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Q81F85 (FUMC_BACCR) 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:BC_1712
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length462 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 – 462462Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161253

Regions

Region97 – 993Substrate binding By similarity
Region127 – 1304B site By similarity
Region137 – 1393Substrate binding By similarity
Region185 – 1862Substrate binding By similarity
Region322 – 3243Substrate binding By similarity

Sites

Active site1861Proton donor/acceptor By similarity
Active site3161 By similarity
Binding site3171Substrate By similarity
Site3291Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81F85 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D87CF7C737840676

FASTA46250,347
        10         20         30         40         50         60 
MEYRIERDTL GEIKVPADKL WAAQTQRSKE NFPIGTEQMP LEIVKAFAIL KKSAALSNQK 

        70         80         90        100        110        120 
LGKLSEEKAE AIVEAADEVI AGKWNEHFPL VVWQTGSGTQ SNMNVNEVIA NRGNQILKEK 

       130        140        150        160        170        180 
GSDVHIHPND DVNMSQSSND TFPTALHVAC VIAVENHVLP AITKLKETLV EKVTAFEHII 

       190        200        210        220        230        240 
KIGRTHLQDA TPLTLGQEIS GWHRMLEKTE RMIAESNTYM KELAIGGTAV GTGINAHPKF 

       250        260        270        280        290        300 
GEMVSEEISQ FTGKQFVSAP NKFHALTSHD EVVYTHGALK ALAADLMKIA NDVRWLASGP 

       310        320        330        340        350        360 
RSGLGEIIIP ANEPGSSIMP GKVNPTQSEA LTMVVAQVMG NDATIGFAAS QGNFELNVFK 

       370        380        390        400        410        420 
PVIAYNFLQS AHLLADAIVS FNDNCAVGIE ADEEVINENV NRSLMLVTAL NPHIGYENAA 

       430        440        450        460 
KIAKHAHKEG LTLKEAALQS GLLTEEQFDE IVDPKKMIAP KE 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP08688.1.
RefSeqNP_831487.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ81F85.
SMRQ81F85. Positions 4-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING226900.BC1712.

Proteomic databases

PRIDEQ81F85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP08688; AAP08688; BC_1712.
GeneID1204061.
KEGGbce:BC1712.
PATRIC32599183. VBIBacCer54481_1700.

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMAIAFNDNC.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycBCER226900:GJEU-1712-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_BACCR
AccessionPrimary (citable) accession number: Q81F85
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
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