ID A0A0Q9LUT6_9MICO Unreviewed; 862 AA.
AC A0A0Q9LUT6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ASG70_02105 {ECO:0000313|EMBL:KRE57228.1};
OS Phycicoccus sp. Soil748.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=1736397 {ECO:0000313|EMBL:KRE57228.1, ECO:0000313|Proteomes:UP000051855};
RN [1] {ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|Proteomes:UP000051855};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE57228.1, ECO:0000313|Proteomes:UP000051855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil748 {ECO:0000313|EMBL:KRE57228.1,
RC ECO:0000313|Proteomes:UP000051855};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRE57228.1}.
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DR EMBL; LMSC01000005; KRE57228.1; -; Genomic_DNA.
DR RefSeq; WP_056882646.1; NZ_LMSC01000005.1.
DR AlphaFoldDB; A0A0Q9LUT6; -.
DR STRING; 1736397.ASG70_02105; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000051855; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..127
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 617
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 862 AA; 94778 MW; 5816DC1E49BE06A7 CRC64;
MKAIRRFSVR TVLPEPIAAL GDLASNLRWS WHPPTRDLFE RIDPQRWAKV RKDPVRLLSA
LSPAELAALA ADTGFVGAVA AAKADLDTYL TEPRWYQAWA QAQDEDGAGA PKAIGYFSPE
FGITEVLPQY SGGLGILAGD HLKTASDLGV PIVGVGLFYK TGYFKQSLNR DGWQQETYPV
LDPDGLPLSM LREEDGTPCV ITLGLPGGRQ LHAHVWKAQV GRVPLLLLDS DVPDNDEAAR
NITNRLYGGG GEQRLQQEML LGIGGVRALR LWSRLTGAPA PDVYHTNEGH AGFLGVERIH
ELTQSADLGF EEALEAVRAA TVFTTHTPVP AGIDRFDAEL ISLHFGGDQA VPGVPVDRLL
ALGAEDYPGG QPGMFNMAVM GLRLGGRANG VSQLHGVVSR EMFDGLWPGF DDDEVPISSV
TNGVHAGTWV DRRVYELADK YLGTHDLERD NAWDRIDEVP REAIWATKRD MREQLVVEAR
RRTRSSWKKR GASPAELGWV DDILDPDILT IGFARRVPTY KRLTLMLRDP ARLKRLLLDE
KRPIQLVIAG KSHPADETGK QLIQQMVRFA DDPEIRHRIV FLPNYDIAMA QYLYPGCDVW
LNNPLRPFEA CGTSGMKAAL NGGLNLSILD GWWDEWFDGG NGWAIPTADG VEDAERRDDL
EAAALYDLIE NSVAPRFYDT DEAGLPQNWL SMISHTLRTL GPKVLASRMV RDYTIQLYGP
AARAGWALAG ETYAGARDLA AYKHKVREGW SSVHVDHVES SGVSDSPQIG ETLHVRAYVS
LGDLTPDEVE VEVVHGTARD SDELRDVQCE PLALVESYEG GRHQFAGDFA LARTGSFGYT
VRVLPKHIGL ASTSELGLVA NA
//
