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O66271 (FUMC_THET2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. 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:TT_C0190
OrganismThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP]
Taxonomic identifier262724 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length466 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 – 466466Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161327

Regions

Region99 – 1013Substrate 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

Experimental info

Sequence conflict341I → F in BAA25700. Ref.1
Sequence conflict2381A → G in BAA25700. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O66271 [UniParc].

Last modified May 24, 2004. Version 2.
Checksum: C0ED1307333A65A8

FASTA46650,882
        10         20         30         40         50         60 
MEYRIERDTM GEVRVPADKY WGAQTQRSLE NFRIGTDRFR MPLEIIRAYG MLKKAAARAN 

        70         80         90        100        110        120 
LELGELPEEI AKAIIQAAEE VVQGKWDDHF PLVVFQTGSG TQTNMNVNEV IANRASEILG 

       130        140        150        160        170        180 
KPLGSKYVHP NDHVNRGQSS NDTFPTAMYV AVALALHQRL YPAVEGLIRT FTAKAQAFDQ 

       190        200        210        220        230        240 
IVKVGRTHLM DAVPITLGQE IGSWAAQLKT TLAAVKEMEK GLYNLAIGGT AVGTGLNAHP 

       250        260        270        280        290        300 
RFGELVAKYL AEETGLPFRV AENRFAALAA HDELVNVMGA IRTLAGALMK IGNDVRWLAS 

       310        320        330        340        350        360 
GPYAGIGEIT IPANEPGSSI MPGKVNPTQV EALTMVVVRV YGNDHTVAFA GSQGNFQLNV 

       370        380        390        400        410        420 
YKPVMAYSTL ESINLLADAV ASFDAHLAQG IEPNLERIEE HLQKNPMLAT ALNKAIGYDK 

       430        440        450        460 
AAEIVKKALK EKKTLKQAAL ELGYLTEEEF DRIVVPMRLA KPHEGA 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequence analysis of the fumC and sodA genes from an extremely thermophilic eubacterium Thermus thermophilus."
Kosuge T., Umehara K., Matsuura S., Hoshino T.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of the extreme thermophile Thermus thermophilus."
Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.
Nat. Biotechnol. 22:547-553(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB27 / ATCC BAA-163 / DSM 7039.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB010884 Genomic DNA. Translation: BAA25700.1.
AE017221 Genomic DNA. Translation: AAS80538.1.
PIRT43727.
RefSeqYP_004165.1. NC_005835.1.

3D structure databases

ProteinModelPortalO66271.
SMRO66271. Positions 4-463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262724.TTC0190.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS80538; AAS80538; TT_C0190.
GeneID2774678.
KEGGtth:TTC0190.
PATRIC23950773. VBITheThe54392_0191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMAGYLEAKI.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycTTHE262724:GCAT-194-MONOMER.
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_THET2
AccessionPrimary (citable) accession number: O66271
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: May 24, 2004
Last modified: May 14, 2014
This is version 88 of the entry and version 2 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