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Reviewed, UniProtKB/Swiss-Prot Q7VA47 (FUMC_PROMA)

Last modified November 3, 2009. Version 38. 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: Pro_1620
OrganismProchlorococcus marinus [Complete proteome] [HAMAP]
Taxonomic identifier1219 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length465 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 – 465465Fumarate hydratase class II HAMAP MF_00743
PRO_0000161296

Regions

Region130 – 1334B site By similarity
Region140 – 1423Substrate binding By similarity

Sites

Binding site1011Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VA47-1 [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: 12917486] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

AE017126 Genomic DNA. Translation: AAQ00664.1.
RefSeqNP_876011.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1463002.
GenomeReviewsGene locus Pro_1620 in contig AE017126_GR.
KEGGpma:Pro1620.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7VA47.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycPMAR167539:PRO_1620-MON.
BRENDA4.2.1.2. 141456.

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_PROMA
AccessionPrimary (citable) accession number: Q7VA47
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: November 3, 2009
This is version 38 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