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Protein

Fumarate hydratase, mitochondrial

Gene

FH

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate = fumarate + H2O.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031SubstrateBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-EC

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase, mitochondrial (EC:4.2.1.2)
Short name:
Fumarase
Gene namesi
Name:FH
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Fumarate hydratase, mitochondrialPRO_0000161335Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
Modified residuei17 – 171N6-succinyllysine; alternateBy similarity
Modified residuei22 – 221N6-acetyllysine; alternateBy similarity
Modified residuei22 – 221N6-succinyllysine; alternateBy similarity
Modified residuei36 – 361N6-acetyllysine; alternateBy similarity
Modified residuei36 – 361N6-succinyllysine; alternateBy similarity
Modified residuei50 – 501N6-acetyllysineBy similarity
Modified residuei71 – 711N6-acetyllysine; alternateBy similarity
Modified residuei71 – 711N6-succinyllysine; alternateBy similarity
Modified residuei78 – 781N6-acetyllysine; alternateBy similarity
Modified residuei78 – 781N6-succinyllysine; alternateBy similarity
Modified residuei169 – 1691N6-acetyllysineBy similarity
Modified residuei212 – 2121N6-acetyllysineBy similarity
Modified residuei248 – 2481N6-acetyllysine; alternateBy similarity
Modified residuei248 – 2481N6-succinyllysine; alternateBy similarity
Modified residuei322 – 3221PhosphoserineBy similarity
Modified residuei423 – 4231N6-succinyllysineBy similarity
Modified residuei429 – 4291N6-succinyllysineBy similarity
Modified residuei458 – 4581N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP10173.

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP10173.
SMRiP10173. Positions 5-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni132 – 1354B siteBy similarity
Regioni142 – 1443Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG002183.
InParanoidiP10173.

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.

P10173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ASQDSFRIEY DTFGELKVPN DKYYGAQTVR STMNFKIGGV TERMPIPVLK
60 70 80 90 100
AFGILKRAAA EVNQDYGLDP KIANAIMKAA DEVAEGKLND HFPLVVWQTG
110 120 130 140 150
SGTQTNMNVN EVISNRAIEM LGGELGSKKP VHPNDHVNKS QSSNDTFPTA
160 170 180 190 200
MHIAAAVEVH EALLPGLQKL HDALDAKSRE FAQIIKIGRT HTQDAVPLTL
210 220 230 240 250
GQEFSGYVQQ VKYAITRIKA AMPRIYELAA GGTAVGTGLN TRIGFAEKVA
260 270 280 290 300
AKVAALTGLP FVTAPNNFEA LAAHDALVEH SGAMNTTACS LMKIANDIRF
310 320 330 340 350
LGSGPRSGLG ELILPENEPG SSIMPGKVNP TQCEALTMVA AQVMGNHVAV
360 370 380 390 400
TVGGSNGHFE LNVFKPMMIK NVLHSARLLG DAAVSFTENC VVGIQANTER
410 420 430 440 450
INKLMNESLM LVTALNPHIG YDKAAKIAKT AHKNGSTLKA TAVELGYLTA
460
EQFDEWVKPR DMLGPK
Length:466
Mass (Da):50,009
Last modified:July 1, 1989 - v1
Checksum:iE89F349D78FD98DC
GO

Sequence databases

PIRiA27657. UFPG.

Cross-referencesi

Sequence databases

PIRiA27657. UFPG.

3D structure databases

ProteinModelPortaliP10173.
SMRiP10173. Positions 5-466.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP10173.
ChEMBLiCHEMBL6143.

Proteomic databases

PRIDEiP10173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG002183.
InParanoidiP10173.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

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. Cited for: PROTEIN SEQUENCE.
    Tissue: Heart.

Entry informationi

Entry nameiFUMH_PIG
AccessioniPrimary (citable) accession number: P10173
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 4, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.