ID A0A0M8VAF0_9ACTN Unreviewed; 853 AA.
AC A0A0M8VAF0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=ADK64_26955 {ECO:0000313|EMBL:KOV61729.1};
OS Streptomyces sp. MMG1121.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV61729.1, ECO:0000313|Proteomes:UP000037687};
RN [1] {ECO:0000313|Proteomes:UP000037687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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}.
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:KOV61729.1}.
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DR EMBL; LGDV01000202; KOV61729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8VAF0; -.
DR STRING; 1415544.ADK64_26955; -.
DR PATRIC; fig|1415544.3.peg.5773; -.
DR Proteomes; UP000037687; 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; 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:UP000037687};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..101
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 596
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 853 AA; 93696 MW; 61AF8C839AF318A1 CRC64;
MSDLARNLRW SWHAETRDLF QSVDPERWAA AEGDPVRLLG SVRPARLAQL AGDRRFLRRL
TAVADDLDDY LTGERWYQAQ ADGLPAAVAY FSPEFGITAA LPQYSGGLGI LAGDHLKAAS
DLGVPLIGVG LLYRHGYFRQ TLSRDGWQQE HYPVLDPNEL PLTRLKEPDG TPAQVSLALP
GGKALLARIW LAQVGRVPLL LLDSDVEEND LGERGVTDRL YGGGGEHRLL QEMLLGIGGV
RAVRTYCRLT GQPEPEVFHT NEGHAGFLGL ERIAELSAGG LDFDSALESV RGGTVFTTHT
PVPAGIDRFD RELVGRHFGP DAELPGIDVQ RILALGMETY PGGEANLFNM AVMGLRLAQR
ANGVSLLHGQ VSREMFAGLW PGFDAEEVPI TSVTNGVHAP TWMAPEVLRL GAREVGAQRA
EDALTVGGSE RWDSVAEIPD EEVWELRRTL REQLVLEVRD RLRASWRQRG AGNAELGWIE
GVLDPDVLTI GFARRVPSYK RLTLMLRDRD RLMELLLHPE RPVQIVVAGK AHPADDGGKR
LVQELVRFAD DPRVRHRIVF LPDYGMAMAQ KLYPGCDIWL NNPLRPLEAC GTSGMKAALN
GCLNLSVLDG WWDEWFQPDF GWAIPTADGA GTDPDRRDDI EAAALYDLLE QRITPRFYER
GRAGLPDRWI QMVRQTLTLL GPKVLAGRMV REYVDRLYAP AAQAHRALTP DTARVLAEWK
TRVRAAWPGV SVDHVETTAT TATAELGTTV SLRVRVALGE LSPDDVEVQA VSGRVDAEDH
ITDATVVPLK PTGAPDLEGR LLYEGPLSLD RTGPYGYTVR ILPAHRLLAS TAEMGLVAVP
VGDVGEGVGV LLR
//
