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O94552 (FUMH_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fumarate hydratase, mitochondrial

Short name=Fumarase
EC=4.2.1.2
Gene names
Name:fum1
ORF Names:SPCC18.18c, SPCC290.01c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

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

Subcellular location

Mitochondrion Potential 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion Potential
Chain40 – 520481Fumarate hydratase, mitochondrial HAMAP-Rule MF_00743
PRO_0000010332

Regions

Region184 – 1874B site By similarity
Region194 – 1963Substrate binding By similarity

Sites

Binding site1551Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O94552 [UniParc].

Last modified September 22, 2009. Version 3.
Checksum: 4AF0DA8BF5E14AE8

FASTA52056,322
        10         20         30         40         50         60 
MASVAHISTA KAIFRAGGLP CRRLITPTLT GLPLKTHRMN STTPTYHLIP KGGKHGEFRQ 

        70         80         90        100        110        120 
ESDTFGPIQV PAEKYWGAQT QRSLQNFRIG GEKERLPLPL VRAFGVLKRA AASVNREFGL 

       130        140        150        160        170        180 
DPKLADAIEQ AAQEVIDGRL DDNFPLVVFQ TGSGTQSNMN SNEVIANRAI EILGGTLGSK 

       190        200        210        220        230        240 
KPVHPNDHVN MSQSSNDTFP TVMHIASVLQ IHTHLLPAMK HLHRALKGKE EEFKNIIKIG 

       250        260        270        280        290        300 
RTHMQDATPL SLGQEFSGYV TQVGYGIERI NNALPRLCLL AQGGTAVGTG LNTFEGFDVK 

       310        320        330        340        350        360 
VAEKVSKLTN IEFKTAPNKF EALAAHDAIV EMSGALNVIA CSLMKIANDI RQLGSGPRCG 

       370        380        390        400        410        420 
LGELILPANE PGSSIMPGKV NPTQCEALTM VCAQVMGNHA TITVAGASGH CELNVFKPLL 

       430        440        450        460        470        480 
AKNILSSIRL LGDACESFTD HCVVGIEPNY EGIARHLRDS LMLVTALNPH IGYDNCAKIA 

       490        500        510        520 
KTALKNKSTL KHEFVTLGFG TPEQFDEWVR PELMISAKKV 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAA21432.3.
PIRT41265.
RefSeqNP_588397.3. NM_001023388.3.

3D structure databases

ProteinModelPortalO94552.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid275911. 1 interaction.
MINTMINT-4685155.
STRING4896.SPCC18.18c-1.

Proteomic databases

PaxDbO94552.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC18.18c.1; SPCC18.18c.1:pep; SPCC18.18c.
GeneID2539345.
KEGGspo:SPCC18.18c.

Organism-specific databases

PomBaseSPCC18.18c.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMARIEKDTM.
OrthoDBEOG73NGC9.
PhylomeDBO94552.

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...

Other

NextBio20800510.
PROO94552.

Entry information

Entry nameFUMH_SCHPO
AccessionPrimary (citable) accession number: O94552
Secondary accession number(s): O74868
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways