ID A0A1H5JDQ4_9ACTN Unreviewed; 872 AA.
AC A0A1H5JDQ4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=SAMN05216489_06883 {ECO:0000313|EMBL:SEE50632.1};
OS Streptomyces sp. 3213.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855348 {ECO:0000313|EMBL:SEE50632.1, ECO:0000313|Proteomes:UP000198754};
RN [1] {ECO:0000313|EMBL:SEE50632.1, ECO:0000313|Proteomes:UP000198754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3213 {ECO:0000313|EMBL:SEE50632.1,
RC ECO:0000313|Proteomes:UP000198754};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNTK01000001; SEE50632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5JDQ4; -.
DR STRING; 1855348.SAMN05216489_06883; -.
DR Proteomes; UP000198754; 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:UP000198754};
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; 95773 MW; 7AF60A296890B038 CRC64;
MKAIRRFTVR PVLPEPLRPL SDLARNLRWS WHAETRDLFQ SVDPERWTAS EGDPVRLLGS
VSAERLAELA EDHRFLRRLT EVAGDLADYV GGDRWYQAQS GELPAAVAYF SPEFGVTAAL
PQYSGGLGIL AGDHLKSASD LGVPLIGVGL LYRHGYFRQS LSRDGWQQET YPVLDPNELP
VALLREDDGS PAQVSIALPG GRSLRARIWL AQVGRVPLLM LDSDVEENDL GARGVTDVLY
GGGSEHRLLQ EMLLGIGGVR AVRTYCRLTG HPEPEVFHTN EGHAGFLGLE RIAELCDAGL
DFDAGLEAVR AGTVFTTHTP VPAGIDRFDR ELVATHFGPD AELPRMDVGN ILRLGMETYP
GGEPNLFNMA VMGLRLGQRA NGVSLLHGSV SREMFSGLWP GFDPEEVPIT SVTNGVHAPT
WVAPEVFRLG ARQIGAQRTE DAMSVGGSDR WDAVAEIPDQ DIWELRRDLR EQLVVEVRER
LRASWRQRGA GSAELGWIDG VLDPDVLTIG FARRVPSYKR LTLMLRDRDR LMDLLLHPDH
PIQIVVAGKA HPADDGGKRL VQELVKFADD PRVRHRIVFL PDYGMAMAQK LYPGCDIWLN
NPLRPLEACG TSGMKAALNG CLNLSVLDGW WDEWFQPDFG WAIPTADGTG TDPDHRDDVE
AAALYDLLEQ RVTPRFYERG QDGLPDRWIE MVRQTLTLLG PKVLAGRMVR EYVERLYTPA
AHAHRTMTPD AARELAAWKG RVRGAWHGVT VDHVETSAAT ATAELGTTLN LRVRVGLGGL
GPDDVEVQAV SGRVDPEDRI GDGVAVPLKP VGGPDAEGHW LYEGPLALDR TGPYGYTVRI
LPAHRLLASS AELGLVAVPL EDGVEGAGVL MR
//
