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Q8XQE8 (FUMC_RALSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:RSp1279
ORF Names:RS05324
Encoded onPlasmid megaplasmid Rsp
OrganismRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum) [Complete proteome] [HAMAP]
Taxonomic identifier267608 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia

Protein attributes

Sequence length461 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
Plasmid
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 – 461461Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161303

Regions

Region97 – 993Substrate binding By similarity
Region128 – 1314B site By similarity
Region138 – 1403Substrate binding By similarity
Region186 – 1872Substrate binding By similarity
Region323 – 3253Substrate binding By similarity

Sites

Active site1871Proton donor/acceptor By similarity
Active site3171 By similarity
Binding site3181Substrate By similarity
Site3301Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XQE8 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 8A44D62B53EDE18B

FASTA46149,403
        10         20         30         40         50         60 
MTTRTERDTF GPIEVPADRL WGAQTQRSLQ NFDIAGDRMP RELIDALARI KRASAAVNQR 

        70         80         90        100        110        120 
LGLLPADKAN AVIAAADEVI AGKHPGEFPL VVWQTGSGTQ SNMNMNEVLA NRASELLGGE 

       130        140        150        160        170        180 
RGEARLVHPN DDVNRSQSSN DVFPTAMHVA AVTAITRHLL PSLRALRETL ARKAIDFDDI 

       190        200        210        220        230        240 
IKIGRTHLQD ATPLTLGQEF SGYAAQLQHS ETHLNAALPH LCELALGGTA VGTGLNAPAG 

       250        260        270        280        290        300 
YAEQVAAELA ALTGLPFVTS PNKFETMASA DGLVHAHGAL KTLAASLTKI ANDIRWLASG 

       310        320        330        340        350        360 
PRSGLGELSI PENEPGSSIM PGKVNPTQSE AMTMLCAQVF GNDVAVNIGG ASGNFELNVF 

       370        380        390        400        410        420 
RPMIAYNFLH SARLLADGMR SFNDHCAVGI EPNRERIAEL VQRSLMLVTA LNPHIGYDKS 

       430        440        450        460 
AQIAKKAHKE GTSLREAALA LGYVTAEQFD AWVRPEQMVG R 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL646053 Genomic DNA. Translation: CAD18430.1.
RefSeqNP_522838.1. NC_003296.1.

3D structure databases

ProteinModelPortalQ8XQE8.
SMRQ8XQE8. Positions 4-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267608.RSp1279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD18430; CAD18430; RSp1279.
GeneID1223591.
KEGGrso:RSp1279.
PATRIC20268209. VBIRalSol70888_4772.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAMESFNIH.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycRSOL267608:GCVU-4788-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_RALSO
AccessionPrimary (citable) accession number: Q8XQE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 80 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