ID A0A101SXE9_9ACTN Unreviewed; 872 AA.
AC A0A101SXE9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=AQJ66_22665 {ECO:0000313|EMBL:KUN81877.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN81877.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN81877.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN81877.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-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:KUN81877.1}.
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DR EMBL; LMWX01000039; KUN81877.1; -; Genomic_DNA.
DR RefSeq; WP_061925382.1; NZ_KQ948862.1.
DR AlphaFoldDB; A0A101SXE9; -.
DR STRING; 285568.AQJ66_22665; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000053024; 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 CDD; cd04299; GT35_Glycogen_Phosphorylase-like; 1.
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:UP000053024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 615
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 872 AA; 96260 MW; D9772681F5678CF7 CRC64;
MKAIRRFTVR PVLPEPLRPL SDLARNLRWS WHAETRDLFQ SVDPEGWAAA KGDPVRLLGG
VRPARLAELA GDRRFRRRLT AAADDLNDYL TGDRWYQSQG DGLPAAVAYF SPEFGITAAL
PQYSGGLGIL AGDHLKAASD LGVPLIGVGL LYRHGYFRQT LSRDGWQQEH YPVLDPHELP
VTQLKEADGT PAQVSLALPG GRALHARIWL ARVGRVPLLM LDSDVEENDL GERGVTDRLY
GGGSEHRLLQ EMLLGIGGVR AVRTYCRLTG HPEPEVFHTN EGHAGFLGLE RIAELCADGL
DFDAALEAVR SGTVFTTHTP VPAGIDRFDR ELVARHFGTD AELPRIDVQR ILALGMETYP
GGEPNLFNMA VMGLRLAQRA NGVSLLHGHV SREMFAGLWP GFDAEEVPIT SVTNGVHAPT
WVAPEVFRLG ARQIGAQRAE DALTVGGSER WDSVTEIPDQ EIWELRRTLR EQLVQEVRER
LRASWRQRGA GDAELGWVDG VLDPDVLTIG FARRVPSYKR LTLMLRDRDR LMELLLHPER
PLQIVVAGKA HPADDGGKRL VQELVRFADD PRVRHRVVFL PDYGMAMAQK LYHGCDVWLN
NPLRPLEACG TSGMKAALNG CLNLSVLDGW WDEWFQPDFG WAIPTADGAG TDPDRRDDIE
AAALYDLLEQ RVTPRFYERG RGGLPDRWIQ MVRQTLGLLG PKVLAGRMVR EYVDRLYAPA
ALSHRALTPD TARELAAWKA RVRAAWSRVS VDHVETTATT ATAELGTTVG LRVRVGLGDL
EPDDVEVQAV SGRVDAEDRI TDATTVPLKP AGAPDLEGRR LYEGPLSLDR TGPYGYTVRI
LPSHRLLASA AELGLVTVPS QDVVEGAGVL LR
//
