ID A0A0T2KTM6_9MICO Unreviewed; 852 AA.
AC A0A0T2KTM6;
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=ASD65_00360 {ECO:0000313|EMBL:KRA23040.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA23040.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA23040.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA23040.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA23040.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA23040.1,
RC ECO:0000313|Proteomes:UP000051216};
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:KRA23040.1}.
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DR EMBL; LMGU01000001; KRA23040.1; -; Genomic_DNA.
DR RefSeq; WP_056216896.1; NZ_LMGU01000001.1.
DR AlphaFoldDB; A0A0T2KTM6; -.
DR STRING; 1736570.ASD65_00360; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000051216; 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:UP000051216};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 606
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 852 AA; 92845 MW; 02E7CC882C388B51 CRC64;
MKAIRTFTVR PVLAAPLAPL DRLASNWRWS WSRSTHALFA SMDPQQWSEI GENPARMLGA
IGQQRLDELA HDADFVARVR EEDDRLSAYL TGDRWFQQLQ GDKPTGIAYF SPEFGVDGSL
PQYSGGLGIL AGDHLKSASD LGVPLTGVGL FYRAGYFRQS IGDDGWQRES YPLLDPYGLG
LTLLRDDTGA PVEISLALPG DRHLAARIWV ADIGRIPLLL LDSATPSNTE EMRRVTDRLY
GGGGEHRLLQ ELLLGVGGVR AVRAYCAITG RSTPEVYHTN EGHAGFQGLE RISELITQQG
LGFDEALAQV RASTVFTTHT PVPAGIDRFP RDLIASYLAS GLFAGLDSER ALALGLEEWE
GGDHGTFNMA VLGLHLGQHA NGVSQLHGEV SRGMFGMLWP GIDTDEVPIT SITNGVHAPT
WVHPALKAVS ERAFGDAYTD THDWTDAAAV SDGELWGVRS LMKSEMVAEA RRRVAASAVE
LSGRAPAWID DLLDPEVLTI GFARRVPTYK RLTLMLRDPE RLTRLLTDPE RPVQIVIGGK
SHPADDSGKI LIQELVRFSR DPKVRGRIVF LPDYDITLAK TLYPGCDVWL NNPLRPLEAC
GTSGMKAALN GVLNLSILDG WWDEWYDGEN GWAIPTADTA SGDEERDDVE SAALYDLIEH
QLVPKFYERE GGIPLAWLAM VRHTMTTLGQ KATSDRMVRD YVTRLYVPAS EHDAALRADG
FAEAKALAAF ITRVKASWPA VHIESVDSSG IPQQAQAGDT LEVRASVRLD GLSPDDVAVE
LAYGRTDEDD DLAADHSVHR LAPAGPAVDG ITTFSCTLPL TVTGTFGYTV RAVPAHSQLV
SPVELGLVTY AS
//
