ID   Q48PL0_PSE14            Unreviewed;       816 AA.
AC   Q48PL0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   10-JUN-2026, entry version 108.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   Name=glgP {ECO:0000313|EMBL:AAZ36847.1};
GN   OrderedLocusNames=PSPPH_0356 {ECO:0000313|EMBL:AAZ36847.1};
OS   Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS   (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ36847.1, ECO:0000313|Proteomes:UP000000551};
RN   [1] {ECO:0000313|EMBL:AAZ36847.1, ECO:0000313|Proteomes:UP000000551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551};
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA   Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T.,
RA   Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.,
RA   Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S.,
RA   Schneider D.J., Mansfield J., Collmer A., Buell C.R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT   1448A reveals divergence among pathovars in genes involved in virulence and
RT   transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
CC   -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC       glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC       glucose-1-phosphate, and plays a central role in maintaining cellular
CC       and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
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       {ECO:0000256|ARBA:ARBA00025174}.
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         Evidence={ECO:0000256|ARBA:ARBA00001275,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000587};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR   EMBL; CP000058; AAZ36847.1; -; Genomic_DNA.
DR   RefSeq; WP_011167450.1; NC_005773.3.
DR   AlphaFoldDB; Q48PL0; -.
DR   KEGG; psp:PSPPH_0356; -.
DR   eggNOG; COG0058; Bacteria.
DR   HOGENOM; CLU_010198_1_1_6; -.
DR   Proteomes; UP000000551; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000003; Alpha-1,4 glucan phosphorylase; 1.
DR   FunFam; 3.40.50.2000:FF:000153; Alpha-1,4 glucan phosphorylase; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   NCBIfam; TIGR02093; P_ylase; 1.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE, LIVER FORM; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000587}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU000587};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000551};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT   MOD_RES         666
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   816 AA;  92011 MW;  DC739429B35369D9 CRC64;
     MSQEPLVRDA DVAAFRAAVL AKLTYSVGKD PDHAFEHDWF EAVALAARDH MVEHWMDHTR
     QIYRKVQKRV YYLSLEFLIG RLLYDSLSNL GLLEVAREAL TELGVDIERI RLLEPDAALG
     NGGLGRLAAC FMESMSTLGI AGHGYGIRYE HGLFRQGIVD GWQQEQTENW LDFGNPWEFE
     RPEVVYSIGF SGSVDTVVTE AGDSRQVWRP GETVRAIAYD TPVVGWRGKS VNTLRLWRAR
     AVEDLHLERF NAGDHFGAVA EVVRAESISR VLYPNDATEA GQELRLRQEY FFVSASLQDL
     LRRHLNQHAT LTDLPDHAAI QMNDTHPSIA VAELMRQLID NHNIPWDTAW KITVGTLGYT
     NHTLLPEALE TWSVGLMERM LPRHMQIIYL INAQHIDTLR AKGVDDVNVL RAVSLIEEDN
     GRRVRMGNLA FLGSHSVNGV SALHTQLMRK TVFAELHKIY PERINNKTNG ITFRRWLFQA
     NPKLTEMLIE ALGEDVLDNA ETRLKELEPF ADKSSFRKQM ADQRLHSKRA LAAIIHERLG
     IAVNPAAMFD VQVKRIHEYK RQLLNLFHTV ALYQAIRAEP GTDWVPRVKI FAGKAAASYN
     SAKLIIKLTN DIARTVNNDP TVRGLLKVVF MPNYNVSLAE SIIPAADLSE QISTAGLEAS
     GTSNMKFGLN GALTIGTLDG ANVEMSEQVG LEHMFIFGMS SQQVEARKRA GEFNAHGDVA
     ASGRLNDVLQ AIRGGVFSPD DPNRYVGLID QLLDYDRFLV CADFDSYWAA QAKVEERWHD
     SKEWWRSAVL NTARMGWFSS DRTIREYAGD IWKALD
//