ID A0A066Z0B6_9ACTN Unreviewed; 893 AA.
AC A0A066Z0B6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=KCH_51020 {ECO:0000313|EMBL:KDN83620.1};
OS Kitasatospora cheerisanensis KCTC 2395.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN83620.1, ECO:0000313|Proteomes:UP000027178};
RN [1] {ECO:0000313|EMBL:KDN83620.1, ECO:0000313|Proteomes:UP000027178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN83620.1,
RC ECO:0000313|Proteomes:UP000027178};
RA Nam D.H.;
RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL Submitted (MAY-2014) 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:KDN83620.1}.
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DR EMBL; JNBY01000095; KDN83620.1; -; Genomic_DNA.
DR RefSeq; WP_035866310.1; NZ_KK853997.1.
DR AlphaFoldDB; A0A066Z0B6; -.
DR PATRIC; fig|1348663.4.peg.4938; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000027178; 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 ECO:0000313|EMBL:KDN83620.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDN83620.1}.
FT DOMAIN 13..123
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 620
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 893 AA; 97249 MW; 5F9CDE908312F2FE CRC64;
MKAIRRFTVR TVLPEQLQPL HELALNLRWS WHPETRELFR SVDPDVWAAV GEDPVRLLGE
VPAARLAALA TDRRFLRRLG DLADDLRDYL TGPRWYQSAN DLGDALPAGI AYFSPEYGIA
AALPQYSGGL GILAGDHLKA ASDLGVPVIG VGLFYRHGYF RQSLSRDGWQ QERYPLLDPD
ALAVTLLREA DATPCRIDLA LPGGRTLAAQ VWRAQVGRVP LLLLDSDIEA NTPAERDVTD
RLYGGGSEHR LLQEILLGIG GVRAVRTYCR LTGHPEPEVF HTNEGHAGFL GLERIAELTT
AHPGLGFADA LEAVRAGTVF TTHTPVPAGI DRFDRELIAR HFGGDAALPG VPVDQVLALG
AENWAGGDPK LFNMAAMGLR LAQRANGVST LHGAVSREMF RGLWPGFDAP EVPITSITNG
VHAPTWIDPA VVRLGATEIG QERAEEAMAV GTASQWTGLE RIGNSEVWEL RRTLRAQLVD
EARRRLRASW QQRGAGEAEL GWTGAVLDPD VLTIGFARRV PSYKRLTLML RDPVRLRALL
LHPERPVQIV VAGKAHPADD GGKRLIQHLV AFADDPAVRH RIVFLPDYDM AMAKALYPGC
DVWLNNPLRP LEACGTSGMK AALNGCLNLS ILDGWWDEWY DGQNGWAIPT ADGGTGEGVL
DPESKEAERR DDIEAAALYD LIEHQVAARF YDRAADGLPH RWISMVRHTL VTLGPKVLAG
RMVREYVERL YVPAAEARRR LAGEASDHAG AKALAGWKAT VRDAWPSVRV EHVEADGVGE
AQELGATLAL RVQVALGRLR PEDVEVQVVS GRVDESDRIS EATTLALKPA SGSGGTDLDG
RVRYEGHLEL SRTGPFGYTV RVLPAHPRLA SSAELGLVAV PVEPGGLEAG VLR
//
