(data stored in SCRATCH zone)

SWISSPROT: Q4ZZH8_PSEU2

ID   Q4ZZH8_PSEU2            Unreviewed;       816 AA.
AC   Q4ZZH8;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE            EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN   OrderedLocusNames=Psyr_0374 {ECO:0000313|EMBL:AAY35444.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35444.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35444.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35444.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35444.1; -; Genomic_DNA.
DR   RefSeq; WP_003403097.1; NC_007005.1.
DR   RefSeq; YP_233482.1; NC_007005.1.
DR   STRING; 205918.Psyr_0374; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   EnsemblBacteria; AAY35444; AAY35444; Psyr_0374.
DR   GeneID; 3365850; -.
DR   KEGG; psb:Psyr_0374; -.
DR   PATRIC; fig|205918.7.peg.381; -.
DR   eggNOG; ENOG4108IUN; Bacteria.
DR   eggNOG; COG0058; LUCA.
DR   HOGENOM; HOG000278444; -.
DR   KO; K00688; -.
DR   OMA; WLEMSIN; -.
DR   BioCyc; PSYR205918:G1G4J-375-MONOMER; -.
DR   Proteomes; UP000000426; 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; Q4ZZH8.
DR   SWISS-2DPAGE; Q4ZZH8.
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU000587,
KW   ECO:0000313|EMBL:AAY35444.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW   ECO:0000256|RuleBase:RU000587};
KW   Transferase {ECO:0000256|RuleBase:RU000587,
KW   ECO:0000313|EMBL:AAY35444.1}.
FT   MOD_RES     666    666       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR000460-1}.
SQ   SEQUENCE   816 AA;  91995 MW;  F18D1EE286187DA8 CRC64;
     MSQEPLVRDA DVAAFRAAVL AKLTYSVGKD PDHAFEHDWF EAVALAARDH MVEHWMDHTR
     QIYRKVQKRV YYLSLEFLIG RLLYDSLSNL GLLEVAREAL TELGVDIERI RLLEPDAALG
     NGGLGRLAAC FMESMSTLGI AGHGYGIRYE HGLFRQGIVD GWQQEQTENW LDFGNPWEFE
     RPEVVYSIGF GGSVDTVPTE AGDSRQVWRP GETVRAIAYD TPVVGWRGKS VNTLRLWRAR
     AVEDLHLERF NAGDHFGAVA EVVRAESISR VLYPNDATEA GQELRLRQEY FFVSASLQDL
     LRRHLNQHAT LTDLSEHAAI QMNDTHPSIA VAELMRQLID NHNIPWDTAW KITVGTLGYT
     NHTLLPEALE TWSVGLMERM LPRHMQIIYL INAQHIDTLR AKGVDDVNVL RAVSLIEEDN
     GRRVRMGNLA FLGSHSVNGV SALHTQLMRK TVFAELHKIY PERINNKTNG ITFRRWLFQA
     NPKLTEMLVE SLGEDVLDNA ETRLKELEPF AEKSSFRKQM ADQRLHSKRA LAAIIHERLG
     IAVNPAAMFD VQVKRIHEYK RQLLNLFHTV ALYQAIRAEP GTDWVPRVKI FAGKAAASYH
     SAKLIIKLTN DIARTVNNDP TVRGLLKVVF MPNYNVSLAE SIIPAADLSE QISTAGLEAS
     GTSNMKFGLN GALTIGTLDG ANVEMSEQVG LEHMFIFGMS SQQVEARKQA GEFSAHDDVA
     ASGRLNDVLQ AIRGGVFSPD DPNRYVGLID QLLAYDRFLV CADFDSYWAA QAKVEERWHD
     SKEWWRSAVL NTARMGWFSS DRTIREYAGD IWKALE
//

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