(data stored in SCRATCH zone)

SWISSPROT: Q3KJ22_PSEPF

ID   Q3KJ22_PSEPF            Unreviewed;       426 AA.
AC   Q3KJ22;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|RuleBase:RU365103};
DE            Short=Kdo transferase {ECO:0000256|RuleBase:RU365103};
DE            EC=2.4.99.12 {ECO:0000256|RuleBase:RU365103};
DE   AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|RuleBase:RU365103};
GN   OrderedLocusNames=Pfl01_0490 {ECO:0000313|EMBL:ABA72234.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72234.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72234.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72234.1,
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: Involved in lipopolysaccharide (LPS) biosynthesis.
CC       Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo)
CC       residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-
CC       1,4'-bisphosphate precursor of lipid A.
CC       {ECO:0000256|RuleBase:RU365103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E.
CC         coli) = alpha-Kdo-(2->6)-lipid IVA + CMP + H(+);
CC         Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603,
CC         ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987;
CC         EC=2.4.99.12; Evidence={ECO:0000256|RuleBase:RU365103};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core
CC       biosynthesis. {ECO:0000256|RuleBase:RU365103}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU365103}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|RuleBase:RU365103}.
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DR   EMBL; CP000094; ABA72234.1; -; Genomic_DNA.
DR   RefSeq; WP_011332155.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0490; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   EnsemblBacteria; ABA72234; ABA72234; Pfl01_0490.
DR   KEGG; pfo:Pfl01_0490; -.
DR   eggNOG; ENOG4105D8A; Bacteria.
DR   eggNOG; COG1519; LUCA.
DR   HOGENOM; HOG000257156; -.
DR   KO; K02527; -.
DR   OMA; FIKYEFW; -.
DR   BioCyc; PFLU205922:G1G4S-495-MONOMER; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.11720; -; 1.
DR   InterPro; IPR007507; Glycos_transf_N.
DR   InterPro; IPR038107; Glycos_transf_N_sf.
DR   InterPro; IPR039901; Kdotransferase.
DR   PANTHER; PTHR42755; PTHR42755; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJ22.
DR   SWISS-2DPAGE; Q3KJ22.
KW   Cell inner membrane {ECO:0000256|RuleBase:RU365103};
KW   Cell membrane {ECO:0000256|RuleBase:RU365103};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103};
KW   Membrane {ECO:0000256|RuleBase:RU365103};
KW   Transferase {ECO:0000256|RuleBase:RU365103,
KW   ECO:0000313|EMBL:ABA72234.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU365103};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365103}.
FT   TRANSMEM      6     23       Helical. {ECO:0000256|RuleBase:RU365103}.
FT   DOMAIN       34    212       Glycos_transf_N. {ECO:0000259|Pfam:
FT                                PF04413}.
SQ   SEQUENCE   426 AA;  46929 MW;  E8A142C9BFA64D47 CRC64;
     MNRTLYTALF YLGLPLVAIR LWLRSRKAPA YAERIGERFS CGMPALQPGG IWVHAVSVGE
     SIAAAPMIRA LLQRYPQLPI TVTCMTPTGS ERILAMFANE PRIQHCYLPY DLPCAAARFL
     DRVQPKLAVI METELWPNHI HQCAKRGIPV ALANGRLSER SAKGYGRFSK LTAPMLAEMS
     LFAVQTEAEA QRFRDLGARP ETVEVTGSIK FDLTIDPQLL QRAHELRGQW QALERPVWIA
     ASTHEGEDEV VLSAHRRLLA NHPDALLILV PRHPERFNSV FELCQREGFA TVRRSTGASV
     DAQTSVLLGD TMGELLFLYA LADSAFVGGS LVPNGGHNLL EPAALAKPVI SGPHLFNFLD
     IAAQLRSAGA LAEVDDAEGL ATEVQRLFEL PRDAQRMADA GLSVMRRNQG ALQRLLDGLG
     RLIDRP
//

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