ID   PHSG_AQUAE              Reviewed;         692 AA.
AC   O66932;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Glycogen phosphorylase;
DE            EC=2.4.1.1;
GN   Name=glgP; OrderedLocusNames=aq_717;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06896.1; -; Genomic_DNA.
DR   PIR; H70362; H70362.
DR   RefSeq; NP_213492.1; NC_000918.1.
DR   RefSeq; WP_010880430.1; NC_000918.1.
DR   AlphaFoldDB; O66932; -.
DR   SMR; O66932; -.
DR   STRING; 224324.aq_717; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   EnsemblBacteria; AAC06896; AAC06896; aq_717.
DR   KEGG; aae:aq_717; -.
DR   PATRIC; fig|224324.8.peg.575; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_015112_0_0_0; -.
DR   InParanoid; O66932; -.
DR   OMA; LYRHGYF; -.
DR   OrthoDB; 137158at2; -.
DR   BRENDA; 2.4.1.1; 396.
DR   Proteomes; UP000000798; 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; 1.
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; Reference proteome; Transferase.
FT   CHAIN           1..692
FT                   /note="Glycogen phosphorylase"
FT                   /id="PRO_0000188548"
FT   MOD_RES         586
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   692 AA;  81158 MW;  4DC0EA2B2E58BEA4 CRC64;
     MEEEKVKEGL WELAYNLWWT WNPPAKELFR SIDPLLWKET KENPIELLRK TKLLENKLKD
     EDFISHFKYV YSLYKTYMNR HSKYEDTYKK PIVFLSPEYG LHHTLLIYAG GLGFLAGDIL
     KESSDLGFPL IGVGFMYPQG YVKQRIRVDG WQEDLDAQNQ KELMPVKKVL DKEGKWLKCY
     VYVRDEKVYF GVWEVNVGKT KLYLLDTNVE ENTPWNREIS SRLYVPDKDL RLRQQIVLGF
     GTVILLEKLG IDAGGFHINE DYPSFVFLAE IFKLLKKGLT WDKAIEEVRK ISLFTTHTPL
     RVAVNTYPFH MIEEQFLFVK DVYGIDVKKV LELGTNPEDP SEGFNSTIMS LRLAKYVNAV
     SKRHQEVSSK MWSFLFKEKE NPIDYVTNGV HFPTWICSDL RRLYEEYLGE NFVELHDHKS
     LWELIRDIPD EELWEYHIRN KERLIEHIKD RARERWVKEK ADPSILMAEG LFLDSDVLTV
     GFARRMTGYK RPDLIFTDVE RLKKIVNDSE RPVQIIFAGK AHPADIEGKK IIQRIFNFAK
     DPEFGGRIAF VEDYDELLAH YMVRGVDVWL NNPLPPLEAC GTSGMKASMN GVLHLSILDG
     WWIEGYNGKN GWAFGDYEVE GDRNRADAEA IYNILENEVI PLYYERDERG VPVKWISMMK
     EAIKSITPNF CSRRMLKDYI NKFYSKILKE EG