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P08417 (FUMH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate hydratase, mitochondrial

Short name=Fumarase
EC=4.2.1.2
Gene names
Name:FUM1
Ordered Locus Names:YPL262W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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

Subunit structure

Homotetramer. Ref.7

Subcellular location

Mitochondrion matrix. Cytoplasm. Note: Both fumarases are encoded by a single nuclear gene. Ref.4

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.

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 – ?Mitochondrion HAMAP-Rule MF_00743
Chain? – 488Fumarate hydratase, mitochondrial HAMAP-Rule MF_00743PRO_0000010333

Regions

Region164 – 1663Substrate binding By similarity

Sites

Binding site1261Substrate By similarity

Amino acid modifications

Modified residue4281Phosphothreonine Ref.6

Experimental info

Sequence conflict1731M → V in AAA66909. Ref.1
Sequence conflict2891K → R in AAA66909. Ref.1
Sequence conflict3921A → V in AAA66909. Ref.1

Secondary structure

................................................................ 488
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08417 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: C099A02409A210E6

FASTA48853,152
        10         20         30         40         50         60 
MLRFTNCSCK TFVKSSYKLN IRRMNSSFRT ETDAFGEIHV PADKYWGAQT QRSFQNFKIG 

        70         80         90        100        110        120 
GARERMPLPL VHAFGVLKKS AAIVNESLGG LDPKISKAIQ QAADEVASGK LDDHFPLVVF 

       130        140        150        160        170        180 
QTGSGTQSNM NANEVISNRA IEILGGKIGS KQVHPNNHCN QSQSSNDTFP TVMHIAASLQ 

       190        200        210        220        230        240 
IQNELIPELT NLKNALEAKS KEFDHIVKIG RTHLQDATPL TLGQEFSGYV QQVENGIQRV 

       250        260        270        280        290        300 
AHSLKTLSFL AQGGTAVGTG LNTKPGFDVK IAEQISKETG LKFQTAPNKF EALAAHDAIV 

       310        320        330        340        350        360 
ECSGALNTLA CSLFKIAQDI RYLGSGPRCG YHELMLPENE PGSSIMPGKV NPTQNEALTQ 

       370        380        390        400        410        420 
VCVQVMGNNA AITFAGSQGQ FELNVFKPVM IANLLNSIRL ITDAAYSFRV HCVEGIKANE 

       430        440        450        460        470        480 
PRIHELLTKS LMLVTALNPK IGYDAASKVA KNAHKKGITL KESALELGVL TEKEFDEWVV 


PEHMLGPK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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]"Crystal structures of native and recombinant yeast fumarase."
Weaver T., Lees M., Zaitsev V., Zaitseva I., Duke E., Lindley P., McSweeny S., Svensson A., Keruchenko J., Keruchenko I., Gladilin K., Banaszak L.
J. Mol. Biol. 280:431-442(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02802 Genomic DNA. Translation: AAA66909.1.
Z73618 Genomic DNA. Translation: CAA97997.1.
BK006949 Genomic DNA. Translation: DAA11174.1.
PIRUFBYM. S65295.
RefSeqNP_015061.1. NM_001184076.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YFMX-ray2.60A1-488[»]
ProteinModelPortalP08417.
SMRP08417. Positions 27-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35951. 152 interactions.
DIPDIP-6451N.
IntActP08417. 3 interactions.
MINTMINT-606236.
STRING4932.YPL262W.

Proteomic databases

MaxQBP08417.
PaxDbP08417.
PeptideAtlasP08417.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL262W; YPL262W; YPL262W.
GeneID855866.
KEGGsce:YPL262W.

Organism-specific databases

CYGDYPL262w.
SGDS000006183. FUM1.

Phylogenomic databases

eggNOGCOG0114.
GeneTreeENSGT00390000002779.
HOGENOMHOG000061736.
KOK01679.
OMAAITNCEL.
OrthoDBEOG73NGC9.

Enzyme and pathway databases

BioCycYEAST:YPL262W-MONOMER.
BRENDA4.2.1.2. 984.
UniPathwayUPA00223; UER01007.

Gene expression databases

GenevestigatorP08417.

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

EvolutionaryTraceP08417.
NextBio980493.
PROP08417.

Entry information

Entry nameFUMH_YEAST
AccessionPrimary (citable) accession number: P08417
Secondary accession number(s): D6W3A8, Q08978
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways