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P10173 (FUMH_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:FH
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
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.

Subcellular location

Mitochondrion 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.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   Molecular functionLyase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

tricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Fumarate hydratase, mitochondrial HAMAP-Rule MF_00743
PRO_0000161335

Regions

Region132 – 1354B site By similarity
Region142 – 1443Substrate binding By similarity

Sites

Binding site1031Substrate By similarity

Amino acid modifications

Modified residue171N6-acetyllysine; alternate By similarity
Modified residue171N6-succinyllysine; alternate By similarity
Modified residue221N6-acetyllysine; alternate By similarity
Modified residue221N6-succinyllysine; alternate By similarity
Modified residue361N6-acetyllysine; alternate By similarity
Modified residue361N6-succinyllysine; alternate By similarity
Modified residue501N6-acetyllysine By similarity
Modified residue711N6-acetyllysine; alternate By similarity
Modified residue711N6-succinyllysine; alternate By similarity
Modified residue781N6-acetyllysine; alternate By similarity
Modified residue781N6-succinyllysine; alternate By similarity
Modified residue1691N6-acetyllysine By similarity
Modified residue2121N6-acetyllysine By similarity
Modified residue2481N6-acetyllysine; alternate By similarity
Modified residue2481N6-succinyllysine; alternate By similarity
Modified residue4231N6-succinyllysine By similarity
Modified residue4291N6-succinyllysine By similarity
Modified residue4581N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P10173 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: E89F349D78FD98DC

FASTA46650,009
        10         20         30         40         50         60 
ASQDSFRIEY DTFGELKVPN DKYYGAQTVR STMNFKIGGV TERMPIPVLK AFGILKRAAA 

        70         80         90        100        110        120 
EVNQDYGLDP KIANAIMKAA DEVAEGKLND HFPLVVWQTG SGTQTNMNVN EVISNRAIEM 

       130        140        150        160        170        180 
LGGELGSKKP VHPNDHVNKS QSSNDTFPTA MHIAAAVEVH EALLPGLQKL HDALDAKSRE 

       190        200        210        220        230        240 
FAQIIKIGRT HTQDAVPLTL GQEFSGYVQQ VKYAITRIKA AMPRIYELAA GGTAVGTGLN 

       250        260        270        280        290        300 
TRIGFAEKVA AKVAALTGLP FVTAPNNFEA LAAHDALVEH SGAMNTTACS LMKIANDIRF 

       310        320        330        340        350        360 
LGSGPRSGLG ELILPENEPG SSIMPGKVNP TQCEALTMVA AQVMGNHVAV TVGGSNGHFE 

       370        380        390        400        410        420 
LNVFKPMMIK NVLHSARLLG DAAVSFTENC VVGIQANTER INKLMNESLM LVTALNPHIG 

       430        440        450        460 
YDKAAKIAKT AHKNGSTLKA TAVELGYLTA EQFDEWVKPR DMLGPK 

« Hide

References

[1]"Amino acid sequence of porcine heart fumarase."
Sacchettini J.C., Frazier M.W., Chiara D.C., Banaszak L.J., Grant G.A.
Biochem. Biophys. Res. Commun. 153:435-440(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Heart.

Cross-references

Sequence databases

PIRUFPG. A27657.

3D structure databases

ProteinModelPortalP10173.
SMRP10173. Positions 5-466.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP10173.
ChEMBLCHEMBL6143.

Proteomic databases

PRIDEP10173.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG002183.

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...

Entry information

Entry nameFUMH_PIG
AccessionPrimary (citable) accession number: P10173
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 19, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways