ID F2R418_STRVP Unreviewed; 860 AA.
AC F2R418;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=SVEN_5104 {ECO:0000313|EMBL:CCA58390.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA58390.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA58390.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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; FR845719; CCA58390.1; -; Genomic_DNA.
DR AlphaFoldDB; F2R418; -.
DR STRING; 953739.SVEN_5104; -.
DR KEGG; sve:SVEN_5104; -.
DR PATRIC; fig|953739.5.peg.241; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000006854; Chromosome.
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:CCA58390.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCA58390.1}.
FT DOMAIN 16..127
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 598
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 860 AA; 93664 MW; 1A97FF95300243C7 CRC64;
MEHVKAIRRF TVRPVLPDTL RPLADLAHNL RWSWHEPTRA LFDSLEPPGP AAPSGTDPVR
ILGALEAPRL AALAADQDFL ARLRAAAEDL DTYLHAPRWY QRTEGSAAGR PAALAYFSPE
FGVTAALPQY SGGLGILAGD HLKAASDLGV PLIGVGLLYR HGYFRQSLGR DGWQQEQYPV
LDPGELPVTL LREADGAPAR ITLALPGGRS LHAHLWIARV GRVPLLMLDS DVEENAPGER
SVTDRLYGGG SEHRLLQEML LGIGGVRAVR TYTRLTGTPE PEVFHTNEGH AGFLGLERIR
ELQGEGLDFD SALETVRAGT VFTTHTPVPA GIDRFDRSLV ARHLGEDGAL PGVDTGRVLA
LGDETPLGGE PGVFNMAAMG LRLAQRANGV STLHGAVSRA MFAGLWPGFD ADEVPITSIT
NGVHAPTWVA PEVGELGPEP TDRELWELRR TLRERLVTDV RQRLRASWRQ RGAAAAELGW
TDSVLDPDVL TIGFARRVPS YKRLTLMLRD KDRLRALLLH PERPVQLVVA GKAHPADDGG
KRLVQELVRF ADDPRVRHRI VFLPDYGMAM ARGLYPGCDV WLNNPLRPLE ACGTSGMKAA
LNGCLNLSVL DGWWDEWFEP DFGWAIPTAD GAAADDEDRR DDLEAAALYE LIERQVAPRF
YERGPDGVPA GWTAMVRRTL GDLGPKVLAD RMVREYVERL YVPAATARRA LTPDRARELA
TWKARVREAW PKVTVDHVEV GDDLADELAD AELGATPVVR VRVALGALAP DDVEVQAVTG
RVDADDTLAD TRAVPLKPAG GPDLEGRQPY AGTFELDRTG TFGCTVRVRP SHPLLAHPAE
LGLVALPEET TGEGAGVLLR
//
