(data stored in SCRATCH zone)

SWISSPROT: Q3KJG3_PSEPF

ID   Q3KJG3_PSEPF            Unreviewed;       816 AA.
AC   Q3KJG3;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   OrderedLocusNames=Pfl01_0349 {ECO:0000313|EMBL:ABA72093.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72093.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72093.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72093.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC       carbohydrate metabolism. Enzymes from different sources differ in
CC       their regulatory mechanisms and in their natural substrates.
CC       However, all known phosphorylases share catalytic and structural
CC       properties. {ECO:0000256|RuleBase:RU000587}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-
CC         D-glucosyl](n-1) + alpha-D-glucose 1-phosphate;
CC         Xref=Rhea:RHEA:41732, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586,
CC         ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601;
CC         EC=2.4.1.1; Evidence={ECO:0000256|RuleBase:RU000587};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU000587};
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC       {ECO:0000256|RuleBase:RU000587}.
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DR   EMBL; CP000094; ABA72093.1; -; Genomic_DNA.
DR   RefSeq; WP_011332035.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0349; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   EnsemblBacteria; ABA72093; ABA72093; Pfl01_0349.
DR   KEGG; pfo:Pfl01_0349; -.
DR   eggNOG; ENOG4108IUN; Bacteria.
DR   eggNOG; COG0058; LUCA.
DR   HOGENOM; HOG000278444; -.
DR   KO; K00688; -.
DR   OMA; WLEMSIN; -.
DR   BioCyc; PFLU205922:G1G4S-353-MONOMER; -.
DR   Proteomes; UP000002704; 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   CDD; cd04300; GT1_Glycogen_Phosphorylase; 1.
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; Q3KJG3.
DR   SWISS-2DPAGE; Q3KJG3.
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU000587,
KW   ECO:0000313|EMBL:ABA72093.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW   ECO:0000256|RuleBase:RU000587};
KW   Transferase {ECO:0000256|RuleBase:RU000587,
KW   ECO:0000313|EMBL:ABA72093.1}.
FT   MOD_RES     666    666       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR000460-1}.
SQ   SEQUENCE   816 AA;  92316 MW;  D8327BAE3C10896A CRC64;
     MTQEPLVREA EVAAFRDAVL TKLTYAVGKD PDHAFDHDWF EAIALAARDH MVEHWMDHTR
     QIYRKGQKRV YYLSLEFLIG RLLYDSLSNL GLLDVAREAL TELGVDLERI RILEPDAALG
     NGGLGRLAAC FMESMSTLGI AGHGYGIRYE HGLFRQAIVD GWQQEQTEHW LDFGNPWEFE
     RPEVVYPIGF GGSVETVTDA NGNSRQVWHP AETVRAIAYD TPVVGWRGAS VNTLRLWRAR
     AMEDLHLERF NAGDHLGAVA EVARAESISR VLYPADSTEA GQELRLRQEY FFVAASLQDL
     LRRHRNMHTS VLTLGDHAAI QLNDTHPSIA VAELMRQLVD VYDVAWDAAW QVTVDTLSYT
     NHTLLPEALE TWPVGLMERM LPRHMQIIYL INAQHIDSLR AKGIHDFDVL RAVSLIEEDN
     GRRVRMGNLA FLGSHSVNGV SGLHTQLMRK TVFAELHKLY PERINNKTNG ITFRRWLYQA
     NPELTSMLVD ALGPDVLDNP EERLLDLEPF AEKPAFRKAF AEQRLHSKKA LAYLIHERLG
     IAVNPAAMFD VQVKRIHEYK RQLLNLMHTV ALYQAIRAEP EIDWVPRVKI FAGKAAASYH
     QAKLIIKLTN DIARVVNNDP TVRGLLKVVF LPNYNVSLAE SIIPAADLSE QISTAGFEAS
     GTSNMKFGLN GALTIGTLDG ANVEMCENIG AEHMFIFGLS AQQVEARKQN HEFSAVPDIA
     ASHRLNDVLQ AIRSGVFSPD DTSRYTGLID SLVDYDRFFV CADFDSYWEA QMRVDAHWHD
     ANNWWRSAVL NTSRMGWFSS DRTIREYATD IWKALE
//

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