ID A0A0S9Q420_9ACTN Unreviewed; 862 AA.
AC A0A0S9Q420;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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=ASF47_11830 {ECO:0000313|EMBL:KQP64622.1};
OS Nocardioides sp. Leaf285.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP64622.1, ECO:0000313|Proteomes:UP000051495};
RN [1] {ECO:0000313|EMBL:KQP64622.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP64622.1,
RC ECO:0000313|Proteomes:UP000051495};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP64622.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP64622.1,
RC ECO:0000313|Proteomes:UP000051495};
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:KQP64622.1}.
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DR EMBL; LMNH01000003; KQP64622.1; -; Genomic_DNA.
DR RefSeq; WP_056864164.1; NZ_LMNH01000003.1.
DR AlphaFoldDB; A0A0S9Q420; -.
DR Proteomes; UP000051495; 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:UP000051495};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..124
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 618
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 862 AA; 93915 MW; D886FF5DA34EACA8 CRC64;
MRAIRRFTVR PVLPESLAAL GELAGNLRWC WHPPTQDVFA AVDPALWESS GRDPVRLLGA
VSRARLDALA HDEAFLARLE EARADLAAYL GSQRWYQRAT ASGSLEGPRA VAYFSPEFGI
TSVLPQYSGG LGILAGDHLK AASDLGVPVV GVGLLYRHGY FTQALSREGW QQETYPVLDP
DELPISLLRE PSGERALISL AMPDGPELLA RIWVASVGRV PLLMLDTDVE GNPEHYVDVT
DRLYGGTSEH RLRQEMLLGV GGVRALRAFA RITGHPAPEV FHTNEGHAGF LGLERIRELT
ADPAGPGLDF DTALEIGRAS TVFTTHTPVP AGIDRFSRTL VEQYFSDAGP TPGVPVERVL
ALGAEDYPGG DAGVFNMAVM GFRLAQRANG VSLLHGEVSR GMFHGLWPAF DEAEVPIGSI
TNGVHAPTWV AREILELAAG EGADPDGDDT DAFWAAVDTV PAERMWAVKR QLRERLVHEA
RRRLAASWEH RGASRAELGW VDSALHPDVL TVGFARRVPS YKRLTLMLRD PARLRRLLLD
PDRPVQLVIA GKSHPADDGG KRLIQELVRF ADDPEVRHRI VFLPDYDIAM AQPLYPGCDV
WLNNPLRPYE ACGTSGMKAA LNGGLNLSVL DGWWDEWYDG ENGWAIPSAD GVEDTERRDD
LEADALYTLL ENEVAPRFYD VDAAGVPTRW VEMLRHTLKS LGPKVLATRM VRDYVRTLYA
PAAATSRALG ADESGARELA TWKARVRAAW PGVRVEHVES SGVGDAPEVG AVLSVRAFVA
LGDLAPDDVT VQLVHGRATG EDELVDTVTV DLAVGETYEG GRHRFDGEVV LDHSGPFGYT
ARVVPRHPLL ASVAELGVVA LP
//
