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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: 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

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
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.
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

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.

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.

Cross-referencesi

Sequence databases

PIRiA27657. UFPG.
UniGeneiSsc.17292.

3D structure databases

ProteinModelPortaliP10173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000026068.

Chemistry databases

BindingDBiP10173.
ChEMBLiCHEMBL6143.

Proteomic databases

PaxDbiP10173.
PeptideAtlasiP10173.
PRIDEiP10173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1317. Eukaryota.
COG0114. LUCA.
HOVERGENiHBG002183.
InParanoidiP10173.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

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_PIG
AccessioniPrimary (citable) accession number: P10173
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 5, 2016
This is version 102 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

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.