ID A0A0S9DA68_9MICC Unreviewed; 870 AA.
AC A0A0S9DA68;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Glycogen phosphorylase {ECO:0000313|EMBL:KQO02804.1};
GN ORFNames=ASF21_00035 {ECO:0000313|EMBL:KQO02804.1};
OS Arthrobacter sp. Leaf234.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQO02804.1, ECO:0000313|Proteomes:UP000053418};
RN [1] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KQO02804.1}.
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DR EMBL; LMLU01000001; KQO02804.1; -; Genomic_DNA.
DR RefSeq; WP_055765125.1; NZ_LMLU01000001.1.
DR AlphaFoldDB; A0A0S9DA68; -.
DR STRING; 1736303.ASF21_00035; -.
DR Proteomes; UP000053418; Unassembled WGS sequence.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1}.
FT DOMAIN 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 611
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 870 AA; 94977 MW; 234D9C16C7FC0000 CRC64;
MKAIRRFTVR TVLPEKIAPL GKLAGNLRWS WHLPTSRLFE EIDPAAWAES GHDPVSFLGS
VTREKLEQLA GDDALVQRIQ AVGAALENYL TEPRWYQSLG DDAPRSIAYF SPEYGISAVL
PQYSGGLGIL AGDHLKSASD LGVPLVGVGL LYQAGYFKQS LSRDAWQQET YPVLDPDGLP
LTLLREEDGS AATVVLPLPN GRQLSAHIWR ADVGRVPLLL LDSNVAGNDE AARNVTDRLY
GGGGDQRLQQ ELLLGMGGVK ALRIFQRLTG MPAPEVFHTN EGHAGFLGIE RIRELMDPAN
ESPMSWEEAL TAGRASTVFT THTPVPAGID RFDRSQIEHF FHAGLAPAVP TDRVLALGAE
NYADGDPAKF NMAVMGLRLA QRANGVAKLH GEVSRGMFSG LWPGFDTREV PISSVTNGVH
VPSWVDPEIA DFARSTFGAE SILDPQWNKV YDVPDTDIWA LRRSLRSNLV DDVRQRLRSS
WKKRGAADAE LTWTDSVLDP DVLTIGFARR VPTYKRLTLM LRNPARLKAL LLHPEHPIQL
VIAGKSHPAD EQGKRMIQDL VRFTDDPEVR HRIVFLPNYD IAMARTLFPG CDVWLNNPLR
PLEACGTSGM KAAINGGLNL SVLDGWWDEM YDGDNGWAIP TANNGASADE RDDIEAAALY
DLLETQVGPR FYSLVPAEGA GAAGPSEPSR DGVPHAWIAM IKHTMATLGP AVSAERMLQD
YVEKLYRPAW RAGQEAAADQ FSLAKRTAAW RSRVQGSWPA VQVEHVDSTG VSEDPQIGDS
LTVNAYVSLG GLDPDDVAVE VAYGRALDSD ELSDVTVEDL DVAENLGSGR YLFTGGIRID
HSGSFGYTVR VLPKHTTLAT KAELGLVVNA
//