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Protein

Fumarate hydratase, mitochondrial

Gene

FH

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

Functioni

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

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 (FH)
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 sitei103SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processTricarboxylic acid cycle

Enzyme and pathway databases

SABIO-RKiP10173
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
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL6143

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001613351 – 466Fumarate hydratase, mitochondrialAdd BLAST466

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17N6-acetyllysine; alternateBy similarity1
Modified residuei17N6-succinyllysine; alternateBy similarity1
Modified residuei22N6-acetyllysine; alternateBy similarity1
Modified residuei22N6-succinyllysine; alternateBy similarity1
Modified residuei36N6-acetyllysine; alternateBy similarity1
Modified residuei36N6-succinyllysine; alternateBy similarity1
Modified residuei41PhosphothreonineBy similarity1
Modified residuei50N6-acetyllysineBy similarity1
Modified residuei71N6-acetyllysine; alternateBy similarity1
Modified residuei71N6-succinyllysine; alternateBy similarity1
Modified residuei78N6-acetyllysine; alternateBy similarity1
Modified residuei78N6-succinyllysine; alternateBy similarity1
Modified residuei169N6-acetyllysineBy similarity1
Modified residuei212N6-acetyllysineBy similarity1
Modified residuei248N6-acetyllysine; alternateBy similarity1
Modified residuei248N6-succinyllysine; alternateBy similarity1
Modified residuei322PhosphoserineBy similarity1
Modified residuei423N6-succinyllysineBy similarity1
Modified residuei429N6-succinyllysineBy similarity1
Modified residuei458N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP10173
PeptideAtlasiP10173
PRIDEiP10173

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000026068

Chemistry databases

BindingDBiP10173

Structurei

3D structure databases

ProteinModelPortaliP10173
SMRiP10173
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni132 – 135B siteBy similarity4
Regioni142 – 144Substrate bindingBy similarity3

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1317 Eukaryota
COG0114 LUCA
HOVERGENiHBG002183
InParanoidiP10173

Family and domain databases

CDDicd01362 Fumarase_classII, 1 hit
Gene3Di1.10.275.10, 1 hit
HAMAPiMF_00743 FumaraseC, 1 hit
InterProiView protein in InterPro
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
PANTHERiPTHR11444 PTHR11444, 1 hit
PfamiView protein in Pfam
PF10415 FumaraseC_C, 1 hit
PF00206 Lyase_1, 1 hit
PRINTSiPR00149 FUMRATELYASE
SUPFAMiSSF48557 SSF48557, 1 hit
TIGRFAMsiTIGR00979 fumC_II, 1 hit
PROSITEiView protein in PROSITE
PS00163 FUMARATE_LYASES, 1 hit

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
UniGeneiSsc.17292

Similar proteinsi

Entry informationi

Entry nameiFUMH_PIG
AccessioniPrimary (citable) accession number: P10173
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: March 28, 2018
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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