UniProt: A0A6P3QQN5

Database: UniProt
Entry: A0A6P3QQN5_PTEVA

LinkDB:  A0A6P3QQN5_PTEVA 
Original site:  A0A6P3QQN5_PTEVA

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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   A0A6P3QQN5_PTEVA        Unreviewed;       729 AA.
AC   A0A6P3QQN5;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   Name=PYGM {ECO:0000313|RefSeq:XP_011367273.1};
OS   Pteropus vampyrus (Large flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC   Pteropodidae; Pteropodinae; Pteropus.
OX   NCBI_TaxID=132908 {ECO:0000313|Proteomes:UP000515202, ECO:0000313|RefSeq:XP_011367273.1};
RN   [1] {ECO:0000313|RefSeq:XP_011367273.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_011367273.1};
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|ARBA:ARBA00037413,
CC       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:ARBA00036074};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41733;
CC         Evidence={ECO:0000256|ARBA:ARBA00036074};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- SUBUNIT: Homodimer. Homotetramer; to form the enzymatically active
CC       phosphorylase A. {ECO:0000256|ARBA:ARBA00046356}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   RefSeq; XP_011367273.1; XM_011368971.2.
DR   AlphaFoldDB; A0A6P3QQN5; -.
DR   GeneID; 105297994; -.
DR   KEGG; pvp:105297994; -.
DR   CTD; 5837; -.
DR   OrthoDB; 9215500at2759; -.
DR   Proteomes; UP000515202; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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:000005; Alpha-1,4 glucan phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000153; Alpha-1,4 glucan phosphorylase; 2.
DR   FunFam; 3.40.50.2000:FF:000197; 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; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF32; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000587};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU000587};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000515202};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         568
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   729 AA;  84375 MW;  AB9A931514EFCAF4 CRC64;
     MSRPLSDQDK RKQISVRGLA GVENVTDLKK NFNRHLHFTL VKDRNVATPR DYYFALAHTV
     RDHLVGRWIR TQQYYYEKDP KRIYYLSLEF YMGRTLQNTM VNLALENACD EAVYQLGLDM
     EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK ISGGWQMEEA
     DDWLRYGNPW EKARPEFTLP VHFYGRVEHT SQGAKWVDTQ VAIQLNDTHP SLAIPELMRI
     LVDLERLDWD KAWEVTVKTC AYTNHTVLPE ALERWPVHLM ETLLPRHLQI IYEINQRFLN
     RVAAAFPGDV DRLRRMSLVE EEAVKRINMA HLCIAGSHAV NGVARIHSEI LKKTIFKDFY
     ELEPHKFQNK TNGITPRRWL VMCNPGLAEV IAERIGEDYI SDLDQLRKLL SYVDDEAFIR
     DVAKVKQENK LKFSAYLEKE YKVHINPNSL FDIQVKRIHE YKRQLLNCLH IITMYNRIKK
     EPNKFFVPRT VMIGGKAAPG YHMAKMIIRL ITAIGDVVNH DPVIGDRLRV IFLENYRVSL
     AEKVIPAADL SEQISTAGTE ASGTGNMKFM LNGALTIGTM DGANVEMAEE AGEENFFIFG
     MRVEDVEKLD QKGYNAQEYY DRVPELRQII EQLNSGFFSP KQPDLFKDIV NMLMHHDRFK
     VFADYEDYIK CQERVNALYK NPREWTRTVI RNIATSGKFS SDRTITQYAR EIWGVEPSRQ
     RLPAPDEMM
//

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