ID   PHSG_BACSU              Reviewed;         798 AA.
AC   P39123;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Glycogen phosphorylase;
DE            EC=2.4.1.1;
GN   Name=glgP; OrderedLocusNames=BSU30940;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8145641; DOI=10.1111/j.1365-2958.1994.tb00301.x;
RA   Kiel J.A.K.W., Boels J.M., Beldman G., Venema G.;
RT   "Glycogen in Bacillus subtilis: molecular characterization of an operon
RT   encoding enzymes involved in glycogen biosynthesis and degradation.";
RL   Mol. Microbiol. 11:203-218(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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.
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   -!- INDUCTION: Expressed exclusively on media containing carbon sources
CC       that allow efficient sporulation.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000305}.
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DR   EMBL; Z25795; CAA81044.1; -; Genomic_DNA.
DR   EMBL; AF008220; AAC00218.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15072.1; -; Genomic_DNA.
DR   PIR; S40052; S40052.
DR   RefSeq; NP_390972.1; NC_000964.3.
DR   RefSeq; WP_004399110.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P39123; -.
DR   SMR; P39123; -.
DR   STRING; 224308.BSU30940; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PaxDb; P39123; -.
DR   PRIDE; P39123; -.
DR   EnsemblBacteria; CAB15072; CAB15072; BSU_30940.
DR   GeneID; 936630; -.
DR   KEGG; bsu:BSU30940; -.
DR   PATRIC; fig|224308.179.peg.3353; -.
DR   eggNOG; COG0058; Bacteria.
DR   InParanoid; P39123; -.
DR   OMA; KHKRTFT; -.
DR   PhylomeDB; P39123; -.
DR   BioCyc; BSUB:BSU30940-MON; -.
DR   Proteomes; UP000001570; 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   2: Evidence at transcript level;
KW   Allosteric enzyme; Carbohydrate metabolism; Glycogen metabolism;
KW   Glycosyltransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..798
FT                   /note="Glycogen phosphorylase"
FT                   /id="PRO_0000188549"
FT   MOD_RES         646
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   798 AA;  91756 MW;  2E5FD08F05C75045 CRC64;
     MFSSKERFAD LFLKRLEMTC GKSFKDSAKL DQYKTLGNMV REYISADWIE TNEKSRSNSG
     KQTYYLSIEF LLGQLLEQNL MNLGVRDVVE AGLKEIGINL EEILQIENDA GLGNGGLGRL
     AACFLDSLAS LNLPGHGMGI RYKHGLFEQK IVDGHQVELP EQWLKNGNVW EVRNADQAVD
     VPFWGEVHMT EKSGRLHFRH EQATIVTAVP YDIPIIGYET GTVNTLRLWN AEPYAHYHGG
     NILSYKRETE AVSEFLYPDD THDEGKILRL KQQYFLVCAS LKSIVNNYRK THKSLSGLHK
     KVSIHINDTH PALAVPELMR ILLDEENMSW EEAWHITVHT ISYTNHTTLS EALEKWPIHL
     FKPLLPRMYM IIEEINERFC RAVWEKYPGD WKRIENMAIT AHGVVKMAHL AIVGSYSVNG
     VAKIHSDILK EREMRDFHLL FPNRFNNKTN GIAHRRWLLK ANPGLSAIIT EAIGDEWVKQ
     PESLIRLEPY ATDPAFIEQF QNNKSKKKQE LADLIFCTAG VVVNPESIFD VQVKRLHAYK
     RQLLNVLHIM YLYNRLKEDS GFSIYPQTFI FGAKASPSYY YAKKIIKLIH SVAEKVNYDP
     AVKQLIKVVF LENYRVSMAE RIFPASDVSE QISTASKEAS GTGNMKFMMN GALTIGTHDG
     ANIEILERVG PDCIYTFGLK ADEVLSYQEN GGYRSREYYQ HDRRIRQVAD QLINGFFEGE
     ADEFESIFDS LLPHNDEYFV LKDFSSYADA QERIQADYRE RRKWSEHSIV NIAHSGYFSS
     DRTIREYAKD IWGIKPMM