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Protein

Aldose 1-epimerase

Gene

Galm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose (By similarity).By similarity

Catalytic activityi

Alpha-D-glucose = beta-D-glucose.PROSITE-ProRule annotation

Pathwayi: hexose metabolism

This protein is involved in the pathway hexose metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway hexose metabolism and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei176Proton donorPROSITE-ProRule annotation1
Binding sitei243SubstrateBy similarity1
Active sitei307Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processCarbohydrate metabolism

Enzyme and pathway databases

UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldose 1-epimerase (EC:5.1.3.3)
Alternative name(s):
Galactose mutarotase
Gene namesi
Name:Galm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2442420. Galm.

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

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001974341 – 342Aldose 1-epimeraseAdd BLAST342

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei14PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8K157.
MaxQBiQ8K157.
PaxDbiQ8K157.
PeptideAtlasiQ8K157.
PRIDEiQ8K157.

2D gel databases

REPRODUCTION-2DPAGEiQ8K157.

PTM databases

iPTMnetiQ8K157.
PhosphoSitePlusiQ8K157.

Expressioni

Gene expression databases

BgeeiENSMUSG00000035473.
CleanExiMM_GALM.
ExpressionAtlasiQ8K157. baseline and differential.
GenevisibleiQ8K157. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ8K157. 2 interactors.
MINTiMINT-1855059.
STRINGi10090.ENSMUSP00000040580.

Structurei

3D structure databases

ProteinModelPortaliQ8K157.
SMRiQ8K157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni81 – 82Substrate bindingBy similarity2

Sequence similaritiesi

Belongs to the aldose epimerase family.Curated

Phylogenomic databases

eggNOGiKOG1604. Eukaryota.
COG2017. LUCA.
GeneTreeiENSGT00510000047589.
HOGENOMiHOG000072798.
HOVERGENiHBG051697.
InParanoidiQ8K157.
KOiK01785.
OMAiATWLSCK.
OrthoDBiEOG091G0COE.
PhylomeDBiQ8K157.
TreeFamiTF324207.

Family and domain databases

Gene3Di2.70.98.10. 1 hit.
InterProiView protein in InterPro
IPR018052. Ald1_epimerase_CS.
IPR015443. Aldose_1-epimerase.
IPR008183. Aldose_1/G6P_1-epimerase.
IPR011013. Gal_mutarotase_sf_dom.
IPR014718. GH-type_carb-bd.
PfamiView protein in Pfam
PF01263. Aldose_epim. 1 hit.
PIRSFiPIRSF005096. GALM. 1 hit.
SUPFAMiSSF74650. SSF74650. 1 hit.
PROSITEiView protein in PROSITE
PS00545. ALDOSE_1_EPIMERASE. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8K157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSVTRTVFG ELPSGGGTVE KFQLRSDQLS VDIISWGCTI TALQVKDRQG
60 70 80 90 100
KASDVVLGFA ELEGYLQKQP YFGAVVGRVA NRIAKGRFTI GGKEYHLPVN
110 120 130 140 150
REPNSLHGGF TGFDKVLWTP QVLTNGVQFF RVSPDGEEGY PGELKVWVTY
160 170 180 190 200
TLDGGELVIN YRAQASQTTP VNLTNHSYFN LAGQGSPNIY DHEVTIAADA
210 220 230 240 250
YLPVDETLIP TGVIAPVEGT AFDLRKPVEL GTHLQDYHIH GFDHNFCLKE
260 270 280 290 300
SKEKKFCARV RHAASGRILE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK
310 320 330 340
HSGLCLETQN WPDSVNQPQF PPALLRPGEE YNHTTWFKFS VA
Length:342
Mass (Da):37,799
Last modified:October 1, 2002 - v1
Checksum:iEEF74211B6F3426B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040998 mRNA. Translation: BAC30776.1.
BC028818 mRNA. Translation: AAH28818.1.
CCDSiCCDS28987.1.
RefSeqiNP_795937.1. NM_176963.4.
UniGeneiMm.29098.

Genome annotation databases

EnsembliENSMUST00000039205; ENSMUSP00000040580; ENSMUSG00000035473.
GeneIDi319625.
KEGGimmu:319625.
UCSCiuc008dqo.1. mouse.

Entry informationi

Entry nameiGALM_MOUSE
AccessioniPrimary (citable) accession number: Q8K157
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2002
Last modified: November 22, 2017
This is version 116 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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families