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Q8Z6R6 (FUMC_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate hydratase class II

Short name=Fumarase C
EC=4.2.1.2
Gene names
Name:fumC
Ordered Locus Names:STY1653, t1337
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161308

Regions

Region98 – 1003Substrate binding By similarity
Region129 – 1324B site By similarity
Region139 – 1413Substrate binding By similarity
Region187 – 1882Substrate binding By similarity
Region324 – 3263Substrate binding By similarity

Sites

Active site1881Proton donor/acceptor By similarity
Active site3181 By similarity
Binding site3191Substrate By similarity
Site3311Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Z6R6 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 4D5E53A59EAE28F9

FASTA46750,216
        10         20         30         40         50         60 
MVTVRREKDS MGVIEVPADK LWGAQTQRSL EHFRISTEKM PVSLIHALAL TKRAAAKVNQ 

        70         80         90        100        110        120 
DLGLLAAEKA SAIIEAADEV LAGKHADEFP LAIWQTGSGT QSNMNMNEVL ANRASEILGG 

       130        140        150        160        170        180 
VRGMERKVHP NDDVNKSQSS NDVFPTAMHV AALLALREHL IPQLSALTDT LRDKSHAFAD 

       190        200        210        220        230        240 
IVKIGRTHLQ DATPLTLGQE ISGWVAMLEH NLRHIEHSLP HVAELALGGT AVGTGLNTHP 

       250        260        270        280        290        300 
EYARRVAEEL ATITAAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS 

       310        320        330        340        350        360 
GPRCGIGEIA IPENEPGSSI MPGKVNPTQC EAVTMLCCQV MGNDVAINMG GASGNFELNV 

       370        380        390        400        410        420 
YRPMVIHNFL QTVRLLADGM ASFNQHCASG IEPNRERITQ LLNESLMLVT ALNTHIGYDK 

       430        440        450        460 
AAEIAKKAHK EGLTLKASAV ALGYLSDAEF DAWVRPELMV GSMTPGR 

« Hide

References

[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL513382 Genomic DNA. Translation: CAD01898.1.
AE014613 Genomic DNA. Translation: AAO68985.1.
RefSeqNP_456063.1. NC_003198.1.
NP_805136.1. NC_004631.1.

3D structure databases

ProteinModelPortalQ8Z6R6.
SMRQ8Z6R6. Positions 4-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220341.STY1653.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO68985; AAO68985; t1337.
CAD01898; CAD01898; CAD01898.
GeneID1248027.
PATRIC18541200. VBISalEnt120419_1664.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_SALTI
AccessionPrimary (citable) accession number: Q8Z6R6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways