ID   A0A0B5IG82_9ACTN        Unreviewed;       849 AA.
AC   A0A0B5IG82;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   ORFNames=SVTN_26270 {ECO:0000313|EMBL:AJF67359.1};
OS   Streptomyces vietnamensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF67359.1, ECO:0000313|Proteomes:UP000031774};
RN   [1] {ECO:0000313|EMBL:AJF67359.1, ECO:0000313|Proteomes:UP000031774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMV4.0001 {ECO:0000313|Proteomes:UP000031774};
RA   Deng M.R., Guo J., Ma L.Y., Feng G.D., Mo C.Y., Zhu H.H.;
RT   "Complete genome sequence of Streptomyces vietnamensis strain GIMV4.0001, a
RT   genetic manipulable producer of the benzoisochromanequinone antibiotic
RT   granaticin.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00006047}.
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DR   EMBL; CP010407; AJF67359.1; -; Genomic_DNA.
DR   RefSeq; WP_041131315.1; NZ_CP010407.1.
DR   AlphaFoldDB; A0A0B5IG82; -.
DR   STRING; 362257.SVTN_26270; -.
DR   KEGG; svt:SVTN_26270; -.
DR   HOGENOM; CLU_015112_0_0_11; -.
DR   Proteomes; UP000031774; 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; 3.
DR   InterPro; IPR011834; Agluc_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   InterPro; IPR024517; Glycogen_phosphorylase_DUF3417.
DR   InterPro; IPR035090; Pyridoxal_P_attach_site.
DR   NCBIfam; TIGR02094; more_P_ylases; 1.
DR   PANTHER; PTHR42655; GLYCOGEN PHOSPHORYLASE; 1.
DR   PANTHER; PTHR42655:SF1; GLYCOGEN PHOSPHORYLASE; 1.
DR   Pfam; PF11897; DUF3417; 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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000460-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031774};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..118
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         589
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   849 AA;  91996 MW;  99506EF8C494DDE0 CRC64;
     MKAIRRFTVR PVLPDTLRPL ADLAHNLRWS WHEPTRALFD SLAPEGLAGA DPVRVLGALE
     APRLAALAAD QEFLDRLRAV AEDLDQYLHA PRWYQGRPGD APAAVAYFSP EFGVAAALPQ
     YSGGLGILAG DHLKSASDLG VPLVGVGLLY RHGYFRQSLG RDGWQQEQYP VLDPGELPVT
     LLREADGTPA RITLALPGGR SLHAQIWIAQ VGRVPLLMLD SDVEENAPGE RSVTDRLYGG
     GSEHRLLQEM LLGIGGVRAV RTYTRLTGHP APEVFHTNEG HAGFLGLERV RELQGEGLDF
     DSALEAVRAG TVFTTHTPVP AGIDRFDRAL VARHLGDDGA LPGVDLGRIL ALGDETPLGG
     EPGVFNMAAM GLRLAQRANG VSTLHGAVSR SMFAGLWPGF DADEVPITSI TNGVHAPTWV
     APEAARTGPD ASDRELWELR RTLRERLVAD VRDRLRASWR QRGAAAAELG WTESVLDPDV
     LTIGFARRVP SYKRLTLMLR DKDRLRALLL HPERPVQLVV AGKAHPADDG GKKLVQELVR
     FADDPRVRHR IVFLPDYGME MARGLYPGCD VWLNNPLRPL EACGTSGMKA ALNGCLNLSV
     LDGWWDEWYE PEFGWAIPTA DGAAAADEDR RDDLEAAALY ELIERRVAPR FYDRGPDGVP
     SGWTAMVRRT LADLGPKVLA DRMVREYVER LYVPAAGSRR ALTPGRARDL AAWKARVRAA
     WPAVAVDHVE IGDDLAEVDA ELGATPVVRV RVALGGLEPD DVEVQAVTGR VDADDTLAAT
     RTVTLKPAGG PDLEGRLPYA GTLELDRTGS FGCTVRVLPA HPLLAHPAEL GLAALPGETT
     GEGAGVLLR
//