ID A0A0N1NF55_9ACTN Unreviewed; 917 AA.
AC A0A0N1NF55;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=OK006_0741 {ECO:0000313|EMBL:KPI05454.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI05454.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI05454.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI05454.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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:KPI05454.1}.
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DR EMBL; LJCU01000236; KPI05454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NF55; -.
DR PATRIC; fig|1592326.3.peg.7431; -.
DR Proteomes; UP000037912; 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 ECO:0000313|EMBL:KPI05454.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPI05454.1}.
FT DOMAIN 42..151
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 660
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 917 AA; 101438 MW; 93490B05BDF00001 CRC64;
MRRVVETPSP LPSSVTYIPP HTSFVKVELV KAIRRFTVRP VLPDALHPLS DLARNLRWSW
HAETRDLFQS VDPERWTASD GDPVRMLGSV PPHRLAELAE DRRFLRRLAA VADDLRDYVT
GDRWYQTQTQ IPDLPAAIAY FSPEFGITAA LPQYSGGLGI LAGDHLKAAS DLGVPLIGVG
LLYRHGYFRQ SLSRDGWQQE HYPVLDPNEL PLVPLRESDG TPAQVTLALP GARALRARIW
LAQVGRVPLL MLDSDVEEND HGERGVTDRL YGGGSEHRLL QEMLLGIGGV RAVRTYCRLT
GHAQPEVFHT NEGHAGFLGL ERIAELAEGQ DGQDGQEGDD GNGGLDFEAA LESVRAGTVF
TTHTPVPAGI DRFDRELVAH HFGPDAELPR IDVERILGLG METYPGGEPN LFNMAVMGLR
LGQRANGVSL LHGHVSREMF SGLWPGFDPD EVPITSVTNG VHAPTWVAPE VFRLGARQIG
AQRTEDAMTV GGSDRWDAVA DIADQEIWDL RRVLREQLVL EVRERLHASW RQRGAGTAEL
GWIDGVLDPD VLTIGFARRV PSYKRLTLML RDRDRLMDLL LHAERPIQIV VAGKAHPADD
GGKRLVQELV RFADDPRVRH RIVFLPDYGM AMAQKLYPGC DIWLNNPLRP LEACGTSGMK
AALNGCLNLS VLDGWWDEWF QPDFGWAIPT ADGTATDDDR RDDLEAAALY ELLEQRVAPR
FYERGQHGLP DRWIEMVRQT LTHLGPKVLA GRMVREYVER LYAPAARAHR ALAPEAAREL
AAWKSRVRAA WPRVTVDHLE ASAATTTAEL GTTLSLRVRV ALADLAPDDV EVQAVSGRVD
SQDRIADASC VPLKPAGGPD LEGRWVYEGP LSLDRTGPFG YTVRILPTHR LLASGAELGL
VTMPSEEVGE EAGVLMR
//
