ID T1ZH45_STRIT Unreviewed; 753 AA.
AC T1ZH45;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN ORFNames=SIR_1819 {ECO:0000313|EMBL:AGU77150.1};
OS Streptococcus intermedius B196.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus; Streptococcus anginosus group.
OX NCBI_TaxID=862967 {ECO:0000313|EMBL:AGU77150.1, ECO:0000313|Proteomes:UP000016233};
RN [1] {ECO:0000313|EMBL:AGU77150.1, ECO:0000313|Proteomes:UP000016233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B196 {ECO:0000313|EMBL:AGU77150.1,
RC ECO:0000313|Proteomes:UP000016233};
RX PubMed=24341328; DOI=10.1186/1471-2164-14-895;
RA Olson A.B., Kent H., Sibley C.D., Grinwis M.E., Mabon P., Ouellette C.,
RA Tyson S., Graham M., Tyler S.D., Van Domselaar G., Surette M.G.,
RA Corbett C.R.;
RT "Phylogenetic relationship and virulence inference of Streptococcus
RT Anginosus Group: curated annotation and whole-genome comparative analysis
RT support distinct species designation.";
RL BMC Genomics 14:895-895(2013).
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; CP003857; AGU77150.1; -; Genomic_DNA.
DR RefSeq; WP_021003327.1; NZ_UZBH01000005.1.
DR AlphaFoldDB; T1ZH45; -.
DR KEGG; sib:SIR_1819; -.
DR PATRIC; fig|862967.3.peg.1838; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000016233; 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 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:UP000016233};
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 753 AA; 85406 MW; BD1B35C8FE2871BE CRC64;
MSNLQKFIQQ TYQKGIAECS NEELYIALLN YTKLASAQKP VNTGKKKLYY ISAEFLIGKL
LSNNLINLGL YDNVKKELAD AGKDLIEVEE VELEPSLGNG GLGRLAACFL DSIATLGLNG
DGVGLNYHFG LFQQVLKNNE QTTIPNFWLT EQNWLVKSSR SYQVPFANFT LTSTLYDIDV
PGYKTATKNR LRLFDLDSVD ASIIEDGIDF DKTDIARNLT LFLYPDDSNK QGELLRIFQQ
YFMVSNGAQL ILDEAIEKGS NLHDLADYAV VQINDTHPSM VIPELIRLLT ARGIELDEAI
SIVRSMTAYT NHTILAEALE KWPLEFLEEV VPQLVPIIKE LDKRVKAEYA DPAVQIIDEH
NRVHMAHLDI HYGYSVNGVA ALHTEILKNS ELKAFYDIYP EKFNNKTNGI TFRRWLMHAN
PRLSNYIDSL IGRDWHHDAS HLEELLEVSS KADVKAELEK IKAHNKRKLA RHLKEHQGVE
INPNSIFDIQ IKRLHEYKRQ QMNALYVIHK YLDIKAGNIP ARPITVFFGG KAAPAYTIAQ
DIIHLILCLS EVIANDPEVS PYLQVVMVEN YNVTAASFLI AAGDISEQIS LASKEASGTG
NMKFMLNGAL TLGTMDGANV EIAELVGQDN IYIFGEDSET VIDLYAKEAY KSSEFYARQT
IKPLVDFIVS DAVLAVGKKE RLERLYNELI HKDWFMTLLD LEDYIETKER MFKDYEDRDV
WLEKVLINIA KAGFFSADRT IAQYNDEIWH LNA
//
