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Protein

Fumarate hydratase, mitochondrial

Gene

fum1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathway:itricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.
Proteins known to be involved in this subpathway in this organism are:
  1. Fumarate hydratase, mitochondrial (fum1)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei155 – 1551SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_276964. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase, mitochondrial (EC:4.2.1.2)
Short name:
Fumarase
Gene namesi
Name:fum1
ORF Names:SPCC18.18c, SPCC290.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC18.18c.
PomBaseiSPCC18.18c. fum1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • mitochondrial matrix Source: PomBase
  • tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3939MitochondrionSequence AnalysisAdd
BLAST
Chaini40 – 520481Fumarate hydratase, mitochondrialPRO_0000010332Add
BLAST

Proteomic databases

MaxQBiO94552.
PaxDbiO94552.

Interactioni

Protein-protein interaction databases

BioGridi275911. 1 interaction.
MINTiMINT-4685155.

Structurei

3D structure databases

ProteinModelPortaliO94552.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 1874B siteBy similarity
Regioni194 – 1963Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiO94552.
KOiK01679.
OMAiIEKDTMG.
OrthoDBiEOG73NGC9.
PhylomeDBiO94552.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O94552-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVAHISTA KAIFRAGGLP CRRLITPTLT GLPLKTHRMN STTPTYHLIP
60 70 80 90 100
KGGKHGEFRQ ESDTFGPIQV PAEKYWGAQT QRSLQNFRIG GEKERLPLPL
110 120 130 140 150
VRAFGVLKRA AASVNREFGL DPKLADAIEQ AAQEVIDGRL DDNFPLVVFQ
160 170 180 190 200
TGSGTQSNMN SNEVIANRAI EILGGTLGSK KPVHPNDHVN MSQSSNDTFP
210 220 230 240 250
TVMHIASVLQ IHTHLLPAMK HLHRALKGKE EEFKNIIKIG RTHMQDATPL
260 270 280 290 300
SLGQEFSGYV TQVGYGIERI NNALPRLCLL AQGGTAVGTG LNTFEGFDVK
310 320 330 340 350
VAEKVSKLTN IEFKTAPNKF EALAAHDAIV EMSGALNVIA CSLMKIANDI
360 370 380 390 400
RQLGSGPRCG LGELILPANE PGSSIMPGKV NPTQCEALTM VCAQVMGNHA
410 420 430 440 450
TITVAGASGH CELNVFKPLL AKNILSSIRL LGDACESFTD HCVVGIEPNY
460 470 480 490 500
EGIARHLRDS LMLVTALNPH IGYDNCAKIA KTALKNKSTL KHEFVTLGFG
510 520
TPEQFDEWVR PELMISAKKV
Length:520
Mass (Da):56,322
Last modified:September 22, 2009 - v3
Checksum:i4AF0DA8BF5E14AE8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21432.3.
PIRiT41265.
RefSeqiNP_588397.3. NM_001023388.3.

Genome annotation databases

EnsemblFungiiSPCC18.18c.1; SPCC18.18c.1:pep; SPCC18.18c.
GeneIDi2539345.
KEGGispo:SPCC18.18c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA21432.3.
PIRiT41265.
RefSeqiNP_588397.3. NM_001023388.3.

3D structure databases

ProteinModelPortaliO94552.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275911. 1 interaction.
MINTiMINT-4685155.

Proteomic databases

MaxQBiO94552.
PaxDbiO94552.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC18.18c.1; SPCC18.18c.1:pep; SPCC18.18c.
GeneIDi2539345.
KEGGispo:SPCC18.18c.

Organism-specific databases

EuPathDBiFungiDB:SPCC18.18c.
PomBaseiSPCC18.18c. fum1.

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiO94552.
KOiK01679.
OMAiIEKDTMG.
OrthoDBiEOG73NGC9.
PhylomeDBiO94552.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
ReactomeiREACT_276964. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi20800510.
PROiO94552.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. 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]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiFUMH_SCHPO
AccessioniPrimary (citable) accession number: O94552
Secondary accession number(s): O74868
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: September 22, 2009
Last modified: July 22, 2015
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.