ID   PHSG_CHLTR              Reviewed;         814 AA.
AC   O84250;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Glycogen phosphorylase;
DE            EC=2.4.1.1;
GN   Name=glgP; OrderedLocusNames=CT_248;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC       carbohydrate metabolism. Enzymes from different sources differ in their
CC       regulatory mechanisms and in their natural substrates. However, all
CC       known phosphorylases share catalytic and structural properties (By
CC       similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; AE001273; AAC67841.1; -; Genomic_DNA.
DR   PIR; A71540; A71540.
DR   RefSeq; NP_219753.1; NC_000117.1.
DR   RefSeq; WP_010725136.1; NC_000117.1.
DR   AlphaFoldDB; O84250; -.
DR   SMR; O84250; -.
DR   STRING; 813.O172_01345; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   EnsemblBacteria; AAC67841; AAC67841; CT_248.
DR   GeneID; 884873; -.
DR   KEGG; ctr:CT_248; -.
DR   PATRIC; fig|272561.5.peg.265; -.
DR   HOGENOM; CLU_010198_1_1_0; -.
DR   InParanoid; O84250; -.
DR   OMA; KHKRTFT; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IBA:GO_Central.
DR   GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005980; P:glycogen catabolic process; IBA:GO_Central.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   PANTHER; PTHR11468; PTHR11468; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02093; P_ylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Carbohydrate metabolism; Glycogen metabolism;
KW   Glycosyltransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..814
FT                   /note="Glycogen phosphorylase"
FT                   /id="PRO_0000188552"
FT   MOD_RES         662
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   814 AA;  92725 MW;  54DB793A7DFE4E5A CRC64;
     MYFDRTKINV ESMKQAILER VYCGVVQTPQ SASTRDIFTA VAKTVLEWMA KGWLKTQSSY
     YDNDVKRVYY ISMEFLLGRS LKSNLLNLGL LDLVKEALFD LGYDFDQLVE MEHDAGLGNG
     GLGRLAACFL DSMATLEIPA YGYGLRYDYG IFDQKIENGF QVESPDEWLR YGNPWEICRG
     EYLYPVHFYG KVKHSIDSRG RDVAELVDSQ EVLAMAYDVP VPGFNNDAVN SLRLWQAQSR
     HGFEFSYFNH GNYIRAIEDI ALAGNITRVL YPNDSISEGQ ELRLKQEYFL VSATIQDILR
     RYTKTHLSLD KLSEKVSVQL NDTHPALGIA EMMRLLVDRE ELDWDVAWDA TTKIFNYTNH
     TILPEALERW SLDLFSKVLP RHLEIIYEIN ARWLAKVSQK YPGDNDKRRA LSIIEEGSSK
     FVNMANLAVV GTNKVNGVST FHSQLIKSTL FKDFVEFFPD KFINVTNGIT PRRWLALSNK
     KLSSLLNRTI GTEYLTNLTH LHKVIPLAED SGFREEWRNI KIQNKEELAA RIYKELGVTV
     NPQSIFDCHI KRIHEYKRQL MNILRVIYFY NEIRNGSGEI VPTTVIFGGK AAPGYAMAKL
     IIKLINNVAA VVNNDPKVND QLKVIFWPNY RVSLAEAIIP ATDLSEQIST AGMEASGTGN
     MKFALNGALT IGTMDGANIE MAEHIGKEHM FIFGLLEEEI SELRKEYYPQ GICNANPTIQ
     EILDMIAQAK FSQEDKDLFK PIVNRLLNEG DPFFVLADLE AYINTQNRVA SLFKQPEEWT
     KKSIYNVGGI GFFSSDRSIA EYASNIWNVS RPTS