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Database: UniProt
Entry: A0A2K5X543_MACFA
LinkDB: A0A2K5X543_MACFA
Original site: A0A2K5X543_MACFA 
ID   A0A2K5X543_MACFA        Unreviewed;       795 AA.
AC   A0A2K5X543;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 26.
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|Ensembl:ENSMFAP00000044533.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000044533.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000044533.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000044533.2}
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   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   AlphaFoldDB; A0A2K5X543; -.
DR   Ensembl; ENSMFAT00000018828.2; ENSMFAP00000044533.2; ENSMFAG00000039378.2.
DR   VEuPathDB; HostDB:ENSMFAG00000039378; -.
DR   GeneTree; ENSGT00950000183148; -.
DR   Proteomes; UP000233100; Chromosome 14.
DR   Bgee; ENSMFAG00000039378; Expressed in skeletal muscle tissue and 10 other cell types or tissues.
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; 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:SF13; GLYCOGEN PHOSPHORYLASE, MUSCLE FORM; 1.
DR   Pfam; PF00343; Phosphorylase; 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};
KW   Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU000587};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU000587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   REGION          168..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   795 AA;  90765 MW;  8DAB7D87AFBD2680 CRC64;
     MPVTRPPTSW AWTWRSWRKL RRMRGWAMGA WAGWQVSGQG LEGGGGRWGP PCWVPDTCLP
     AHPQPAFSTP WQHWAWPLMA TGFAMSLGFL TRRSPGAGRW RRLMTGFATA TPGRRPAPSS
     HYLCTSTAMW STPARVPSGW THRWYWPCPT IRPCPAIATT SSTPCASGLP RLPMTSTSRT
     VSSSAGSQQP QPARWPRPAQ ALPCLHFRPS VNVGGYIQAV LDRNLAENIS RVLYPNDNFF
     EGKELRLKQE YFVVAATLQD IIRRFKSSKF GCRDPVRTNF DAFPDKVAIQ LNDTHPSLAI
     PELMRILVDL ERMDWDKAWD VTVRTCAYTN HTVLPEALER WPVHLLETLL PRHLQIIYEI
     NQRFLNRVAA TFPGDVDRLR RMSLVEEGAV KRINMAHLCI AGSHAVNGVA RIHSEILKKT
     IFKDFYELEP HKFQNKTNGI TPRRWLVLCN PGLAEVIAER IGEDFISDLD QLRKLLSFVD
     DEAFIRDVAK VKQENKLKFA AYLEREYKVH INPNSLFDIQ VKRIHEYKRQ LLNCLHVITL
     YNRIKREPNK FFVPRTVMIG GKAAPGYHMA KMIIRLITAI GDVVNHDPTV GDRLRVIFLE
     NYRVSLAEKV IPAADLSEQI STAGTEASGT GNMKFMLNGA LTIGTMDGAN VEMAEEAGEE
     NFFIFGMRVE DVDKLDQRGY NAQEYYDRIP ELRQVIEQLS SGFFSPKQPD LFKDIVNMLM
     HHDRFKVFAD YEDYIKCQEK VSALYKNPRE WTRMVIRNIA TSGKFSSDRT IAQYAREIWG
     VEPSRQRLPA PDEAI
//
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