ID A0A0Q5E1M8_9MICO Unreviewed; 857 AA.
AC A0A0Q5E1M8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=ASF68_03370 {ECO:0000313|EMBL:KQQ51500.1};
OS Plantibacter sp. Leaf314.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Plantibacter.
OX NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ51500.1, ECO:0000313|Proteomes:UP000051200};
RN [1] {ECO:0000313|EMBL:KQQ51500.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ51500.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ51500.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ51500.1,
RC ECO:0000313|Proteomes:UP000051200};
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:KQQ51500.1}.
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DR EMBL; LMOB01000001; KQQ51500.1; -; Genomic_DNA.
DR RefSeq; WP_056006804.1; NZ_LMOB01000001.1.
DR AlphaFoldDB; A0A0Q5E1M8; -.
DR STRING; 1736333.ASF68_03370; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000051200; 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:UP000051200};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..857
FT /note="glycogen phosphorylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006247562"
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 857 AA; 94018 MW; 1AE3804D0EE80BED CRC64;
MKAIRRFTVR ALIPESLTSL TALAANLRWS WHEPTQRLFD EIAPDVWRES GHDPITGLGL
VTPERLAELA ADADFVGRAE ALHADLRRYL EEPRWYQGLP DPKPQTIAYF SPEFGVAAAL
PQYSGGLGIL AGDHLKSASD LGVPLVGVGL LYRSGYFAQS ITNDGWQQES YPVQDPDGLP
LTVLREPDGT PVTVTLALPE DRSLSARVWI AEVGRVPLLL LDTDIPENVA ELRAVTDRLY
GGGGEHRLHQ ELLLGIGGVR AIKQWSELTD HPLPQVYHSN EGHAGFLGLE RISDLVGNGL
SFDEALQLVR GGTVFTTHTP VPAGIDRFEN DVIERYFSGD LLPGVAAPDV LALGDETANG
GSPEVFNLAI MGLRLAQRAN GVSRLHGEVS RAMFRGLWPG FDVSDVPITS ITNGVHAPSW
TDPALLGFAD ERWGGIEPGR ADWAGPSVSD DELWMLKRGM RERLVADVRR RIADGYRAQN
PLAVVPSWID ELLDPEVLTI GFARRVPGYK RLTLMMRDPD RLRSLLLHPD RPIQIVVAGK
AHPADDEGKR LIQRLVQFAQ DPLLRARIVF LPDYGIGMAK TLYPGCDVWL NNPLRPLEAC
GTSGMKAALN GALNLSILDG WWDEYADGEN GWAIPSADGT PDDDERDALE AASLYDVIEH
QLAPRYYDRE HGAPPWRWLQ MVRHTISTLS EPLSADRMVR EYTERMYLPA AEMERALSAS
DQLGARDLAA YKRRVRDAWP QLAVAHVESG GVDEVPQVGD VLRLRAYVQL GSLSPDDVTV
EVVSGVPGAA GELLDVGSQP LEQQQTPSTS RPEHTLEYAG TLPLDRAGGF GYTVRIVPKH
ELLLTPAELG LVALADQ
//
