ID A0A0C4WJJ1_9GAMM Unreviewed; 815 AA.
AC A0A0C4WJJ1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:AJE20124.1};
GN ORFNames=Achr_6250 {ECO:0000313|EMBL:AJE20124.1};
OS Azotobacter chroococcum NCIMB 8003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE20124.1, ECO:0000313|Proteomes:UP000068210};
RN [1] {ECO:0000313|EMBL:AJE20124.1, ECO:0000313|Proteomes:UP000068210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE20124.1,
RC ECO:0000313|Proteomes:UP000068210};
RX PubMed=26061173;
RA Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT (ATCC 4412).";
RL PLoS ONE 10:E0127997-E0127997(2015).
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; CP010415; AJE20124.1; -; Genomic_DNA.
DR RefSeq; WP_039801777.1; NZ_CP010415.1.
DR AlphaFoldDB; A0A0C4WJJ1; -.
DR STRING; 1328314.Achr_6250; -.
DR KEGG; acx:Achr_6250; -.
DR HOGENOM; CLU_010198_1_1_6; -.
DR Proteomes; UP000068210; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000068210};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
FT MOD_RES 665
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 815 AA; 91910 MW; 1134857DB3CEA98E CRC64;
MPEVSPVPEE VAAFRARIVD KLRYAVGKDP EHAVGFDWFE AVALAARDHL VETWMDHASR
TYRQGRKRVY YLSLEFLVGR LLQATLNNLG LLEVARAALA ELDVDLERIR ELEPDAALGN
GGLGRLAACF MESMATLGIP AYGYGIRYDY GLFRQTIVDG WQQEQTETWL EFGNPWEFER
PEVSYRICFG GSVVCRDGES GRQCHVWQPG EEMRAIAYDT PIVGWRRHSV NTLRLWRGRA
ETDLHLERFN AGDHLGAVAE SVRAESISRV LYPADDTPAG QELRLRQEYF FVSASLQDLL
RRHLKQRGSL LDLPEYAAIQ LNDTHPSIAV AELMRLLLDV HGLDWDKAWE LTVATLSYTN
HTLLPEALES WPVALMERLL PRHMQIIYLI NAQHIDHLRA QGMHDFDLLR AVSLIEEEHG
RRVRMGNLAF LGSHSVNGVS ALHTELMRKT VFAQLHRLYP ERISNKTNGI TFRRWLYQSN
PRLTALLVDA LGEPLLDDPE HLLGGLEAQA GQSAFHQHFR TLRRHNKEVL TALVQDRLGI
ALDPEALFDV QVKRIHEYKR QLLNLLHCVA LYQAIRDEPG VDWGPRVKIL AGKAAASYYQ
AKLIIKLAND IARTVNGDPT VRGRLKVVFL PNYNVSLAEV IIPAADLSEQ ISTAGMEASG
TSNMKFALNG ALTIGTLDGA NVEMSERIGS EHMFIFGLGA QQVEARRRSG EVGGAAAVAA
SPRLSEVLTA IRSGVFSPDD PGRYAGLVDG LLQHDNFMVC ADFEAYWQAQ LEVDARWRTP
GQWWRSAVLN TARMGWFSSD RTIREYAREI WRLPE
//
