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Q5R8U1

- GALM_PONAB

UniProt

Q5R8U1 - GALM_PONAB

Protein

Aldose 1-epimerase

Gene

GALM

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei176 – 1761Proton donorPROSITE-ProRule annotation
    Binding sitei243 – 2431SubstrateBy similarity
    Active sitei307 – 3071Proton acceptorBy similarity

    GO - Molecular functioni

    1. aldose 1-epimerase activity Source: UniProtKB-EC
    2. carbohydrate binding Source: InterPro

    GO - Biological processi

    1. hexose metabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Carbohydrate 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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 342341Aldose 1-epimerasePRO_0000197436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R8U1.
    SMRiQ5R8U1. Positions 1-342.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni81 – 822Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the aldose epimerase family.Curated

    Phylogenomic databases

    HOVERGENiHBG051697.
    InParanoidiQ5R8U1.
    KOiK01785.

    Family and domain databases

    Gene3Di2.70.98.10. 1 hit.
    InterProiIPR018052. Ald1_epimerase_CS.
    IPR015443. Aldose_1-epimerase.
    IPR008183. Aldose_1/G6P_1-epimerase.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    [Graphical view]
    PfamiPF01263. Aldose_epim. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005096. GALM. 1 hit.
    SUPFAMiSSF74650. SSF74650. 1 hit.
    PROSITEiPS00545. ALDOSE_1_EPIMERASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q5R8U1-1 [UniParc]FASTAAdd to Basket

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    MASATRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG    50
    RSSDVVLGFA ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN 100
    KEPNSLHGGV RGFDKVLWTP RVLSNGIQFS RISPDGEEGY PGELKVWVTY 150
    TLDGGELVVN YRAQASQATP VNLTNHSYFN LAGQGSPNIY DHEVTIEADT 200
    YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN GFDHNFCLKG 250
    SKEKHFCARV HHAASGRVLE VYTTQPGVQF YMGNFLDGTL KGKNGAVYPK 300
    HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA 342
    Length:342
    Mass (Da):37,819
    Last modified:December 21, 2004 - v1
    Checksum:iD00C2A67753D6DFF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859658 mRNA. Translation: CAH91819.1.
    RefSeqiNP_001126052.1. NM_001132580.1.
    UniGeneiPab.14287.

    Genome annotation databases

    GeneIDi100173004.
    KEGGipon:100173004.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859658 mRNA. Translation: CAH91819.1 .
    RefSeqi NP_001126052.1. NM_001132580.1.
    UniGenei Pab.14287.

    3D structure databases

    ProteinModelPortali Q5R8U1.
    SMRi Q5R8U1. Positions 1-342.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100173004.
    KEGGi pon:100173004.

    Organism-specific databases

    CTDi 130589.

    Phylogenomic databases

    HOVERGENi HBG051697.
    InParanoidi Q5R8U1.
    KOi K01785.

    Enzyme and pathway databases

    UniPathwayi UPA00242 .

    Family and domain databases

    Gene3Di 2.70.98.10. 1 hit.
    InterProi IPR018052. Ald1_epimerase_CS.
    IPR015443. Aldose_1-epimerase.
    IPR008183. Aldose_1/G6P_1-epimerase.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR014718. Glyco_hydro-type_carb-bd_sub.
    [Graphical view ]
    Pfami PF01263. Aldose_epim. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005096. GALM. 1 hit.
    SUPFAMi SSF74650. SSF74650. 1 hit.
    PROSITEi PS00545. ALDOSE_1_EPIMERASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiGALM_PONAB
    AccessioniPrimary (citable) accession number: Q5R8U1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 52 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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