ID A0A098Y111_9ACTN Unreviewed; 849 AA.
AC A0A098Y111;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=IN07_21850 {ECO:0000313|EMBL:KGH44633.1};
OS Modestobacter caceresii.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH44633.1, ECO:0000313|Proteomes:UP000029713};
RN [1] {ECO:0000313|EMBL:KGH44633.1, ECO:0000313|Proteomes:UP000029713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH44633.1,
RC ECO:0000313|Proteomes:UP000029713};
RA Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT "Biosystematic studies on Modestobacter strains isolated from extreme
RT hyper-arid desert soil and from historic building.";
RL Submitted (JUL-2014) 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}.
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:KGH44633.1}.
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DR EMBL; JPMX01000118; KGH44633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A098Y111; -.
DR STRING; 1522368.IN07_21850; -.
DR OrthoDB; 9760804at2; -.
DR Proteomes; UP000029713; 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 Reference proteome {ECO:0000313|Proteomes:UP000029713};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..120
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 605
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 849 AA; 93254 MW; C4A39B7CAA474BF8 CRC64;
MRALRRLTVR ASLPEALMPL SQLVTNLRWS WHPETRDLFE ALDPELWASC GGDPVRVLGE
VSAERLAALA DDPVFLQRLT AVADDLREYL DAPHWYQSLG AEAPATIAYF SAEFGITEVL
PQYSGGLGIL AGDHLKAASD LGVPLIGVGL LYRSGYFSQG LSADGWQLEH YPALDPHGLP
LKLVRDADRN AVVIAVPLPE GRTLYAHVYR AQVGRVSLLL LDSDIEENSP AERGVTDRLY
GGGEDHRLRQ EMLLGIGGVR AVRAFCSLTG TPPPEVFHAN EGHAGFQGVE RIRELTESHG
LSFPEALQAV RGGTVFTTHT PVPAGIDRFP KALIERYFAG FGVPLDQLLP LGAEDDPSKF
NMAHMGLRLG QRANGVSELH GHVSRDMFGP LWPGFDPDDV PIGSITNGVH APTWTARELV
ELGTQTTSQG DPLEVDEDVH FDGVDRIPAA ELWRTRRLLR GRLVEEVRRR VRATALSRGA
AEAELGWTET AFDPDVLTIG FARRVPSYKR LTLMLRDPGR LKALLLDEER PVQLVIAGKS
HPADDGGKQL IQQMVKFADD PEIRHRIAFL PNYDIGMARY LYWGCDVWLN NPLRPLEACG
TSGMKSALNG GLNLSIRDGW WDEWFDGQNG WAIPTADGVE DPERRDDVEA QAIYELLDRQ
VVPRFYEVDS DGLPTRWVEM VRDTLRETGP KVLATRMVRD YVQRLYVPAA GAARSMAAGG
YEPARAEAAW RAKLLEHWPG VRVAHVEAAG VGETPEIGGG IDLRAEVELP GLAPSDVLVE
AAYGRVDDAD GLHQVTTLEL RHDGVEGSRH WFTGTVPLTR TGAFGYTVRV LPHSAHLVVP
AELGVVVNA
//
