ID A0A316TDZ7_9ACTN Unreviewed; 871 AA.
AC A0A316TDZ7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, 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=DJ010_16940 {ECO:0000313|EMBL:PWN01721.1};
OS Nocardioides silvaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2201891 {ECO:0000313|EMBL:PWN01721.1, ECO:0000313|Proteomes:UP000245507};
RN [1] {ECO:0000313|EMBL:PWN01721.1, ECO:0000313|Proteomes:UP000245507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2018079 {ECO:0000313|EMBL:PWN01721.1,
RC ECO:0000313|Proteomes:UP000245507};
RA Li C., Wang G.;
RT "Nocardioides silvaticus genome.";
RL Submitted (MAY-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:PWN01721.1}.
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DR EMBL; QGDD01000008; PWN01721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316TDZ7; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000245507; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245507};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..125
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 627
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 871 AA; 95638 MW; 985995C60CE04D4D CRC64;
MRAIRRFTVR PLLPPALAPI GELAANLRWS WHPETQDVFA AVDPDLWAAS GRDPVRLLGE
VPAGRWDELA ADEGFVRRLG EVRADLESYL TAPRWYQRAS ERQPDVAWPR QIAYFSPEFG
ITAVLPQYSG GLGILAGDHL KAASDLGVPI LGVGLLYRHG YFKQSLSREG WQQETYPVLD
PDGLPISLLH EPDPSTGSGG TGKRATISIA MPDGPDLLAR IWVASVGRVP LLMLDTDVEG
NPDHYVDITD RLYGGNSEHR LRQELLLGIG GVRAIRTYCR ITGAPEPEVF HTNEGHAGFL
GIERIRELTV AEDGPRLDLE TAIEVGRAST VFTTHTPVPA GIDRFPRTMV EQYFADAGPT
PGVPVERILA LGAEDYEGGD PGVFNMAVMG FRLAQRANGV SQLHGHVSRG MFNGLWPAFD
EAEVPIGSIT NGVHAPTWVA REVLAVAASY GADPESDDTE GFWAAVDKVP AGELWGTKRM
LRSRLVDEAR RRLARSWEKR GSARAELGWI DSALDPDVLT IGFARRAASY KRLTLMMRDP
ERLKRLLLHP ERPVQLVIAG KAHPADDGGK KLIQDIVRLS DDPEIRHRIV FLPNYDIAMA
QPLYPGCDVW LNNPLRPYEA CGTSGMKAAL NGGLNLSVLD GWWDEWFDGD NGWAIPTADG
VDDVDHRDDL EAAALYDLIE HEVAPRFYDL DHDGIPVRWV EMLRHTWKSL GPKVLATRMV
SDYVRQLYAP AATNARALNS DYAGARELAQ WKARVRAGWS GVRVEHVETH GVGDEPLVGS
PMTVRSYVAL GELSPDDVEV QLVSGRVNAE DVLVDPVTTV LQPTESYDGG RHRFDAEVGL
ARSGPFGYTV RVVPSNPLLV APAELGVVTV A
//
