ID O08329_GEOSE Unreviewed; 798 AA.
AC O08329;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 13-SEP-2023, entry version 81.
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:BAA19592.1};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422 {ECO:0000313|EMBL:BAA19592.1};
RN [1] {ECO:0000313|EMBL:BAA19592.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TRBE14 {ECO:0000313|EMBL:BAA19592.1};
RX PubMed=9244254;
RA Takata H., Takaha T., Okada S., Takagi M., Imanaka T.;
RT "Characterization of a gene cluster for glycogen biosynthesis and a
RT heterotetrameric ADP-glucose pyrophosphorylase from Bacillus
RT stearothermophilus.";
RL J. Bacteriol. 179:4689-4698(1997).
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 -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; D87026; BAA19592.1; -; Genomic_DNA.
DR AlphaFoldDB; O08329; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04300; GT35_Glycogen_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; 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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000587};
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 646
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 798 AA; 92117 MW; E4FF6CF19DCA7C27 CRC64;
MFTDKETFKQ AFLIRLETLC GKQFEESTTR DHYYVLGHMV REHISRHWIA TNERNRAQKR
KQVYYLSIEF LLGRLLGSNL LNLGVRQVVE EGLRDLGIRL EDVEESEADA GLGNGGLGRL
AACFLDSLAT LNLPGHGHGI RYKHGLFDQK IVDGYQVELP QQWLRHGNVW EIRKEELAVE
VNFWGKVEVY EQNGCLVFRH IDSKKVMAVP YDMPVIGYGT NTVNTLRLWN AEPAKTFPLH
KDVMQYKRET EAISEFLYPD DAHDEGKILR LKQQYFLVAA SLGSIVRAHR LQHGNLHQLH
EYVAIHVNDT HPVLAIPELM RILLDEEGMS WEEAWHITTH TIAYTNHTTL SERLRMAIHL
FQPLLPRIYM IVEEINERFC RELWERYPGD WGRIEQMAII AHGVVKMAHL AIAGSHSVNG
VAKLHTEILK QREMRLFYEW APHKFNNKTN GVTHRRWLLK ANPELSALIT DTTGSRWIHE
PETLIELKPH ASDPAFQQAL SAVKQQRKGK LAARIYEKTG IRVDESSIFD VQVKRLHAYK
RQLLNVLHIM YLYNRLKEDP HFSIYPRTFI FGAKASPGYY YAKRIIKLIH SVADKVNNDK
QTNEQLKVIF LENYRVSLAE EIFPAADVSE QISTASIEAS GTGNMKFMMN GALTLGTLDG
ANVEIAEAVG KENMFLFGLT AEEVLNYYEH GGYRAHEYYH HDKRIKQVVD QLVNGFFPDV
ADYFEPIYDS LLTQNDEYFV LRDFAAYTEA HERVEAAYRD PARWWYMSAV NIAHSGYFAS
DRTIAEYAVD IWGISPSM
//
