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Protein

ADP-glucose phosphorylase

Gene

At5g18200

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of ADP-glucose and inorganic phosphate (Pi) into glucose-1-phosphate and ADP. Does not possess galactose-1-phosphate uridylyltransferase activity.1 Publication

Catalytic activityi

ADP + alpha-D-glucose 1-phosphate = ADP-alpha-D-glucose + phosphate.1 Publication

Cofactori

Zn2+3 PublicationsNote: Binds 2 zinc ions per subunit.3 Publications

Kineticsi

kcat is 2.7 sec(-1).1 Publication

  1. KM=6.9 µM for ADP-alpha-D-glucose (at pH 8.5 and 25 degrees Celsius)1 Publication
  2. KM=90 µM for phosphate (at pH 8.5 and 25 degrees Celsius)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi63 – 631Zinc 13 Publications
    Metal bindingi66 – 661Zinc 13 Publications
    Binding sitei94 – 941ADP-alpha-D-glucose1 Publication
    Metal bindingi133 – 1331Zinc 1; via pros nitrogen3 Publications
    Binding sitei173 – 1731ADP-alpha-D-glucose1 Publication
    Metal bindingi184 – 1841Zinc 1; via pros nitrogen3 Publications
    Active sitei186 – 1861Tele-AMP-histidine intermediate2 Publications
    Binding sitei188 – 1881ADP-alpha-D-glucose1 Publication
    Metal bindingi216 – 2161Zinc 23 Publications
    Metal bindingi219 – 2191Zinc 23 Publications
    Metal bindingi255 – 2551Zinc 2; via pros nitrogen3 Publications
    Metal bindingi310 – 3101Zinc 2; via pros nitrogen3 Publications
    Binding sitei321 – 3211ADP-alpha-D-glucose; via carbonyl oxygen1 Publication

    GO - Molecular functioni

    • ADP binding Source: UniProtKB
    • nucleotidyltransferase activity Source: UniProtKB
    • ribose-5-phosphate adenylyltransferase activity Source: TAIR
    • UDP-glucose:hexose-1-phosphate uridylyltransferase activity Source: InterPro
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • carbohydrate metabolic process Source: TAIR
    • galactose metabolic process Source: InterPro
    • glucose metabolic process Source: UniProtKB-KW
    • positive regulation of cellular response to phosphate starvation Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT5G18200-MONOMER.
    ReactomeiR-ATH-70370. Galactose catabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ADP-glucose phosphorylase (EC:2.7.7.-)
    Alternative name(s):
    ADP-glucose:phosphate adenylyltransferase
    Gene namesi
    Ordered Locus Names:At5g18200
    ORF Names:MRG7.16
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G18200.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351ADP-glucose phosphorylasePRO_0000169887Add
    BLAST

    Proteomic databases

    PaxDbiQ9FK51.
    PRIDEiQ9FK51.

    PTM databases

    iPTMnetiQ9FK51.

    Expressioni

    Gene expression databases

    GenevisibleiQ9FK51. AT.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    STRINGi3702.AT5G18200.1.

    Structurei

    Secondary structure

    1
    351
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 285Combined sources
    Turni29 – 324Combined sources
    Beta strandi33 – 375Combined sources
    Helixi39 – 435Combined sources
    Helixi45 – 473Combined sources
    Helixi70 – 723Combined sources
    Beta strandi76 – 816Combined sources
    Beta strandi88 – 936Combined sources
    Beta strandi98 – 1003Combined sources
    Helixi101 – 1033Combined sources
    Turni104 – 1063Combined sources
    Beta strandi117 – 1193Combined sources
    Beta strandi123 – 1286Combined sources
    Beta strandi131 – 1344Combined sources
    Helixi137 – 1393Combined sources
    Helixi142 – 15918Combined sources
    Beta strandi167 – 1759Combined sources
    Helixi176 – 1783Combined sources
    Beta strandi186 – 1949Combined sources
    Helixi197 – 21317Combined sources
    Turni217 – 2204Combined sources
    Helixi221 – 2244Combined sources
    Beta strandi225 – 2306Combined sources
    Beta strandi232 – 2387Combined sources
    Beta strandi248 – 2547Combined sources
    Helixi259 – 2613Combined sources
    Helixi264 – 28421Combined sources
    Beta strandi290 – 2956Combined sources
    Helixi303 – 3086Combined sources
    Beta strandi312 – 3176Combined sources
    Helixi324 – 3296Combined sources
    Beta strandi333 – 3364Combined sources
    Helixi338 – 34710Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z84X-ray1.83A/B1-351[»]
    1ZWJX-ray2.30A/B1-351[»]
    2H39X-ray2.23A/B1-351[»]
    2Q4HX-ray1.83A/B1-351[»]
    2Q4LX-ray2.30A/B1-351[»]
    ProteinModelPortaliQ9FK51.
    SMRiQ9FK51. Positions 21-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9FK51.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 444ADP-alpha-D-glucose binding1 Publication
    Regioni72 – 743ADP-alpha-D-glucose binding1 Publication
    Regioni179 – 1824ADP-alpha-D-glucose binding1 Publication
    Regioni325 – 3262ADP-alpha-D-glucose binding1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG2958. Eukaryota.
    COG1085. LUCA.
    HOGENOMiHOG000230491.
    InParanoidiQ9FK51.
    KOiK00965.
    OMAiIGAHEVI.
    OrthoDBiEOG09360GMF.
    PhylomeDBiQ9FK51.

    Family and domain databases

    Gene3Di3.30.428.10. 2 hits.
    InterProiIPR001937. GalP_UDPtransf1.
    IPR005849. GalP_Utransf_N.
    IPR011146. HIT-like.
    [Graphical view]
    PANTHERiPTHR11943. PTHR11943. 1 hit.
    PfamiPF01087. GalP_UDP_transf. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000808. GalT. 1 hit.
    SUPFAMiSSF54197. SSF54197. 2 hits.
    TIGRFAMsiTIGR00209. galT_1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9FK51-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTSPSHASDR GGGDGDSVEN QSPELRKDPV TNRWVIFSPA RAKRPTDFKS
    60 70 80 90 100
    KSPQNPNPKP SSCPFCIGRE QECAPELFRV PDHDPNWKLR VIENLYPALS
    110 120 130 140 150
    RNLETQSTQP ETGTSRTIVG FGFHDVVIES PVHSIQLSDI DPVGIGDILI
    160 170 180 190 200
    AYKKRINQIA QHDSINYIQV FKNQGASAGA SMSHSHSQMM ALPVVPPTVS
    210 220 230 240 250
    SRLDGTKDYF EETGKCCLCE AKSKHFVIDE SSHFVSVAPF AATYPFEIWI
    260 270 280 290 300
    IPKDHSSHFH HLDDVKAVDL GGLLKLMLQK IAKQLNDPPY NYMIHTSPLK
    310 320 330 340 350
    VTESQLPYTH WFLQIVPQLS GVGGFEIGTG CYINPVFPED VAKVMREVSL

    T
    Length:351
    Mass (Da):39,005
    Last modified:March 1, 2001 - v1
    Checksum:i3C62EFE9129C67A7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti148 – 1481I → V in AAM64928 (Ref. 4) Curated
    Sequence conflicti349 – 3491S → N in AAM64928 (Ref. 4) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB012246 Genomic DNA. Translation: BAB09478.1.
    CP002688 Genomic DNA. Translation: AED92518.1.
    BT005792 mRNA. Translation: AAO64194.1.
    AY087378 mRNA. Translation: AAM64928.1.
    RefSeqiNP_197321.1. NM_121825.3.
    UniGeneiAt.24598.

    Genome annotation databases

    EnsemblPlantsiAT5G18200.1; AT5G18200.1; AT5G18200.
    GeneIDi831938.
    GrameneiAT5G18200.1; AT5G18200.1; AT5G18200.
    KEGGiath:AT5G18200.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB012246 Genomic DNA. Translation: BAB09478.1.
    CP002688 Genomic DNA. Translation: AED92518.1.
    BT005792 mRNA. Translation: AAO64194.1.
    AY087378 mRNA. Translation: AAM64928.1.
    RefSeqiNP_197321.1. NM_121825.3.
    UniGeneiAt.24598.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z84X-ray1.83A/B1-351[»]
    1ZWJX-ray2.30A/B1-351[»]
    2H39X-ray2.23A/B1-351[»]
    2Q4HX-ray1.83A/B1-351[»]
    2Q4LX-ray2.30A/B1-351[»]
    ProteinModelPortaliQ9FK51.
    SMRiQ9FK51. Positions 21-351.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT5G18200.1.

    PTM databases

    iPTMnetiQ9FK51.

    Proteomic databases

    PaxDbiQ9FK51.
    PRIDEiQ9FK51.

    Protocols and materials databases

    DNASUi831938.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G18200.1; AT5G18200.1; AT5G18200.
    GeneIDi831938.
    GrameneiAT5G18200.1; AT5G18200.1; AT5G18200.
    KEGGiath:AT5G18200.

    Organism-specific databases

    TAIRiAT5G18200.

    Phylogenomic databases

    eggNOGiKOG2958. Eukaryota.
    COG1085. LUCA.
    HOGENOMiHOG000230491.
    InParanoidiQ9FK51.
    KOiK00965.
    OMAiIGAHEVI.
    OrthoDBiEOG09360GMF.
    PhylomeDBiQ9FK51.

    Enzyme and pathway databases

    BioCyciARA:AT5G18200-MONOMER.
    ReactomeiR-ATH-70370. Galactose catabolism.

    Miscellaneous databases

    EvolutionaryTraceiQ9FK51.
    PROiQ9FK51.

    Gene expression databases

    GenevisibleiQ9FK51. AT.

    Family and domain databases

    Gene3Di3.30.428.10. 2 hits.
    InterProiIPR001937. GalP_UDPtransf1.
    IPR005849. GalP_Utransf_N.
    IPR011146. HIT-like.
    [Graphical view]
    PANTHERiPTHR11943. PTHR11943. 1 hit.
    PfamiPF01087. GalP_UDP_transf. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000808. GalT. 1 hit.
    SUPFAMiSSF54197. SSF54197. 2 hits.
    TIGRFAMsiTIGR00209. galT_1. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAGLUP_ARATH
    AccessioniPrimary (citable) accession number: Q9FK51
    Secondary accession number(s): Q8LB75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: March 1, 2001
    Last modified: September 7, 2016
    This is version 108 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Functions by a double-displacement chemical mechanism and ping-pong kinetics through a covalent nucleotidyl-enzyme intermediate.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.