ID A0A3P3W1Y2_9MICO Unreviewed; 852 AA.
AC A0A3P3W1Y2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN Name=glgP {ECO:0000313|EMBL:RRJ88784.1};
GN ORFNames=EG850_01195 {ECO:0000313|EMBL:RRJ88784.1};
OS Gulosibacter macacae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Gulosibacter.
OX NCBI_TaxID=2488791 {ECO:0000313|EMBL:RRJ88784.1, ECO:0000313|Proteomes:UP000274391};
RN [1] {ECO:0000313|EMBL:RRJ88784.1, ECO:0000313|Proteomes:UP000274391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102482-1 {ECO:0000313|EMBL:RRJ88784.1,
RC ECO:0000313|Proteomes:UP000274391};
RA Li G., Jiang Y.;
RT "YIM 102482-1 draft genome.";
RL Submitted (NOV-2018) 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:RRJ88784.1}.
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DR EMBL; RQVS01000001; RRJ88784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3W1Y2; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000274391; 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; 2.
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:UP000274391};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..123
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 613
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 852 AA; 95145 MW; BDAC149125EAD9E4 CRC64;
MKAFDSLNVQ TILPEALRPL EVISKNLRWS WRPESERLFR SIDDHLWRET GHNPVVLLKR
ISASRAEELA NDAEFLHRMQ QEVEELETYL ALDRWYEKQT RGTEDADTIV AYFSMEFGIA
QSLPIYSGGL GVLSGDHMKS ASDLGAPIIG IGLLYTYGYF SQTLSREGWQ QERYTQHAPE
DLAVTPVLDK TGEQLHVSVT FPGDREVQIA VWKAQVGNAP LLLLDTNIPA NDEDMRSITD
RLYGGDAEHR IKQELVLGVG GVRAVQAYCE IEGLSQPDVY HMNEGHAGFS GTERIGQLIR
QGETFETALA VVRASTIFTT HTPVPAGIDR FDMNLAARYL QADEQGLSKL APGVPVARVM
ELGAEDDLSR FNMAHLGLRS AQYANGVAKL HGKVSRGMFR DLYPNFDQRE VPITSITNGV
HIPTWTRGPI KSVVAAMSGG RDLATANHWR EADAVGSPEL WRIRNELRSD LITRARRLVR
QSWVARGAQE AELGWTNNIL DDKVLTVGFA RRVSTYKRLT LMLQNPERLR RILTNPDRPV
QFIIAGKAHP ADMGGKQLLQ ELVRFADEAG VRDRIIFLPD YDVTIAKFLV AGSDIWLNNP
IRPQEASGTS GMKAVMNGCL TLSISDGWWD EFRDDTVGWT IPEAVTNDER QRDLLESEAL
YDLLEHEIAP LFYDRDEQGI PQDWVSKVRR SMSIVGPQVS AERMVRDYCT ELYMPAGRSA
RAALNEGAAR EFAEWQQKVR ASWPLVVVHD VRNETASPVA GGNVEITAKV SLGDLEAKDV
KVEAIIGRVD EAGNLVAPRS VEMALNGWDD DRWGASIEID DPGNFGYTVR AVPKHALLRS
PAEMGLVQLP RK
//
