ID   PHSG_CHLMU              Reviewed;         813 AA.
AC   Q9PKE6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Glycogen phosphorylase;
DE            EC=2.4.1.1;
GN   Name=glgP; OrderedLocusNames=TC_0519;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39361.1; -; Genomic_DNA.
DR   PIR; G81694; G81694.
DR   RefSeq; WP_010230672.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKE6; -.
DR   SMR; Q9PKE6; -.
DR   STRING; 243161.TC_0519; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PRIDE; Q9PKE6; -.
DR   EnsemblBacteria; AAF39361; AAF39361; TC_0519.
DR   GeneID; 1245879; -.
DR   KEGG; cmu:TC_0519; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_010198_1_1_0; -.
DR   OMA; KHKRTFT; -.
DR   OrthoDB; 137158at2; -.
DR   Proteomes; UP000000800; Chromosome.
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   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; Transferase.
FT   CHAIN           1..813
FT                   /note="Glycogen phosphorylase"
FT                   /id="PRO_0000188550"
FT   MOD_RES         662
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   813 AA;  92652 MW;  921CD13E1624916D CRC64;
     MHFDRMKINV ESMKQAILER VYCGVVQTPQ SASTRDIFTA VAKTVSEWMA KGWLKTQSSY
     YDNDVKRVYY ISMEFLLGRS LKSNLLNLGL LDLVNEALSD LGYDFDQLVE MEHDAGLGNG
     GLGRLAACFL DSMATLGIPA YGYGLRYDYG IFDQQIENGY QVESPDEWLR YGNPWEICRG
     EYLYPVHFYG KVKHSMDSRG RDVAELVDSQ EVLAMAYDVP VPGFNNDTVN SLRLWQAQSR
     HGFEFSYFNH GNYIRAIEDI ALASNITRVL YPNDSISEGQ ELRLKQEYFL VSATIQDILR
     RYTKTHLSLD KLSEKVSVQL NDTHPALGIA EMMHILVDRE ELDWDVAWDT TTKIFNYTNH
     TILPEALERW SLDLFSKVLP RHLEIIYEIN ARWLKKVSQK YPGDDDKRRA LSIIEEGSSK
     FINMANLAVI GTSKVNGVSS FHSQLIKNTL FKDFVEFFPD KFINVTNGIT PRRWLALSNK
     RLSALLNRSI GTDYLTNLTH LNKVISLAED SGFREEWHKI KIQNKEDLSA RIYKELGVSV
     NPQSIFDCHI KRIHEYKRQL MNILRVIYFY NEIRNGSTEI VPTTVIFGGK AAPGYAMAKL
     IIKLINNVAH IVNNDPKAKD LLKVVFWPNY RVSLAEAIIP ATDLSEQIST AGMEASGTGN
     MKFALNGALT IGTMDGANIE MAEHIGKEHM FIFGLLEEEI SALRNEYYPQ GICNANPKIQ
     EILDMVLQAR LPEEDKDLFK PIVNRLLNEG DPFFVLADLE SYLDAHNRVA RLFTQPEEWT
     KKSIYNVGGI GFFSSDRSIT DYASNIWNVS QSS