(data stored in SCRATCH9089 zone)

SWISSPROT: 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   11-DEC-2019, entry version 102.
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}.
DR   EMBL; AE004439; AAK02629.1; -; Genomic_DNA.
DR   RefSeq; WP_010906718.1; NC_002663.1.
DR   SMR; Q9CN90; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   EnsemblBacteria; AAK02629; AAK02629; PM0545.
DR   KEGG; pmu:PM0545; -.
DR   PATRIC; fig|272843.6.peg.552; -.
DR   eggNOG; ENOG4108IUN; Bacteria.
DR   eggNOG; COG0058; LUCA.
DR   HOGENOM; HOG000278444; -.
DR   KO; K00688; -.
DR   OMA; KSPIDFN; -.
DR   BioCyc; PMUL272843:G1FZ8-576-MONOMER; -.
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;
DR   PRODOM; Q9CN90.
DR   SWISS-2DPAGE; Q9CN90.
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
//

If you have problems or comments...

PBIL Back to PBIL home page