(data stored in ACNUC1104 zone)

SWISSPROT: D3VGW5_XENNA

ID   D3VGW5_XENNA            Unreviewed;       425 AA.
AC   D3VGW5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 42.
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   Name=waaA {ECO:0000313|EMBL:CBJ88250.1};
GN   OrderedLocusNames=XNC1_0162 {ECO:0000313|EMBL:CBJ88250.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88250.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88250.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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; FN667742; CBJ88250.1; -; Genomic_DNA.
DR   RefSeq; WP_010847620.1; NC_014228.1.
DR   STRING; 406817.XNC1_0162; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   EnsemblBacteria; CBJ88250; CBJ88250; XNC1_0162.
DR   KEGG; xne:XNC1_0162; -.
DR   eggNOG; ENOG4105D8A; Bacteria.
DR   eggNOG; COG1519; LUCA.
DR   HOGENOM; HOG000257156; -.
DR   KO; K02527; -.
DR   OMA; FIKYEFW; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000008075; 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; IPR001296; Glyco_trans_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; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VGW5.
DR   SWISS-2DPAGE; D3VGW5.
KW   Cell inner membrane {ECO:0000256|RuleBase:RU365103};
KW   Cell membrane {ECO:0000256|RuleBase:RU365103};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103};
KW   Membrane {ECO:0000256|RuleBase:RU365103};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Transferase {ECO:0000256|RuleBase:RU365103,
KW   ECO:0000313|EMBL:CBJ88250.1}.
FT   DOMAIN       33    211       Glycos_transf_N. {ECO:0000259|Pfam:
FT                                PF04413}.
FT   DOMAIN      249    398       Glycos_transf_1. {ECO:0000259|Pfam:
FT                                PF00534}.
SQ   SEQUENCE   425 AA;  47446 MW;  4C741C63DDB15045 CRC64;
     MLLRLYQVLL YLIQPIIWLR LLLRSRKSPA YRKRWGERYG FCAKKVTPGG ILLHSVSVGE
     TLAAIPLVRI LRHHYPLLPI TITTMTPTGS ERVLSALGSD VNHVYLPYDL PGSMSRFFDH
     VNPKLVIIME TELWPNLITQ LHQREIPLVI ANARLSARSA AGYQKISSFI KTILNKITLI
     AAQNQEDGER FIELGLRRSQ LSVTGSLKFD ISVTPELAAK AITLRRQWAP HRPVWIATST
     HDGEESILLE AHCKLLKQFP DLLLILVPRH PERFNKAAEL TQKAGLSAIL RSAGTIPEAD
     VQVVIGDTMG ELMLLYGIAD MAFVGGSLIE RGGHNPLEAA AHAIPVIMGP HTFNFKDICA
     KLEKADGLIT VTDSQSLSSA IHSLLADEDY RRYYGHHAAE VLHENQGALQ RLLKLLEPYL
     PPRSH
//

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