ID I2AAK9_9MYCO Unreviewed; 880 AA.
AC I2AAK9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=glycogen phosphorylase {ECO:0000256|ARBA:ARBA00012591};
DE EC=2.4.1.1 {ECO:0000256|ARBA:ARBA00012591};
GN ORFNames=W7S_06750 {ECO:0000313|EMBL:AFJ34333.1};
OS Mycobacterium sp. MOTT36Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1168287 {ECO:0000313|EMBL:AFJ34333.1, ECO:0000313|Proteomes:UP000002868};
RN [1] {ECO:0000313|EMBL:AFJ34333.1, ECO:0000313|Proteomes:UP000002868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOTT36Y {ECO:0000313|EMBL:AFJ34333.1,
RC ECO:0000313|Proteomes:UP000002868};
RX PubMed=22815454; DOI=10.1128/JB.00752-12;
RA Kim B.J., Choi B.S., Choi I.Y., Lee J.H., Chun J., Hong S.H., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare clinical strain
RT MOTT-36Y, belonging to the INT5 genotype.";
RL J. Bacteriol. 194:4141-4142(2012).
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; CP003491; AFJ34333.1; -; Genomic_DNA.
DR RefSeq; WP_014711093.1; NC_017904.1.
DR AlphaFoldDB; I2AAK9; -.
DR KEGG; mmm:W7S_06750; -.
DR PATRIC; fig|1168287.3.peg.1380; -.
DR HOGENOM; CLU_015112_0_0_11; -.
DR Proteomes; UP000002868; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000460-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..123
FT /note="DUF3417"
FT /evidence="ECO:0000259|Pfam:PF11897"
FT MOD_RES 629
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 880 AA; 97025 MW; 9F0F19A40AD4837B CRC64;
MKALRRFTVR AHLPERLTAL DQLSTNLRWS WDTPTQDLFA SIDPDLWQRC GCDPVALLGA
VKPARLDELA IDETFLRRLD ELTAELNDYL NRPLWYQQQQ DHGAEMPAAI AYFSMEFGIA
EVLPNYSGGL GILAGDHLKS ASDLGVPLVA VGLYYRSGYF RQSLTADGWQ HENYPSLDPQ
GLPLRLLTDA TGDPALVELM LPDSAQLHAR IWVAQVGRVP LLLLDSDVPE NEHDLRGVTD
RLYGGDQEHR MRQEILAGIG GVRAIRAYTA IHGLPAPEVF HMNEGHAGFL GAERIRELMT
GAALDFDTAL AVVRSSTVFT THTPVPAGID RFPIDMVRLY FDDHLADESA SGGDGTAADA
TSAPVLLPGV PTARILALGA EDDPTKFNMA HMGLRLAQRA NGVSSLHGRV SRAMFNELWP
GFDPGEVPIG SITNGVHART WAAPQWLQLG YELAGSDSFS DPGVWLRLQQ VDAGHLWWIR
SQLRSLLVDD VRRRLRRSWL ERGASDAELG WIATAFDPEV LTIGFARRVP TYKRLTLMLH
DPDRLEQLLL DSERPIQLIV AGKSHPADDG GKALIQQVVR FADRPQVRHR IAFLPDYDMS
MARLLYWGCD VWLNNPLRPL EACGTSGMKS ALNGGLNLSI RDGWWDEWYD GENGWEIPSA
DGVADAERRD DLESSALYRL LEEAVAPKFY ERDQHGVPPR WIEMVRHTLQ TLGPKVLASR
MVRDYVEQYY TPAAQSLRKT LAPADGGGEF GAARELAAYR RRAYEAWPKI VITDVDSTGL
PDSPVLGSKL TLTATVQLAG LAPEEVTVQA VVGRVDAGDA LLEPITVEMS YTGTAEGGNQ
VFSTTTPLPL AGSVGYTVRV LPRHPMLAAS NELGLVTLAR
//
