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P08417

- FUMH_YEAST

UniProt

P08417 - FUMH_YEAST

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Protein

Fumarate hydratase, mitochondrial

Gene
FUM1, YPL262W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei126 – 1261Substrate By similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: SGD

GO - Biological processi

  1. fumarate metabolic process Source: SGD
  2. tricarboxylic acid cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciYEAST:YPL262W-MONOMER.
BRENDAi4.2.1.2. 984.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase, mitochondrial (EC:4.2.1.2)
Short name:
Fumarase
Gene namesi
Name:FUM1
Ordered Locus Names:YPL262W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPL262w.
SGDiS000006183. FUM1.

Subcellular locationi

Mitochondrion matrix. Cytoplasm
Note: Both fumarases are encoded by a single nuclear gene.1 Publication

GO - Cellular componenti

  1. cytosol Source: SGD
  2. mitochondrial matrix Source: SGD
  3. mitochondrion Source: SGD
  4. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 488Fumarate hydratase, mitochondrialUniRule annotationPRO_0000010333
Transit peptidei1 – ?MitochondrionUniRule annotation

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei428 – 4281Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP08417.
PaxDbiP08417.
PeptideAtlasiP08417.

Expressioni

Gene expression databases

GenevestigatoriP08417.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi35951. 152 interactions.
DIPiDIP-6451N.
IntActiP08417. 3 interactions.
MINTiMINT-606236.
STRINGi4932.YPL262W.

Structurei

Secondary structure

1
488
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 314
Beta strandi33 – 353
Beta strandi38 – 436
Helixi48 – 547
Helixi61 – 644
Helixi68 – 8720
Helixi93 – 10715
Helixi112 – 1143
Beta strandi118 – 1214
Helixi126 – 14217
Helixi155 – 1595
Turni160 – 1623
Helixi165 – 18218
Helixi185 – 20218
Turni203 – 2053
Beta strandi207 – 2126
Beta strandi215 – 2217
Helixi222 – 24726
Turni255 – 2573
Helixi267 – 27913
Helixi289 – 2946
Helixi297 – 32327
Beta strandi327 – 3304
Helixi353 – 37725
Helixi387 – 41125
Helixi413 – 4153
Helixi420 – 42910
Helixi432 – 4343
Turni435 – 4373
Helixi438 – 4403
Helixi443 – 45614
Helixi460 – 4667
Helixi472 – 4787
Helixi481 – 4833

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YFMX-ray2.60A1-488[»]
ProteinModelPortaliP08417.
SMRiP08417. Positions 27-485.

Miscellaneous databases

EvolutionaryTraceiP08417.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 1663Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0114.
GeneTreeiENSGT00390000002779.
HOGENOMiHOG000061736.
KOiK01679.
OMAiAITNCEL.
OrthoDBiEOG73NGC9.

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.

P08417-1 [UniParc]FASTAAdd to Basket

« Hide

MLRFTNCSCK TFVKSSYKLN IRRMNSSFRT ETDAFGEIHV PADKYWGAQT    50
QRSFQNFKIG GARERMPLPL VHAFGVLKKS AAIVNESLGG LDPKISKAIQ 100
QAADEVASGK LDDHFPLVVF QTGSGTQSNM NANEVISNRA IEILGGKIGS 150
KQVHPNNHCN QSQSSNDTFP TVMHIAASLQ IQNELIPELT NLKNALEAKS 200
KEFDHIVKIG RTHLQDATPL TLGQEFSGYV QQVENGIQRV AHSLKTLSFL 250
AQGGTAVGTG LNTKPGFDVK IAEQISKETG LKFQTAPNKF EALAAHDAIV 300
ECSGALNTLA CSLFKIAQDI RYLGSGPRCG YHELMLPENE PGSSIMPGKV 350
NPTQNEALTQ VCVQVMGNNA AITFAGSQGQ FELNVFKPVM IANLLNSIRL 400
ITDAAYSFRV HCVEGIKANE PRIHELLTKS LMLVTALNPK IGYDAASKVA 450
KNAHKKGITL KESALELGVL TEKEFDEWVV PEHMLGPK 488
Length:488
Mass (Da):53,152
Last modified:November 1, 1997 - v2
Checksum:iC099A02409A210E6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731M → V in AAA66909. 1 Publication
Sequence conflicti289 – 2891K → R in AAA66909. 1 Publication
Sequence conflicti392 – 3921A → V in AAA66909. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02802 Genomic DNA. Translation: AAA66909.1.
Z73618 Genomic DNA. Translation: CAA97997.1.
BK006949 Genomic DNA. Translation: DAA11174.1.
PIRiS65295. UFBYM.
RefSeqiNP_015061.1. NM_001184076.1.

Genome annotation databases

EnsemblFungiiYPL262W; YPL262W; YPL262W.
GeneIDi855866.
KEGGisce:YPL262W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J02802 Genomic DNA. Translation: AAA66909.1 .
Z73618 Genomic DNA. Translation: CAA97997.1 .
BK006949 Genomic DNA. Translation: DAA11174.1 .
PIRi S65295. UFBYM.
RefSeqi NP_015061.1. NM_001184076.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YFM X-ray 2.60 A 1-488 [» ]
ProteinModelPortali P08417.
SMRi P08417. Positions 27-485.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 35951. 152 interactions.
DIPi DIP-6451N.
IntActi P08417. 3 interactions.
MINTi MINT-606236.
STRINGi 4932.YPL262W.

Proteomic databases

MaxQBi P08417.
PaxDbi P08417.
PeptideAtlasi P08417.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL262W ; YPL262W ; YPL262W .
GeneIDi 855866.
KEGGi sce:YPL262W.

Organism-specific databases

CYGDi YPL262w.
SGDi S000006183. FUM1.

Phylogenomic databases

eggNOGi COG0114.
GeneTreei ENSGT00390000002779.
HOGENOMi HOG000061736.
KOi K01679.
OMAi AITNCEL.
OrthoDBi EOG73NGC9.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci YEAST:YPL262W-MONOMER.
BRENDAi 4.2.1.2. 984.

Miscellaneous databases

EvolutionaryTracei P08417.
NextBioi 980493.
PROi P08417.

Gene expression databases

Genevestigatori P08417.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. 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 ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are encoded by a single nuclear gene FUM1."
    Wu M., Tzagoloff A.
    J. Biol. Chem. 262:12275-12282(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 44-52, SUBCELLULAR LOCATION.
    Strain: ATCC 201238 / W303-1B.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
    Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
    Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiFUMH_YEAST
AccessioniPrimary (citable) accession number: P08417
Secondary accession number(s): D6W3A8, Q08978
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6920 molecules/cell in log phase SD medium.
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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

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