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Database: UniProt
Entry: A0A0Q8UM91_9ACTN
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ID   A0A0Q8UM91_9ACTN        Unreviewed;       861 AA.
AC   A0A0Q8UM91;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE            EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN   ORFNames=ASE19_19800 {ECO:0000313|EMBL:KRC46118.1};
OS   Nocardioides sp. Root79.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC46118.1, ECO:0000313|Proteomes:UP000051414};
RN   [1] {ECO:0000313|EMBL:KRC46118.1, ECO:0000313|Proteomes:UP000051414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root79 {ECO:0000313|EMBL:KRC46118.1,
RC   ECO:0000313|Proteomes:UP000051414};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC46118.1, ECO:0000313|Proteomes:UP000051414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root79 {ECO:0000313|EMBL:KRC46118.1,
RC   ECO:0000313|Proteomes:UP000051414};
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:KRC46118.1}.
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DR   EMBL; LMIP01000015; KRC46118.1; -; Genomic_DNA.
DR   RefSeq; WP_056895894.1; NZ_LMIP01000015.1.
DR   AlphaFoldDB; A0A0Q8UM91; -.
DR   OrthoDB; 9760804at2; -.
DR   Proteomes; UP000051414; 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:UP000051414};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..125
FT                   /note="DUF3417"
FT                   /evidence="ECO:0000259|Pfam:PF11897"
FT   MOD_RES         616
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ   SEQUENCE   861 AA;  94443 MW;  F9B9D1E040E35AF4 CRC64;
     MRAIRRFTVR PVLPDALASL GELAANLRWS WHPPTQALFE EIDADRWHEV GHDPLRLLGE
     VPGERWAELA ADEGYVARVA DVRADLASYL TGERWYQRAS AAAPDETWPA SIAYFSPEFG
     ITAVLPQYSG GLGILAGDHL KAASDLGAPI VGVGLLYRHG YFKQALSREA WQVESYPVLD
     PDGLPISLLH EHDGNRATIS IRMPGGPDLL ARIWVASVGR VPLLLLDTDF EENPEQYRLI
     TDRLYGGNTE HRLRQELLLG VGGVRALRAY SRITGAPAPE VFHTNEGHAG FLGVERIREL
     TADSDLDFAT ALEIGRTSTV FTTHTPVPAG IDRFPRTLVE QYLGEQGSTP GVPVELVLGL
     GSEDYEGGDP GVFNMAVMGF RLAQRANGVS QLHGHVSRGM FNGLWPAFDE AEVPITSITN
     GVHAPTWVAP EVVALASAQG ADWEGDDTEA FWAAFEKVAG TDVWSTKRAL RERLVADARR
     RLRKSWEKRG AAPAELGWID DALDPDVLTI GFARRVPSYK RLTLMLRDPE RLKALLLHPE
     RPVQLVVAGK AHPADDGGKR LIQELVRFAD AEDVRHRIVF LPNYDIALAQ PLYPGCDVWL
     NNPLRPYEAC GTSGMKASLN GGLNLSILDG WWDEWYEPEF GWPIPSADGL EDYSDKRDDL
     EAAALYDLIE NEVAPRFYDV DADGVPVRWV EMLRHTWAQL GPKVLATRMV RDYIAKLYAP
     AAAYSRLLAS TPDGARDLAS WKARVRGAWD GVRVEHVEAA GVGDTVEVGA GLAVHAYVAL
     GELAPGDVEV QLVHGRVDAE DDLVDTAVAP LRLVESYDGG RHRFDGDLEL GRPGPFGYTV
     RVVPKHPLMV APAELGVVAL A
//
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