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Database: UniProt
Entry: A0A452ISG9_9SAUR
LinkDB: A0A452ISG9_9SAUR
Original site: A0A452ISG9_9SAUR 
ID   A0A452ISG9_9SAUR        Unreviewed;       794 AA.
AC   A0A452ISG9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
OS   Gopherus agassizii (Agassiz's desert tortoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Gopherus.
OX   NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000030880.1, ECO:0000313|Proteomes:UP000291020};
RN   [1] {ECO:0000313|Proteomes:UP000291020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28562605;
RA   Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA   Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT   "The Agassiz's desert tortoise genome provides a resource for the
RT   conservation of a threatened species.";
RL   PLoS ONE 12:e0177708-e0177708(2017).
RN   [2] {ECO:0000313|Ensembl:ENSGAGP00000030880.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   Ensembl; ENSGAGT00000035021.1; ENSGAGP00000030880.1; ENSGAGG00000021754.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   NCBIfam; TIGR02093; P_ylase; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF26; GLYCOGEN PHOSPHORYLASE, LIVER FORM; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 2.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Transferase {ECO:0000256|RuleBase:RU000587}.
FT   REGION          765..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  91808 MW;  60CC7C555CC2DEE7 CRC64;
     MSRPLTDQEK RKQISIRGIV GVENVAELKK GFNRHLHFTL VKDRNVATPR DYYFALAHTV
     RDHLVGRWIR TQQYYYEKDP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDI
     EELEDIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA
     DDWLRHGNPW EKARPEYMLP VHFYGRVEHT KSGLKWVDTQ VVLALPYDTP VPGYMNNTVN
     TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
     VAATLQDVIR RFKASKFGST ESVRTMFESF PDQVCNDSVS KHAFHFLINV LVAWDITKRT
     FAYTNHTVLP EALERWPVDL VEKLLPRHLQ IIYEINQRHL DKVTALFPND IDRLRRMSLI
     EEGGVKRINM AHLCIIGSHA VNGVIHSDIV KTRVFKDFAE LEPEKFQNKT NGITPRRWLL
     LCNPGLAELI AEKIGEDYVK DLSQLIKLHK FVNDDIFIRE VSKVKQENKV KFAQYLEKEY
     KVKINPSSMF DVHVKRIHEY KRQLMNCLHI ITMYNRIKRD PMKPFVPRTV IIGGKAAPGY
     HMAKMIIRLI TAVGHVVNND PVVGNKLKVI FLENYRVSLA EKGNMLYRAV EEAAFKIFLP
     YLETAEGNGL GSXLKQAIDQ IKSGFFSPKQ PDLFNEVTNM LFHHDRFKVF ADYEAYVKCQ
     DKVSQLYMNA KEWTKMVIRN IAASGKFSSD RTIKEYARDI WNVEPSDLKI PPPNEPRDVA
     DDKNPNSISS KAVA
//
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