ID   PHSG_HAEIN              Reviewed;         821 AA.
AC   P45180;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Glycogen phosphorylase;
DE            EC=2.4.1.1;
GN   Name=glgP; OrderedLocusNames=HI_1361;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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; L42023; AAC23008.1; -; Genomic_DNA.
DR   PIR; D64119; D64119.
DR   RefSeq; NP_439512.1; NC_000907.1.
DR   RefSeq; WP_005693999.1; NC_000907.1.
DR   AlphaFoldDB; P45180; -.
DR   SMR; P45180; -.
DR   STRING; 71421.HI_1361; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PRIDE; P45180; -.
DR   EnsemblBacteria; AAC23008; AAC23008; HI_1361.
DR   KEGG; hin:HI_1361; -.
DR   PATRIC; fig|71421.8.peg.1415; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_010198_1_1_6; -.
DR   OMA; KHKRTFT; -.
DR   PhylomeDB; P45180; -.
DR   BioCyc; HINF71421:G1GJ1-1386-MON; -.
DR   Proteomes; UP000000579; 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..821
FT                   /note="Glycogen phosphorylase"
FT                   /id="PRO_0000188554"
FT   MOD_RES         667
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   821 AA;  94441 MW;  B28D751D587736A4 CRC64;
     MIMDNFDSPF QYNRPEMTVE AIKKSIVYKL IFLIGRSPRE ASQRDWLNAT LHAVRDLVTE
     GWITTARQTR AEDSRRVYYL SMEFLIGRTL SNAMIAEGIY GLAQEALSEL NVDLEEVLEK
     EVDPGLGNGG LGRLAACFMD SIATLGLPGM GYGIRYEYGM FRQKIENGQQ VERPDAWLEK
     GAPWEFIRPS KRFTVEFGGN IHFEGKKCIW QDTEKVTALA YDQMIPGYQN NSAATLRLWS
     AHAGEVFNLA DFNRGEHLAA LEEHSANKNL SRVLYPDDST WNGRELRLRQ EYFLVSASLQ
     DILRRHKRTH NSLENLADKV AIHLNDTHPA LAIPELMRIL VDDEGFEWKK AWEMTRNIFS
     YTCHTLMSEA LETWPVEMMA KILPRHLQMI FEINDHFLEY VRTYVTTDND FIRRVSLIEE
     GYQRKVRMGW LSVVGSHKIN GVAEIHSDLM VTSTFADFAR IFPERFTNVT NGITPRRWLA
     VANPQLAALF DKYIGSEWRC DLSQIEKLKP FAQEKAFKEA VADIKFANKV KLAEYVKSEL
     GVELDPHALF DVQVKRIHEY KRQMLNVLHI IARYNEMLTN PEKDWQPRVF ILAGKAASAY
     YAAKQTIHLI NDVANVINND ERLKGRLKVV FIPNYSVSLA QLIIPAADIS EQISLAGTEA
     SGTSNMKFAL NGALTLGTLD GANVEILENV GEDNIFIFGN TVEQVEQLRR EGYRSFEYYQ
     NDAQLRTVVD QIIEGKFSPE DPQRYHQLLQ GLQYHDYYQA FADFRSYVET QKAVDEKYKQ
     RDQWIESTIQ NIVNMGFFSS DRTIKEYAER IWKVEPVQLG D