ID   PHSG_SHIFL              Reviewed;         815 AA.
AC   P0AC87; P13031;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Glycogen phosphorylase;
DE            EC=2.4.1.1;
GN   Name=glgP; OrderedLocusNames=SF3451, S4312;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44911.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP19270.1; -; Genomic_DNA.
DR   RefSeq; NP_709204.1; NC_004337.2.
DR   RefSeq; WP_000993449.1; NZ_WPGW01000010.1.
DR   AlphaFoldDB; P0AC87; -.
DR   SMR; P0AC87; -.
DR   STRING; 198214.SF3451; -.
DR   EnsemblBacteria; AAN44911; AAN44911; SF3451.
DR   EnsemblBacteria; AAP19270; AAP19270; S4312.
DR   GeneID; 1026471; -.
DR   GeneID; 66672688; -.
DR   KEGG; sfl:SF3451; -.
DR   KEGG; sfx:S4312; -.
DR   PATRIC; fig|198214.7.peg.4071; -.
DR   HOGENOM; CLU_010198_1_1_6; -.
DR   OMA; KHKRTFT; -.
DR   OrthoDB; 137158at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome; Transferase.
FT   CHAIN           1..815
FT                   /note="Glycogen phosphorylase"
FT                   /id="PRO_0000188558"
FT   MOD_RES         662
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   815 AA;  93173 MW;  B8046B91D8D7B468 CRC64;
     MNAPFTYSSP TLSVEALKHS IAYKLMFTIG KDPVVANKHE WLNATLFAVR DRLVERWLRS
     NRAQLSQETR QVYYLSMEFL IGRTLSNAML SLGIYEDVQG ALEAMGLNLE ELIDEENDPG
     LGNGGLGRLA ACFLDSLATL GLPGRGYGIR YDYGMFKQNI VNGSQKESPD YWLEYGNPWE
     FKRHNTRYKV RFGGRIQQEG KKTRWIETEE ILGVAYDQII PGYDTDATNT LRLWSAQASS
     EINLGKFNQG DYFAAVEDKN HSENVSRVLY PDDSTYSGRE LRLRQEYFLV SSTIQDILSR
     HYQLHKTYDN LADKIAIHLN DTHPVLSIPE MMRLLIDEHQ FSWDDAFEVC CQVFSYTNHT
     LMSEALETWP VDMLGKILPR HLQIIFEIND YFLKTLQEQY PNDTDLLGRA SIIDESNGRR
     VRMAWLAVVV SHKVNGVSEL HSNLMVQSLF ADFAKIFPGR FTNVTNGVTP RRWLAVANPS
     LSAVLDEHLG RNWRTDLSLL NELQQHCDFP MVNHAVHQAK LENKKRLAEY IAQQLNVVVN
     PKALFDVQIK RIHEYKRQLM NVLHVITRYN RIKADPDAKW VPRVNIFGGK AASAYYMAKH
     IIHLINDVAK VINNDPQIGD KLKVVFIPNY SVSLAQLIIP AADLSEQISL AGTEASGTSN
     MKFALNGALT IGTLDGANVE MLDHVGADNI FIFGNTAEEV EELRRQGYKP REYYEKDEEL
     HQVLTQIGSG VFSPEDPGRY RDLVDSLINF GDHYQVLADY RSYVDCQDKV DELYELQEEW
     TAKAMLNIAN MGYFSSDRTI KEYADHIWHI DPVRL