEALAA HDAIVETHGA LRQLAMSLFK IANDIRLLAS 310 320 330 340 350 360 GPRSGIGEIL IPENEPGSSI MPGKVNPTQC EXMTMVCAQV FGNDTTIAFV GSQGHFQLNV 370 380 390 400 410 420 FNPVMIANFL QSAQLLGDAC VSFDEHCAVG IEPNYPRIKQ QLENSLMLVT ALNTHIGYEN 430 440 450 460 AAKIAKTAHK NGTTLREEAI NLGLVSAEDF DKWVRPEDMV GSLK

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC23045.1.
RefSeq	NP_439551.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P71384.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI1398.
Proteomic databases
PRIDE	P71384.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC23045; AAC23045; HI_1398.
GeneID	950314.
KEGG	hin:HI1398.
PATRIC	20191495. VBIHaeInf48452_1458.
Phylogenomic databases
eggNOG	COG0114.
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	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_HAEIN

Accession

Primary (citable) accession number: P71384

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program