ID G1RP19_NOMLE Unreviewed; 847 AA.
AC G1RP19;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=PYGL {ECO:0000313|Ensembl:ENSNLEP00000014983.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000014983.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000014983.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000014983.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; ADFV01040106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01040107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01040108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01040109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003267721.1; XM_003267673.2.
DR AlphaFoldDB; G1RP19; -.
DR STRING; 61853.ENSNLEP00000014983; -.
DR Ensembl; ENSNLET00000015732.2; ENSNLEP00000014983.1; ENSNLEG00000012305.2.
DR GeneID; 100604991; -.
DR KEGG; nle:100604991; -.
DR CTD; 5836; -.
DR eggNOG; KOG2099; Eukaryota.
DR GeneTree; ENSGT00950000183148; -.
DR HOGENOM; CLU_010198_1_1_1; -.
DR InParanoid; G1RP19; -.
DR OMA; HCACSVA; -.
DR OrthoDB; 5473321at2759; -.
DR TreeFam; TF300309; -.
DR Proteomes; UP000001073; Chromosome 1a.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016208; F:AMP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0032052; F:bile acid binding; IEA:Ensembl.
DR GO; GO:0005536; F:glucose binding; IEA:Ensembl.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0002060; F:purine nucleobase binding; IEA:Ensembl.
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:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl.
DR GO; GO:0070266; P:necroptotic process; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
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:SF26; GLYCOGEN PHOSPHORYLASE, LIVER FORM; 1.
DR Pfam; PF00343; Phosphorylase; 1.
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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU000587};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 681
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 847 AA; 97160 MW; 59A5F9B2154B50EC CRC64;
MAKPLTDQEK RRQISIRGIV GVENVAELKK SFNRHLHFTL VKDRNVATTR DYFFALAHTV
RDHLVGRWIR TQQHYYDKCP KRVYYLSLEF YMGRTLQNTM INLGLQNACD EAIYQLGLDI
EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEYGIFNQK IRDGWQVEEA
DDWLRYGNPW EKSRPEFMLP VHFYGKVEHT NTGAKWIDTQ VVLALPYDTP VPGYMNNTVN
TMRLWSARAP NDFNLRDFNV GDYIQAVLDR NVAENISRVL YPNDNFFEGK ELRLKQEYFV
VAATLQDIIR RFKASKFVST RGAGTVFDAF PDQVAIQLND THPALAIPEL MRIFVDIEKL
PWSKAWELTQ KTFAYTNHTV LPEALERWPV DLVEKLLPRH LEIIYEINQK HLDRIVALFP
KDVDRLRRMS LIEEEGSKRI NMAHLCIVGS HAVNGVAKIH SDIVKTKVFK DFSELEPDKF
QNKTNGITPR RWLLLCNPGL AELIAEKIGE DYVKDLSQLT KLHSFLGDDV FLRELAKVKQ
ENKLKFSQFL ETEYKVKINP SSMFDVQVKR IHEYKRQLLN CLHVITMYNR IKKDPKKLFV
PRTVIIGGKA APGYHMAKMI IKLITSVADV VNKDPMVGSK LKVIFLENYR VSLAEKVIPA
TDLSEQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVDDVA
ALDKKGYEAK EYYEALPELK LVIDQIDNGF FSPKQPDLFK DIINMLFYHD RFKVFADYEA
YVKCQDKVSQ LYMNPKAWNT MVLKNIAASG KFSSDRTIKE YARDIWNVEP SDLKISLSNE
SNKVNGN
//
