UniProt: A0A6P5YJW5

Database: UniProt
Entry: A0A6P5YJW5_DURZI

LinkDB:  A0A6P5YJW5_DURZI 
Original site:  A0A6P5YJW5_DURZI

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
All databases (13)   

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ID   A0A6P5YJW5_DURZI        Unreviewed;      1055 AA.
AC   A0A6P5YJW5;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   Name=LOC111292628 {ECO:0000313|RefSeq:XP_022740824.1};
OS   Durio zibethinus (Durian).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Helicteroideae; Durio.
OX   NCBI_TaxID=66656 {ECO:0000313|Proteomes:UP000515121, ECO:0000313|RefSeq:XP_022740824.1};
RN   [1] {ECO:0000313|RefSeq:XP_022740824.1}
RP   IDENTIFICATION.
RC   TISSUE=Fruit stalk {ECO:0000313|RefSeq:XP_022740824.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
CC   -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC       glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC       glucose-1-phosphate, and plays a central role in maintaining cellular
CC       and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC         glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC         Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001275,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   RefSeq; XP_022740824.1; XM_022885089.1.
DR   AlphaFoldDB; A0A6P5YJW5; -.
DR   GeneID; 111292628; -.
DR   KEGG; dzi:111292628; -.
DR   OrthoDB; 9215500at2759; -.
DR   Proteomes; UP000515121; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:TreeGrafter.
DR   CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000003; Alpha-1,4 glucan phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000105; Alpha-1,4 glucan phosphorylase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   NCBIfam; TIGR02093; P_ylase; 1.
DR   PANTHER; PTHR11468:SF28; ALPHA-GLUCAN PHOSPHORYLASE 1; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000587};
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU000587}; Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515121};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   REGION          70..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..560
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..628
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1055 AA;  118750 MW;  5A6900CC7BD0C3A3 CRC64;
     MATWRFSTTP SGAEAVSSCN AVARFIDFSR GRNSGVVCGG GGGSGIKAKQ LMLMRRWQVR
     PMRRSFSVRN VSSEPQQKVK DPVTQQQESL GTVSPFPPDA SSIASSIKYH AEFTPLFSSE
     KFDLPKAFFA TAQSICDALI INWNATYDYY ERLNVKQAYY LSMEFLQGRA LLNAIGNLGL
     TGAYADALSK LGHNLENIAF QEPDAALGNG GLGRLASCFL DSLATLNYPA WGYGLRYKYG
     LFKQRITKEG QEEVAEDWLE MSNPWEIVRN DVTYPVKFYG KVVAGSDGNK HWIGGEDIKA
     VAYDVPIPGY KTQTTINLRL WSTKAPSEDF DLFAFNSGDH IQAAEALYNA EKICYVLYPG
     DESIEGKILR LKQQYTLCSA SLQDIIARFE RRLGAKVKWE EFPEKVAVQM NDTHPTLCIP
     ELMRILIDVK GLSWKEAWNI TQRTMAYTNH TVLPEALEKW SLELMQKLLP RHVEIIEMID
     EELIRTIVSE YGTADSNLLE KKLKQMRILE NVELPAAFSD LLVKPEESPV AVPSDELEKS
     EDEEEEGEVE EEVELTDGEN VELPAASSDL LVKPKESPVA VPSDELEKSE DEEEEEGGVE
     DEEEEEGGVE EEGVEEEGGV EEEVEPTDGE NKPVKEGTQG KKKIPEPVRD PPKMVRMANL
     CVVGGHAVNG VAAIHSEIVK DEVFNDFFKL WPEKFQNKTN GVTPRRWIRF CNPNLSKIIT
     NWTGTEDWVL NTEKLAELRK FVDNEDLQAQ WREAKRSNKL KAVSFLKEKT GYIVSPDAMF
     DIQVKRIHEY KRQLLNILGI VYRYKMMKEM SASERKEKFV PRVCIFGGKA FATYVQAKRI
     VKFITDVGAT VNHDPDIGDL LKVVFVPDYN VSVAELLIPA SELSQHISTA GMEASGTSNM
     KFAMNGCILI GTLDGANVEI REEVGEDNFF LFGAEAHEIA GLRKERAEGK FVPDPCFEDV
     KEFVRSGVFG PYNYDELMGS LEGNEGFGRA DYFLVGKDFP SYIECQEKVD EAYKDQKRWT
     RMSILNTAGS YKFSSDRTIH EYAREIWNIK PAELP
//

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