ID A0A0B5DMR6_9ACTN Unreviewed; 877 AA.
AC A0A0B5DMR6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=BJY54_004530 {ECO:0000313|EMBL:MBB4793918.1}, CP978_23370
GN {ECO:0000313|EMBL:QEV43450.1}, SNOD_23055
GN {ECO:0000313|EMBL:AJE42595.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AJE42595.1, ECO:0000313|Proteomes:UP000031526};
RN [1] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE42595.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE42595.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [3] {ECO:0000313|EMBL:QEV43450.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV43450.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:MBB4793918.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4793918.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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}.
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DR EMBL; CP009313; AJE42595.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4793918.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV43450.1; -; Genomic_DNA.
DR RefSeq; WP_043449343.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_23055; -.
DR KEGG; snq:CP978_23370; -.
DR HOGENOM; CLU_015112_0_0_11; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; 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:MBB4793918.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:MBB4793918.1}.
FT DOMAIN 13..122
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 617
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 877 AA; 96060 MW; 40A0989D3473994E CRC64;
MKAIRRFTVR PVLPEALHPL GDLARNLRWS WHAETRDLFQ SVDPGRWDGC GGDPVRLLGG
VPPARLAELA EDRRFLRRLA ATADDLADYL GGDRWYQSHP AASDLPSAIA YFSPEFGITA
ALPQYSGGLG ILAGDHLKAA SDLGAPLIGV GLLYRHGYFR QTLSRDGWQQ EHYPVLDPHE
LPLTPLREPD GTPARVTLAL PGGRRLRALV WLAQVGRVPL LLLDSDVEEN DLGERGVTDR
LYGGGGEHRL LQEMLLGIGG VRALRTYCRL TGHAEPEVYH TNEGHAGFLG LERIAELCDT
GLGFDAALEA VRAGTVFTTH TPVPAGIDRF DRELVARHFG PDAELPGIPV ERILRLGSET
YPGGEPGLFN MAVMGLRLGR RANGVSLLHG RVSREMFSGL WPGFDPDEVP ITSVTNGVHA
PTWVAPEVFR LGARQIGAER TENALMVGGS ERWDAIAEIP GQDIWELRRA LRERLVAEVR
ERLYASWRQR GAGSAELGWI DGVLDPDVLT VGFARRVPSY KRLTLMLRDR DRLTELLLHP
ERPLQIVVAG KAHPADDGGK RLIQELVRFT DDPRVRHRIV FLPDYGMAMA QKLYPGCDVW
LNNPLRPLEA CGTSGMKAAL NGCLNLSVLD GWWDEWFQPD FGWAIPTADG AGTDEDRRDE
LEAAALYDLL EHRVAPRFYE RGRGGLPDRW IEMVRRTLMQ LGPKVPAGRM VREYVDRLYT
PAAHAHRAMT PDAARELAGW KARVRAAWAG VTVDHVETTA VTAATATAEL GATLSLRVLA
GLGELAPGDV EVQAVSGRVD TEDRIADATA TALKPVGGPD PEGRWCYEGP LSLDRTGPFG
YTVRILPAHR LLASGAELGL VAVPSQEAGE GAGVLLR
//
