ID M3BIH6_STRMB Unreviewed; 875 AA.
AC M3BIH6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=H340_16611 {ECO:0000313|EMBL:EME99364.1};
OS Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EME99364.1, ECO:0000313|Proteomes:UP000011740};
RN [1] {ECO:0000313|EMBL:EME99364.1, ECO:0000313|Proteomes:UP000011740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EME99364.1,
RC ECO:0000313|Proteomes:UP000011740};
RX PubMed=23558536;
RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT Transglutaminase.";
RL Genome Announc. 1:E0014313-E0014313(2013).
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:EME99364.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AORZ01000050; EME99364.1; -; Genomic_DNA.
DR RefSeq; WP_004946437.1; NZ_CP072827.1.
DR AlphaFoldDB; M3BIH6; -.
DR STRING; 1223523.H340_16611; -.
DR PATRIC; fig|1223523.3.peg.3401; -.
DR eggNOG; COG0058; Bacteria.
DR Proteomes; UP000011740; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT MOD_RES 615
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 875 AA; 95566 MW; A6EFC6C727A0BCB8 CRC64;
MKAIRRFSVR PVLPEPLRPL SELARNLRWS WHPETRELFQ TLDPEGWRAA GGDPLRLLGA
VPAARLTALA DDRRFRRRLA AAADDLHDYL TGARWYQEQP PGLPAAVAYF SPEFGITAAL
PQYSGGLGIL AGDHLKSASD LGVPLIGVGL LYRHGYFRQS LSREGWQQEH YPLLDPNELP
LSLLREADGT PATVALALPG GRSLRAHVWK AEVGRVPLLL LDSDVEENAP GERDVTDRLY
GGGSEHRLLQ EMLLGIGGVR AVRAYCRLTG HPAPEVFHTN EGHAGFLGLE RIRELSAGGL
DFDAALESVR AGAVFTTHTP VPAGIDRFDR ELVARHFADG AELPGIDVDR VLRLGAEDYP
GGDPALFNMA VMGLRLAQRA NGVSVLHGEV SRRMFAGLWP GFDDTEVPIT SITNGVHAPT
WVAPEVFRLG ARRIGVARAE DALTLGGSER WDSVADISDA DVWELRRTLR EQLVEEVRER
LRASWRERGA GTAELGWIDG VLDPDVLTIG FARRVPSYKR LTLMLRDRER LTRLLLDPER
PIQIVVAGKA HPADDSGKRL VQELVRFADD PRVRHRVVFL PDYGMAMAQK LYPGCDVWLN
NPLRPLEACG TSGMKAALNG CLNLSVLDGW WDEWYEPDFG WAIPTADGSA TDEERRDDLE
AAALYGLLEE RVAPRFYDRG PDGLPGRWIE MVRSTLGSLG PKVLAGRMVR EYVERLYGPA
AEAQRALTPD AARELAAWKA RVRAAWPAVA VDHVEAAADG PLDGTAELGS TVTLRVTVTL
GDLDPADVEV QALAGRVDAA DRLTGAAAVP LKPAGTSALD GRRLYEGPLT FDRTGPFGYT
VRILPSHRLL ADGAEMGLVA VPPEASGEAA GVLMR
//
