ID   PHSG_SYNY3              Reviewed;         849 AA.
AC   P73511;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Glycogen phosphorylase;
DE            EC=2.4.1.1;
GN   Name=glgP; OrderedLocusNames=sll1356;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; BA000022; BAA17551.1; -; Genomic_DNA.
DR   PIR; S77217; S77217.
DR   AlphaFoldDB; P73511; -.
DR   SMR; P73511; -.
DR   IntAct; P73511; 8.
DR   STRING; 1148.1652631; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PaxDb; P73511; -.
DR   EnsemblBacteria; BAA17551; BAA17551; BAA17551.
DR   KEGG; syn:sll1356; -.
DR   eggNOG; COG0058; Bacteria.
DR   InParanoid; P73511; -.
DR   OMA; HCACSVA; -.
DR   PhylomeDB; P73511; -.
DR   Proteomes; UP000001425; 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..849
FT                   /note="Glycogen phosphorylase"
FT                   /id="PRO_0000188559"
FT   MOD_RES         679
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   849 AA;  96649 MW;  657D2C5E83C23A3D CRC64;
     MEHLPMAFNT TNPLIQVEDD RTGLSVETLK RALADNLFYL QGKFPAIATK NDCYMALAYT
     IRDRLLQRWL NTFQTYLNCD NRVVCYLSAE YLLGPHLGNN LINLGLWEPV QQAVEESGLS
     LDELIDIEEE PGLGNGGLGR LAACFMDSLA TLEIPAIGYG IRYEFGIFDQ EIKDGWQVEI
     TDKWLQLGNP WEIARPESAV LVKLGGHTEP YTDDQGNYRV RWIAGSLVKG IPYDTPILGY
     KVSTANNLRL WKSEAAESFD FQRFNVGDYY GAVQDKMSSE NLTKVLYPND EQIQGKELRL
     AQQYFFVSCS LQDMIRIHLS DNPTLENFHE HFAVQMNDTH PSIAVAELMR LLVDEHHYEW
     QRAWAITEAT FGFTNHTLLP EALEKWSLPL FGEMLPRHLE IIYEINQRFL DQVRMKYPND
     GDRLARLSII DEAGEKSVRM AYLATVGSHA INGVAALHSQ LVKETILKDF YELWPEKFSN
     KTNGVTPRRW MVLSNPRLSN LISSRIGDGW IKNLDELKQL EPFADLAGFR QDWCKVKREV
     KQDLARYIHT RTDLVVNPDS LFDVQVKRIH EYKRQHLNIL HVIHLYLQIK NNPNLDVTPR
     TFIYGGKAAP GYFTAKLIIK LINSVADVVN NDPTIGDRLK VIFLPDYNVK FGQRVYPAAD
     LSEQISTAGK EASGTGNMKF SMNGALTIGT LDGANIEIRE EVGAENFFLF GLTTPEVEKT
     LAEGYQPWEY YNNNANLKAV VDLINSGFFS HGDTALFRPL MDSLLGQDPY LVFADFQAYV
     DCQNQVGEAY KDQENWARMA ILNVARMGKF SSDRTIREYA EDIWAIKPVV IELEDLCPDG
     QCLLISPNK