ID E4NH68_KITSK Unreviewed; 894 AA.
AC E4NH68;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN Name=glgP {ECO:0000313|EMBL:BAJ30848.1};
GN OrderedLocusNames=KSE_50700 {ECO:0000313|EMBL:BAJ30848.1};
OS Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS / NBRC 14216 / KM-6054) (Streptomyces setae).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ30848.1, ECO:0000313|Proteomes:UP000007076};
RN [1] {ECO:0000313|EMBL:BAJ30848.1, ECO:0000313|Proteomes:UP000007076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA Takahashi Y., Fujita N.;
RT "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT snapshot of the family Streptomycetaceae.";
RL DNA Res. 17:393-406(2010).
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; AP010968; BAJ30848.1; -; Genomic_DNA.
DR RefSeq; WP_014138147.1; NC_016109.1.
DR AlphaFoldDB; E4NH68; -.
DR STRING; 452652.KSE_50700; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR KEGG; ksk:KSE_50700; -.
DR PATRIC; fig|452652.3.peg.5069; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000007076; 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:BAJ30848.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007076};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAJ30848.1}.
FT DOMAIN 13..126
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 623
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 894 AA; 97076 MW; EC70E0E8E9B118FF CRC64;
MKAIRRFTVR TVLPEQLQPL HELALNLRWS WHPETRELFR SVDPDVWAAV GEDPVRLLGE
VPAARLAALA GDRRFLRRLG DLSDELRDYL TGPRWYQGAT DPADPEGPLP AGIAYFSPEY
GIAAALPQYS GGLGILAGDH LKAASDLGVP IIGVGLFYRH GYFRQSLDRD GWQQERYPLL
DPDALAVTLL REPDGTPCRI DLALPGGRTL AAQVWRAQVG RVPLLLLDSD VEANSPAERD
VTDRLYGGGS EHRLLQEILL GIGGVRAVRT YCRLTGHPEP EVFHTNEGHA GFLGLERIGE
LTTAHPGLGF ADALEAVRAG TVFTTHTPVP AGIDRFDREL VARHFGGDAA LPGVPVDQVL
ALGAESWSGG DPKLFNMAAM GLRLAQRANG VSTLHGAVSR EMFRGLWPGF DAPEVPITSI
TNGVHAPTWI DPAVVRLGAT EIGQQRAEDA MAVGTAPQWT GLERIGNAEV WELRRALRAQ
LVDEARRRLR ASWKQRGAGE AELGWTGGVL DADVLTIGFA RRVPSYKRLT LMLRDPARLR
RLLLDPERPV QIVIAGKAHP ADDGGKRLIQ QLVAFADDPA VRHRIVFLPD YDMAMAKTLY
PGCDVWLNNP LRPLEACGTS GMKAALNGCL NLSILDGWWD EWYDGQNGWA IPTADGGTGE
GVVDPESKEA ERRDDIEAAA LYDLIEHQVA ARFYDRGADG LPHRWISMVR HTLVTLGPKV
LAGRMVREYV ERLYAPAASA KRRLEGPAGD YAAAKALAGW KAGVREAWPA VRVEHVEADG
AGEAQELGAT LALRVQVNLG RLGPDDVEVQ VVAGRVDESD RISEATTLAL KPAGGGTDLD
GRIRYEGHLE LSRTGPFGYT VRILPTHPRL ASVAELGLLA APAETGGMDA GVLR
//
