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Reviewed, UniProtKB/Swiss-Prot Q7VR50 (FUMC_BLOFL)

Last modified February 9, 2010. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP MF_00743

Subunit structure

Homotetramer By similarity. HAMAP MF_00743

Subcellular location

Cytoplasm By similarity HAMAP 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. HAMAP MF_00743

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Fumarate hydratase class II HAMAP MF_00743
PRO_0000161264

Regions

Region113 – 1164B site By similarity
Region123 – 1253Substrate binding By similarity

Sites

Binding site851Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VR50-1 [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 

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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: 12886019] [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.

3D structure databases

SMRQ7VR50. Positions 4-444.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7VR50.

Genome annotation databases

GeneID1499573.
GenomeReviewsGene locus Bfl373 in contig BX248583_GR.
KEGGbfl:Bfl373.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHBG284369.
OMARIEKDTM.
PhylomeDBQ7VR50.

Enzyme and pathway databases

BioCycCBLO203907:BFL373-MONOMER.

Family and domain databases

HAMAPMF_00743. FumaraseC.
[Tree]
InterProIPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
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: February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents