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Q7V5R2 (FUMC_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 72. 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:PMT_1485
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length466 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 – 466466Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161297

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
Q7V5R2 [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 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE21660.1.
RefSeqNP_895312.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V5R2.
SMRQ7V5R2. Positions 6-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT1485.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE21660; CAE21660; PMT_1485.
GeneID1728513.
KEGGpmt:PMT1485.
PATRIC23011523. VBIProMar135351_1905.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

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_PROMM
AccessionPrimary (citable) accession number: Q7V5R2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: March 19, 2014
This is version 72 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