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Q7VA47 (FUMC_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:Pro_1620
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length465 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 – 465465Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161296

Regions

Region99 – 1013Substrate binding By similarity
Region130 – 1334B site By similarity
Region140 – 1423Substrate binding By similarity
Region188 – 1892Substrate binding By similarity
Region325 – 3273Substrate binding By similarity

Sites

Active site1891Proton donor/acceptor By similarity
Active site3191 By similarity
Binding site3201Substrate By similarity
Site3321Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VA47 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F2F17242168FDA54

FASTA46551,045
        10         20         30         40         50         60 
MAQSFRIEND SMGTIKVPDQ ALWGAQTQRS LINFAIGHNK MPMKLIYSIV QIKASAAIVN 

        70         80         90        100        110        120 
CRLGVLDKQR KNFILNACNE ISNGMHDEQF PLSVWQTGSG TQTNMNVNEV ISNIASHLNG 

       130        140        150        160        170        180 
NKLGSHEPLH PNDHVNRSQS TNDVFPAAIQ IATVQEILEN LLPELDQLIE TFDKKIIKWN 

       190        200        210        220        230        240 
RIIKTGRTHL QDAVPLTLGQ EASAWKEQLI ASRNRLNKSL NELYPLPLGG TAIGTGLNAP 

       250        260        270        280        290        300 
AKFDKEIALE IAKSTRSPFV SAQNKFAIMA SHDALVHTMS QLKLLAVSLF KIVNDLRLLS 

       310        320        330        340        350        360 
CGPRGGLGEL RLPENEPGSS IMPGKVNPTQ CEAMAMVCTQ IMALDSAVTM AGSGGHLQMN 

       370        380        390        400        410        420 
SYKPLIAFNL LESIDLLSSA CKSSRILMIE GIEPNLEKIQ NSLQNSLMLI TSLTPIIGYE 

       430        440        450        460 
KASKIAQCAH EKDITLKEAT KLLGYLNEDD FDRIVNPQSM TGMEN 

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAQ00664.1.
RefSeqNP_876011.1. NC_005042.1.

3D structure databases

ProteinModelPortalQ7VA47.
SMRQ7VA47. Positions 4-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro1620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAQ00664; AAQ00664; Pro_1620.
GeneID1463002.
KEGGpma:Pro_1620.
PATRIC23030061. VBIProMar8617_1712.

Phylogenomic databases

eggNOGCOG0114.
KOK01679.
OMAMESFNIH.
OrthoDBEOG6V1M4M.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-1656-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.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_PROMA
AccessionPrimary (citable) accession number: Q7VA47
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 69 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