ID   PHSG_MYCTO              Reviewed;         863 AA.
AC   P9WMW0; L0T6B6; Q10639;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Glycogen phosphorylase;
DE            EC=2.4.1.1;
GN   Name=glgP; OrderedLocusNames=MT1370;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45634.1; -; Genomic_DNA.
DR   PIR; D70770; D70770.
DR   RefSeq; WP_003900319.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMW0; -.
DR   SMR; P9WMW0; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   EnsemblBacteria; AAK45634; AAK45634; MT1370.
DR   KEGG; mtc:MT1370; -.
DR   PATRIC; fig|83331.31.peg.1477; -.
DR   HOGENOM; CLU_015112_0_0_11; -.
DR   Proteomes; UP000001020; 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; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   Pfam; PF11897; DUF3417; 1.
DR   Pfam; PF00343; Phosphorylase; 2.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02094; more_P_ylases; 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..863
FT                   /note="Glycogen phosphorylase"
FT                   /id="PRO_0000427233"
FT   MOD_RES         618
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   863 AA;  95516 MW;  E5E4D35F01A8FB99 CRC64;
     MKALRRFTVR AHLPERLAAL DQLSTNLRWS WDKPTQDLFA AIDPALWEQC GHDPVALLGA
     VNPARLDELA LDAEFLGALD ELAADLNDYL SRPLWYQEQQ DAGVAAQALP TGIAYFSLEF
     GVAEVLPNYS GGLGILAGDH LKSASDLGVP LIAVGLYYRS GYFRQSLTAD GWQHETYPSL
     DPQGLPLRLL TDANGDPVLV EVALGDNAVL RARIWVAQVG RVPLLLLDSD IPENEHDLRN
     VTDRLYGGDQ EHRIEQEILA GIGGVRAIRA YTAVEKLTPP EVFHMNEGHA GFLGIERIRE
     LVTDAGLDFD TALTVVRSST VFTTHTPVPA GIDRFPLEMV QRYVNDQRGD GRSRLLPGLP
     ADRIVALGAE DDPAKFNMAH MGLRLAQRAN GVSLLHGRVS RAMFNELWAG FDPDEVPIGS
     VTNGVHAPTW AAPQWLQLGR ELAGSDSLRE PVVWQRLHQV DPAHLWWIRS QLRSMLVEDV
     RARLRQSWLE RGATDAELGW IATAFDPNVL TVGFARRVPT YKRLTLMLRD PDRLEQLLLD
     EQRPIQLIVA GKSHPADDGG KALIQQVVRF ADRPQVRHRI AFLPNYDMSM ARLLYWGCDV
     WLNNPLRPLE ACGTSGMKSA LNGGLNLSIR DGWWDEWYDG ENGWEIPSAD GVADENRRDD
     LEAGALYDLL AQAVAPKFYE RDERGVPQRW VEMVRHTLQT LGPKVLASRM VRDYVEHYYA
     PAAQSFRRTA GAQFDAAREL ADYRRRAEEA WPKIEIADVD STGLPDTPLL GSQLTLTATV
     RLAGLRPNDV TVQGVLGRVD AGDVLMDPVT VEMAHTGTGD GGYEIFSTTT PLPLAGPVGY
     TVRVLPRHPM LAASNELGLV TLA