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Protein

Fumarate hydratase, mitochondrial

Gene

FUM1

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

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathwayi: tricarboxylic 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)DescriptionActionsGraphical viewLength
Binding sitei126SubstrateBy similarity1

GO - Molecular functioni

  • fumarate hydratase activity Source: SGD

GO - Biological processi

  • fumarate metabolic process Source: SGD
  • malate metabolic process Source: GO_Central
  • protein tetramerization Source: GO_Central
  • 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.
ReactomeiR-SCE-71403. 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
Ordered Locus Names:YPL262W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL262W.
SGDiS000006183. FUM1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000010333? – 488Fumarate hydratase, mitochondrial
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei428PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP08417.
PRIDEiP08417.

PTM databases

iPTMnetiP08417.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi35951. 154 interactors.
DIPiDIP-6451N.
IntActiP08417. 4 interactors.
MINTiMINT-606236.

Structurei

Secondary structure

1488
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 31Combined sources4
Beta strandi33 – 35Combined sources3
Beta strandi38 – 43Combined sources6
Helixi48 – 54Combined sources7
Helixi61 – 64Combined sources4
Helixi68 – 87Combined sources20
Helixi93 – 107Combined sources15
Helixi112 – 114Combined sources3
Beta strandi118 – 121Combined sources4
Helixi126 – 142Combined sources17
Helixi155 – 159Combined sources5
Turni160 – 162Combined sources3
Helixi165 – 182Combined sources18
Helixi185 – 202Combined sources18
Turni203 – 205Combined sources3
Beta strandi207 – 212Combined sources6
Beta strandi215 – 221Combined sources7
Helixi222 – 247Combined sources26
Turni255 – 257Combined sources3
Helixi267 – 279Combined sources13
Helixi289 – 294Combined sources6
Helixi297 – 323Combined sources27
Beta strandi327 – 330Combined sources4
Helixi353 – 377Combined sources25
Helixi387 – 411Combined sources25
Helixi413 – 415Combined sources3
Helixi420 – 429Combined sources10
Helixi432 – 434Combined sources3
Turni435 – 437Combined sources3
Helixi438 – 440Combined sources3
Helixi443 – 456Combined sources14
Helixi460 – 466Combined sources7
Helixi472 – 478Combined sources7
Helixi481 – 483Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YFMX-ray2.60A1-488[»]
ProteinModelPortaliP08417.
SMRiP08417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08417.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni164 – 166Substrate bindingBy similarity3

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000002779.
HOGENOMiHOG000061736.
InParanoidiP08417.
KOiK01679.
OMAiKANEPRI.
OrthoDBiEOG092C5NA9.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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

        10         20         30         40         50
MLRFTNCSCK TFVKSSYKLN IRRMNSSFRT ETDAFGEIHV PADKYWGAQT
60 70 80 90 100
QRSFQNFKIG GARERMPLPL VHAFGVLKKS AAIVNESLGG LDPKISKAIQ
110 120 130 140 150
QAADEVASGK LDDHFPLVVF QTGSGTQSNM NANEVISNRA IEILGGKIGS
160 170 180 190 200
KQVHPNNHCN QSQSSNDTFP TVMHIAASLQ IQNELIPELT NLKNALEAKS
210 220 230 240 250
KEFDHIVKIG RTHLQDATPL TLGQEFSGYV QQVENGIQRV AHSLKTLSFL
260 270 280 290 300
AQGGTAVGTG LNTKPGFDVK IAEQISKETG LKFQTAPNKF EALAAHDAIV
310 320 330 340 350
ECSGALNTLA CSLFKIAQDI RYLGSGPRCG YHELMLPENE PGSSIMPGKV
360 370 380 390 400
NPTQNEALTQ VCVQVMGNNA AITFAGSQGQ FELNVFKPVM IANLLNSIRL
410 420 430 440 450
ITDAAYSFRV HCVEGIKANE PRIHELLTKS LMLVTALNPK IGYDAASKVA
460 470 480
KNAHKKGITL KESALELGVL TEKEFDEWVV PEHMLGPK
Length:488
Mass (Da):53,152
Last modified:November 1, 1997 - v2
Checksum:iC099A02409A210E6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti173M → V in AAA66909 (PubMed:3040736).Curated1
Sequence conflicti289K → R in AAA66909 (PubMed:3040736).Curated1
Sequence conflicti392A → V in AAA66909 (PubMed:3040736).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YFMX-ray2.60A1-488[»]
ProteinModelPortaliP08417.
SMRiP08417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35951. 154 interactors.
DIPiDIP-6451N.
IntActiP08417. 4 interactors.
MINTiMINT-606236.

PTM databases

iPTMnetiP08417.

Proteomic databases

MaxQBiP08417.
PRIDEiP08417.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YPL262W.
SGDiS000006183. FUM1.

Phylogenomic databases

GeneTreeiENSGT00390000002779.
HOGENOMiHOG000061736.
InParanoidiP08417.
KOiK01679.
OMAiKANEPRI.
OrthoDBiEOG092C5NA9.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciYEAST:YPL262W-MONOMER.
BRENDAi4.2.1.2. 984.
ReactomeiR-SCE-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

EvolutionaryTraceiP08417.
PROiP08417.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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...

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: November 2, 2016
This is version 171 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.1 Publication
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

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

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 one 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.