PHSG_PASMU
ID PHSG_PASMU Reviewed; 818 AA.
AC Q9CN90;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Glycogen phosphorylase;
DE EC=2.4.1.1;
GN Name=glgP; OrderedLocusNames=PM0545;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; AE004439; AAK02629.1; -; Genomic_DNA.
DR RefSeq; WP_010906718.1; NC_002663.1.
DR AlphaFoldDB; Q9CN90; -.
DR SMR; Q9CN90; -.
DR STRING; 747.DR93_1322; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR EnsemblBacteria; AAK02629; AAK02629; PM0545.
DR KEGG; pmu:PM0545; -.
DR PATRIC; fig|272843.6.peg.552; -.
DR HOGENOM; CLU_010198_1_1_6; -.
DR OMA; KHKRTFT; -.
DR Proteomes; UP000000809; 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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR InterPro; IPR035090; Pyridoxal_P_attach_site.
DR PANTHER; PTHR11468; PTHR11468; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR TIGRFAMs; TIGR02093; P_ylase; 1.
DR PROSITE; PS00102; PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Carbohydrate metabolism; Glycogen metabolism;
KW Glycosyltransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..818
FT /note="Glycogen phosphorylase"
FT /id="PRO_0000188557"
FT MOD_RES 667
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 818 AA; 94037 MW; 89E7643EDD48D5B1 CRC64;
MIMDNFDSPF LYNRPEITVD SLKKSIVYKL IFSIGRSPKE ASQRDWLNAT LYAVRDFVTE
GWITTARQSR SEETRRVYYL SMEFLIGRTL SNAMLAEGVY DVAKQALSEL NVNLEDVLEK
EVDPGLGNGG LGRLAACFMD SIATLALPGV GYGIRYEYGM FKQEIEDGHQ VEKPDAWLDK
GAAWEFIRPS KRHTVRFGGG IHFEGKKCIW TSKEEVEALA YDQMIPGYAN DSAATLRLWS
AYAGDRFDLA DFNKGDYFAA VQDRTLSKNI SRVLYPDDST WSGRELRLRQ EYFLVSASLQ
DIIYRHKRIH NTMENFADKV AIHLNDTHPA LAIPELMVIL IDQEGYEWKK AWDITRRVFS
YTCHTLMSEA LETWPVEMMA HILPRHLQMI FEINDYFLEY VRTYVSTDAE FIRRVSLIEE
GDHRKVRMGW LSVVGSNKVN GVAAIHSELM VTSTFADFAR IYPERFTNVT NGITPRRWIG
VANPELSALF DRYIGKEWRR DLSQLTLLKD KVQDPELKKS IAQIKYNNKV KLANYIKNEL
GVEVDPNALF DVQVKRIHEY KRQILNVLHI IARYNAMLEN PEKDWVPRVF ILAGKAASAY
YAAKQTINLI NDVANIINHD ERLQGRLKVV FIPNYSVSLA ELIIPAADIS EQISLAGTEA
SGTSNMKFAL NGALTIGTLD GANVEILDNV GQDHIFIFGN TVEQVESLRR HGYRPFDYYQ
NDEELRKVVD QIISGRFSPT DANRYHQLLQ SLQYHDYYQA FADFRSYVDM QQNVDAKYQD
QNAWIDSTLQ NIVNMSYFSS DRTILEYAEK IWKIKPVK