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Database: UniProt
Entry: T0TUB6_9STRE
LinkDB: T0TUB6_9STRE
Original site: T0TUB6_9STRE 
ID   T0TUB6_9STRE            Unreviewed;       386 AA.
AC   T0TUB6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   ORFNames=HSISS3_1509 {ECO:0000313|EMBL:EQC74666.1};
OS   Streptococcus sp. HSISS3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1316412 {ECO:0000313|EMBL:EQC74666.1};
RN   [1] {ECO:0000313|EMBL:EQC74666.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSISS3 {ECO:0000313|EMBL:EQC74666.1};
RA   Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA   Kleerebezem M.;
RT   "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT   Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL   PLoS ONE 8:E83418-E83418(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}.
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:EQC74666.1}.
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DR   EMBL; ASKH01000022; EQC74666.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0TUB6; -.
DR   PATRIC; fig|1316412.3.peg.609; -.
DR   HOGENOM; CLU_010198_3_1_9; -.
DR   Proteomes; UP000015931; 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: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; IPR000811; Glyco_trans_35.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR   Pfam; PF00343; Phosphorylase; 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|RuleBase:RU000587};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000587}.
SQ   SEQUENCE   386 AA;  44248 MW;  23FF6785D9C661DF CRC64;
     MDIHFSTSVN GVAALHTEIL KSSELKPFYD LYPERFNNKT NGITFRRWLE FSNQELADYI
     KELIGDGYLT DATQLEKLAA FADDPAVHKR LAEIKYDNKL SLKRYLKANK GIDLDENSII
     DTQIKRFHEY KRQQMNALYV IHKYLEIKKG NLPKRKITII FGGKAAPAYV IAQDIIHLIL
     SLSELINNDP EVSKYLNVHL VENYNVTVAE HLIPATDISE QISLASKEAS GTGNMKFMLN
     GALTLGTMDG ANVEIAELVG PENIFTFGKD SDTIIDLYEK EGYVSRDYYK KDANIKAAVD
     FIVSEDLVKL GDKERLERLH KELISKDWFM TLIDLAEYID KKEEVYAAYE DQDAWNKKVV
     YNIAEAGFFS SDRTIEQYDK DIWHTK
//
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