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Reviewed, UniProtKB/Swiss-Prot Q7V5R2 (FUMC_PROMM)

Last modified November 3, 2009. Version 39. 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: PMT_1485
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle. HAMAP MF_00743

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

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 termComplete proteome
Gene Ontology (GO)
   Biological processtricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 466466Fumarate hydratase class II HAMAP MF_00743
PRO_0000161297

Regions

Region131 – 1344B site By similarity
Region141 – 1433Substrate binding By similarity

Sites

Binding site1021Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V5R2-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 395908D8DD84B12D

FASTA46650,233
        10         20         30         40         50         60 
MMADLMRIEH DSMGTIEVPA GVLWGAQTQR SLLNFAISTD RMPVELIHAL ALIKQAAASV 

        70         80         90        100        110        120 
NCRLGVLDEV QRDQIIKAAS AVASGLHDDQ FPLRVWQTGS GTHTNMNVNE VISNLASQAN 

       130        140        150        160        170        180 
DEPLGSHRPV HPNDHVNRSQ STNDAFPTAI HIAAVQGITN NLLPELEQLI AAFARKSDAW 

       190        200        210        220        230        240 
SDIIKIGRTH LQDAVPLTLG QEASAWRDQI ASAHSRIQSS LIELYPLPLG GTAVGTGLNA 

       250        260        270        280        290        300 
PARFGQETAA QLASITGLPF SSAKNKFAVM ASHDGLVNAM AQLRMLAVAL FKISNDLRLL 

       310        320        330        340        350        360 
ACGPRAGLAE LHLPENEPGS SIMPGKVNPS QCEAMAMVCL QVIGLDSAVT MAGGSGHLQM 

       370        380        390        400        410        420 
NVYKPLIGFN LLHSIELLHD ACRKYRLAMV QGIEPNRIKI QHDLEQSLML VTALAPEIGY 

       430        440        450        460 
DKASEIAHLA HEKGFSLREA ALKLGYVSKE DFDRIVNPAL MTSARL 

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References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

BX548175 Genomic DNA. Translation: CAE21660.1.
RefSeqNP_895312.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ7V5R2.

Genome annotation databases

GeneID1728513.
GenomeReviewsGene locus PMT_1485 in contig BX548175_GR.
KEGGpmt:PMT1485.
NMPDRfig|74547.1.peg.1479.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7V5R2.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycPMAR74547:PMT1485-MON.

Family and domain databases

HAMAPMF_00743.
[Tree]
InterProIPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_PROMM
AccessionPrimary (citable) accession number: Q7V5R2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: November 3, 2009
This is version 39 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