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
//