Reviewed, UniProtKB/Swiss-Prot Q68W74 (FUMC_RICTY)

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:	RT0657

Organism

Rickettsia typhi [Complete proteome] [HAMAP]

Taxonomic identifier

785 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group

Protein attributes

Sequence length	461 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 – 461	461	Fumarate hydratase class II HAMAP MF_00743		PRO_0000278001
Regions
	Region	129 – 132	4	B site By similarity
	Region	139 – 141	3	Substrate binding By similarity
Sites
	Binding site	100	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q68W74-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 46A16449E3DE705C	FASTA	461	51,014
	10 20 30 40 50 60 MKNYRIESDS FGEIQIEEKF YWGAQTQRSL NNFKISKQKM PKILIHALAI LKKCAAQVNY 70 80 90 100 110 120 EFGDLEYKIA TSIDKAIDRI LAGEFEDNFP LVVWQTGSGT QTNMNMNEVI ASIANEELTG 130 140 150 160 170 180 KKGGKSPVHP NDHVNKGQSS NDSFPTAMHI ATVLATKQQL IPALNNLLTY LQDKSKDWDK 190 200 210 220 230 240 IIKIGRTHLQ DATPLTLKQE FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSKI 250 260 270 280 290 300 GFDIKFAEKV AEFTQQPFKT APNKFESLAA HDALVEFSGT LNTISVSLMK IANDIRLLGS 310 320 330 340 350 360 GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA GSNGHLELNV 370 380 390 400 410 420 FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIERINA LRDKSLMLVT VLNPHIGYDN 430 440 450 460 AAKIAKEAYK YGITLKEAAK KLNFLSEEEF DKIVIPEKMI S

References

[1]

"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae." McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. , Hong C., Yu X.-J., Walker D.H., Weinstock G.M. J. Bacteriol. 186:5842-5855(2004) [PubMed: 15317790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017197 Genomic DNA. Translation: AAU04118.1.
RefSeq	YP_067600.1.
3D structure databases
HSSP	HSSP built from PDB template 1YFM based on UniProtKB P08417.
SMR	Q68W74. Positions 4-460.
ModBase	Search...
Genome annotation databases
GeneID	2959051.
GenomeReviews	Gene locus RT0657 in contig AE017197_GR.
KEGG	rty:RT0657.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG284369.
OMA	HEFGDLE.
Enzyme and pathway databases
BioCyc	RTYP257363:RT0657-MONOMER.
BRENDA	4.2.1.2. 281221.
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_RICTY

Accession

Primary (citable) accession number: Q68W74

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	October 11, 2004
Last modified:	February 9, 2010
This is version 40 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)