ID I0S7M9_STRAP Unreviewed; 752 AA.
AC I0S7M9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:EID19382.1};
GN ORFNames=HMPREF1043_2234 {ECO:0000313|EMBL:EID19382.1};
OS Streptococcus anginosus subsp. whileyi CCUG 39159.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=1095729 {ECO:0000313|EMBL:EID19382.1, ECO:0000313|Proteomes:UP000003245};
RN [1] {ECO:0000313|EMBL:EID19382.1, ECO:0000313|Proteomes:UP000003245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 39159 {ECO:0000313|EMBL:EID19382.1,
RC ECO:0000313|Proteomes:UP000003245};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EID19382.1}.
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DR EMBL; AICP01000065; EID19382.1; -; Genomic_DNA.
DR RefSeq; WP_003038352.1; NZ_AICP01000065.1.
DR AlphaFoldDB; I0S7M9; -.
DR PATRIC; fig|1095729.3.peg.2097; -.
DR Proteomes; UP000003245; Unassembled WGS sequence.
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 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 603
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 752 AA; 85420 MW; 7C128AA16590DCB2 CRC64;
MSNLQEFIQQ TYQKEIAECS NEELYIALLN YTKLASAQKP VNTGKKKLYY ISAEFLIGKL
LSNNLINLGL YDDVKKELAD AGKDLIEVEE VELEPSLGNG GLGRLAACFL DSIATLGLNG
DGVGLNYHFG LFQQVLKNNE QTTVPNFWLT EQNLLVKSSR SYQVPFADFT LTSTLYDIDV
PGYKMATKNR LRLFDLDSVD ASIIEDGIDF DKTDIARNLT LFLYPDDSNK KGELLRIFQQ
YFMVSNGAQL IIDEAIEKGS NLHDLADYAV IQINDTHPSM VIPEMIRLLT ERGISLDEAI
NIVKNMTAYT NHTILAEALE KWPLEFLEEV VPHLVPIIKE LDKRVKAEYA DPAVQIIDEH
DRVHMAHMDI HYGYSVNGVA ALHTEILKNS ELKAFYDIYP EKFNNKTNGI TFRRWLMHAN
PRLSNYIDSL IGRDWHHDAS KLEDLLEFSG KADVKAELEK IKAHNKRKLV RHLKEHQVVE
INPESIFDIQ IKRLHEYKRQ QMNALYVIHK YLDIKAGNIP ARPITVFFGG KAAPAYTIAQ
DIIHLILCLS EVIANDPEVS PYLQVVMVEN YNVTAASFLI AAGDISEQIS LASKEASGTG
NMKFMLNGAL TLGTSDGANV EIHELVGDDN IYIFGEDSET VIDLYAKEAY KSSEFYARKA
IKPLVDFIVS DAVLAVGKKE RLERLYNELI NKDWFMTLLD LEDYIETKER MFADYEDRDV
WLEKVLVNIA KAGFFSADRT IAQYNDEIWH LN
//
