ID I7LL09_METBM Unreviewed; 740 AA.
AC I7LL09;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN OrderedLocusNames=BN140_2594 {ECO:0000313|EMBL:CCJ37517.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ37517.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(2012).
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; HE964772; CCJ37517.1; -; Genomic_DNA.
DR RefSeq; WP_014868488.1; NC_018227.2.
DR AlphaFoldDB; I7LL09; -.
DR STRING; 1201294.BN140_2594; -.
DR GeneID; 13354704; -.
DR KEGG; mbg:BN140_2594; -.
DR PATRIC; fig|1201294.9.peg.2916; -.
DR HOGENOM; CLU_015112_0_0_2; -.
DR BioCyc; MBOU1201294:BN140_RS12885-MONOMER; -.
DR Proteomes; UP000009007; 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:CCJ37517.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCJ37517.1}.
FT DOMAIN 13..122
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 609
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 740 AA; 85303 MW; D2ED8995ABAC4E24 CRC64;
MKTEIPYDRF AHVPERIFGL VDLAYNLWWS WHSSATVLFK QLNRAEWKLS RHNPVRMLLE
TPPRFFERAA NNPEYLRRYD IIMFRFRQYM EPTTSWFAQR YPGRVPLTIA YFSSEFGLHH
SLPFYAGGLG ILAGDHIKAA GDLGLPMVAV GFMYAEGYLH QHMEGNGWQK NVAEILDRDA
APVLRVTGDN GRQLVVQVPL IDPPIYVAVW KVQVGRVPLY LLDTHIDENL PENRSISHRL
YLKELECRLR QELVLGIGGR KVLHTLGVDY SAMHLNEGHS AFALLERLRE RLVAGMPPDE
ARERIRGTSV FTTHTPVPAA HDVFPEDLMA KYFRSYCPSL GLDWDEFMAL GEDPHNPGAS
FNMTAFALRM SLFHNAVSQR HGEVTREMWQ PLWPDLAVED VPIDAITNGV HVPTWLNHRI
ETLLDRYMDP IYPNWREEYD NPIVWEVVDE IPDDELWGEH QWLKMKLFAR LRERKRRKWA
GHREEPANLA AEGLMLDTTA LTIGFARRFA EYKRADLIFE DLDRLDRIVN NRWRPVQFIF
AGKAHPADEK GKRILQKIYQ YSQDPRFGGR ISFIEDYDEQ LARYMVHGVD VWMNTPVPLM
EASGTSGMKA GMNGVLNLSV LDGWWVEGYN GRNGWAFEGH APYGGNNRAD ANTLYDLIEN
EIAPLYYSRT IDNVPHKWAR MMKESIKSIA PQYCSLRMLK QYITNYYPSV CMYAAEPGKP
MAGIQEVCPT EPGSGGFTEK
//
