Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7VR50 (FUMC_BLOFL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. 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:Bfl373
OrganismBlochmannia floridanus [Complete proteome] [HAMAP]
Taxonomic identifier203907 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia

Protein attributes

Sequence length448 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 – 448448Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161264

Regions

Region83 – 853Substrate binding By similarity
Region113 – 1164B site By similarity
Region123 – 1253Substrate binding By similarity
Region171 – 1722Substrate binding By similarity
Region308 – 3103Substrate binding By similarity

Sites

Active site1721Proton donor/acceptor By similarity
Active site3021 By similarity
Binding site3031Substrate By similarity
Site3151Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VR50 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: CDEC7863B7D10F2D

FASTA44849,649
        10         20         30         40         50         60 
MICNRLWGDQ TESSLKFFNI STEKMPWELI KALAQIKRVS AQVNYDLKLL DYERSQAIIA 

        70         80         90        100        110        120 
AVDEILSGNH KNEFPLSVWQ TGSGTQSNMN MNEVLANRAN ELLRKNQINI VVHPNDHVNK 

       130        140        150        160        170        180 
SQSSNDVFPS AMHIAAVVNL KTKLIPVIKL LQKTFLKKSI EFRNIIKIGR THLQDAIPLT 

       190        200        210        220        230        240 
LGQEISGWDF MLKNNTNHIQ STILDLSALA LGGTAVGTGF SAHVEYAERV VLGLSKLIHH 

       250        260        270        280        290        300 
SFFSAPNKFE SLSTCDAIVY SHGTLKGLAI SMMKIANDIR LLSSGPQCGL GELIIPANEP 

       310        320        330        340        350        360 
GSSIMPGKVN PTQCESMTMS CCQVMGNDLS ISLGGSSGQL QLNTYRPLII YNFLQSIRLL 

       370        380        390        400        410        420 
TDSIKNFHDY CIVGIRPKFK RIEKLLNKSL MLVTALSSHI GYDKSAQIAQ TAYLNGITLK 

       430        440 
AASIQSGYVT EKQFDDWVCP ENMIYPDM 

« Hide

References

[1]"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes."
Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248583 Genomic DNA. Translation: CAD83439.1.
RefSeqNP_878664.1. NC_005061.1.

3D structure databases

ProteinModelPortalQ7VR50.
SMRQ7VR50. Positions 4-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203907.Bfl373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD83439; CAD83439; Bfl373.
GeneID1499573.
KEGGbfl:Bfl373.
PATRIC31964347. VBICanBlo38691_0363.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMAMESFNIH.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycBFLO203907:GHF7-373-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_BLOFL
AccessionPrimary (citable) accession number: Q7VR50
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 74 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