ID F9US53_LACPL Unreviewed; 798 AA.
AC F9US53;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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:CCC77600.1};
GN OrderedLocusNames=lp_0024 {ECO:0000313|EMBL:CCC77600.1};
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC77600.1, ECO:0000313|Proteomes:UP000000432};
RN [1] {ECO:0000313|EMBL:CCC77600.1, ECO:0000313|Proteomes:UP000000432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC {ECO:0000313|Proteomes:UP000000432};
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W.,
RA Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R.,
RA de Vries M., Ursing B., de Vos W.M., Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WCFS1;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.F.T.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CCC77600.1, ECO:0000313|Proteomes:UP000000432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC {ECO:0000313|Proteomes:UP000000432};
RX PubMed=22156394; DOI=10.1128/JB.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.F.T.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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 -!- 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|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; AL935263; CCC77600.1; -; Genomic_DNA.
DR RefSeq; WP_003643612.1; NC_004567.2.
DR RefSeq; YP_004888114.1; NC_004567.2.
DR AlphaFoldDB; F9US53; -.
DR STRING; 220668.lp_0024; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR EnsemblBacteria; CCC77600; CCC77600; lp_0024.
DR KEGG; lpl:lp_0024; -.
DR PATRIC; fig|220668.9.peg.22; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR OrthoDB; 9760804at2; -.
DR PhylomeDB; F9US53; -.
DR Proteomes; UP000000432; 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: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 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587,
KW ECO:0000313|EMBL:CCC77600.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000000432};
KW Transferase {ECO:0000256|RuleBase:RU000587, ECO:0000313|EMBL:CCC77600.1}.
FT MOD_RES 644
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 798 AA; 90522 MW; ED68EF0BA5524736 CRC64;
MKLTCAQFKK DFLSEIETLY STSLSDTSTI GQFIALGQLV RRYNSQSWTR TAKFYRDHHQ
KQVYYFSIEF LPGRLLASNL LNLNLLTTVK KGLTELGLDF ETISQAEPDP ALGNGGLGRL
AACYMDAMAS LKIAGNGNGI RYRYGLFKQV FMDGYQVELP DDWLHHGNVW ETRRDNKSCI
VQFGGNVWLQ PQADGSLQPQ SENTEDVLAV PYDVGIVGYH NDITNTLRLW SAELPPSATY
SSQDQRDRIS EITKVLYPDD SNSAGQQLRL RQEYFFSSAG VQSIVRDFCA THHGIKLLGK
KVAIHINDTH PTLVIPEMMR LLMDEHHCSW EVAWTLTTQV MSYTNHTILQ EALETWPIDM
FKNLLPRIYQ IIAEIDRRYR EQQTPIFGKA LVDQTAPLGN GQVRMAYLAV IGSHSVNGVA
PLHTELLKTD VLRGLYQVYP ERFNNKTNGI ATRRWVQLAN QPLAQLIDQT IGSDWRRQPD
LLQTLLPYQQ DDHFLYQLGQ VKLTNKQALA AYVQRTMGIK IRTDAIYDVQ IKRLHAYKRQ
LLHVFEILRE YFAIKDHPQQ PVVPRVHIFG AKAAPSYHYA KAIIKLINVV ADMVNQDPAI
GDRLKIVFIP NYGVSIAELI IPAADVSEQI STASKEASGT SNMKLMANGA LSLATYDGAN
IDIMQAAGAE NEYPFGLKVN EVYDYYHRGN YHAADFYDAD PELKRLLDSL IDGTIPGIPT
VGREIYDSLL RYNDEFFVLA DYRAYVTQQQ QISRDFQNQP TWQQRSLANI AASGHFAADL
AVARYADDIW QVPHERLN
//
