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Q9RR70 (FUMC_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 90. 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:DR_2627
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length464 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
Reference 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 – 464464Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161274

Regions

Region100 – 1023Substrate binding By similarity
Region131 – 1344B site By similarity
Region141 – 1433Substrate binding By similarity
Region189 – 1902Substrate binding By similarity
Region326 – 3283Substrate binding By similarity

Sites

Active site1901Proton donor/acceptor By similarity
Active site3201 By similarity
Binding site3211Substrate By similarity
Site3331Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RR70 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6CE8DC9A8D90A07E

FASTA46449,876
        10         20         30         40         50         60 
MTKTRQETDT MGKMDVDASR YWGAQTERSI HNFPIGRDTF VWGRPVIRAL GILKKGAAQA 

        70         80         90        100        110        120 
NAELGELPAD VADLIVKAAD EVIAGKLDEH FPLVVFQTGS GTQSNMNANE VISNRAIELA 

       130        140        150        160        170        180 
GGEMGSKKPV HPNDHVNRGQ SSNDTFPTAM HIAVVLELNE RLYGAVGKLR DTLHAKAEQY 

       190        200        210        220        230        240 
KDLVKVGRTH LQDATPITLG QEIGGWVAQL DYALSEVKHA GEGLLDLAIG GTAVGTGLNA 

       250        260        270        280        290        300 
HPKFGDLAAK KYEEETGYHF RSAENKFAAL SAHDALVQTS AALRTLAGAL MKMANDVRWL 

       310        320        330        340        350        360 
ASGPRNGIGE ITIPENEPGS SIMPGKVNPT QSEAMTMVAT RVFGNDATVA FAGSQGNFQL 

       370        380        390        400        410        420 
NVFKPVMVHA VLESIRLISD ACLAFNDHCA VGIQPNEAKI KENLDKNLMQ VTALNRHIGY 

       430        440        450        460 
DKAAAIAKKA HKEGTSLKDA ALALGYVTED EFAQWVVPLG MTHN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF12164.1.
PIRB75250.
RefSeqNP_296346.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RR70.
SMRQ9RR70. Positions 5-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_2627.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF12164; AAF12164; DR_2627.
GeneID1797634.
KEGGdra:DR_2627.
PATRIC21633009. VBIDeiRad64572_2875.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAMESFNIH.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycDRAD243230:GH46-2682-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_DEIRA
AccessionPrimary (citable) accession number: Q9RR70
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 90 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