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Database: UniProt
Entry: B6EPB9_ALISL
LinkDB: B6EPB9_ALISL
Original site: B6EPB9_ALISL 
ID   B6EPB9_ALISL            Unreviewed;       420 AA.
AC   B6EPB9;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|ARBA:ARBA00019077, ECO:0000256|RuleBase:RU365103};
DE            Short=Kdo transferase {ECO:0000256|RuleBase:RU365103};
DE            EC=2.4.99.12 {ECO:0000256|ARBA:ARBA00012621, ECO:0000256|RuleBase:RU365103};
DE   AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|ARBA:ARBA00031445, ECO:0000256|RuleBase:RU365103};
GN   Name=kdtA {ECO:0000313|EMBL:CAQ77847.1};
GN   OrderedLocusNames=VSAL_I0162 {ECO:0000313|EMBL:CAQ77847.1}, VSAL_I0261
GN   {ECO:0000313|EMBL:CAQ77946.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ77847.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ77847.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ77847.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC       the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-
CC       Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate
CC       precursor of lipid A. {ECO:0000256|RuleBase:RU365103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) =
CC         alpha-Kdo-(2->6)-lipid IVA (E. coli) + 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|ARBA:ARBA00034406,
CC         ECO:0000256|RuleBase:RU365103};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004713, ECO:0000256|RuleBase:RU365103}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU365103}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000256|RuleBase:RU365103}.
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DR   EMBL; FM178379; CAQ77847.1; -; Genomic_DNA.
DR   EMBL; FM178379; CAQ77946.1; -; Genomic_DNA.
DR   RefSeq; WP_012549045.1; NC_011312.1.
DR   AlphaFoldDB; B6EPB9; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   KEGG; vsa:VSAL_I0162; -.
DR   KEGG; vsa:VSAL_I0261; -.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_036146_2_0_6; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000001730; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.11720; 3-Deoxy-D-manno-octulosonic-acid transferase, N-terminal domain; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 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:SF1; 3-DEOXY-D-MANNO-OCTULOSONIC ACID TRANSFERASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR42755; 3-DEOXY-MANNO-OCTULOSONATE CYTIDYLYLTRANSFERASE; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   Pfam; PF04413; Glycos_transf_N; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU365103};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103};
KW   Membrane {ECO:0000256|RuleBase:RU365103};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT   DOMAIN          35..212
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   DOMAIN          247..398
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   ACT_SITE        62
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            131
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT   SITE            209
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ   SEQUENCE   420 AA;  46585 MW;  79592E6C70714D6E CRC64;
     MLIRLVYTLL LTLLSPVLLF GLYKKKPNKP QFGDRWKEHF GFTPTLKKSE QPLWIHAVSV
     GEAIAATPLI KALKQQSPEQ PILVTTTTST GAEQIAKLGD LVEHRYMPID FPFAVNGFLK
     TVNPSKLLII ETELWPNTLH SVGKSNIPIY VVNARLSEKS CQGYTKIQPV FTELSKHLTK
     VLCQTQADAD RFARLGINKE RLCATGSIKF DIQISDEIKQ QGQELRQLLD NDRPIWIAAS
     THKGEDEQVL DAHKEVLKEH PNALLILVPR HPERFDTVFE LSKNSGFSSI RRTSNKTVTA
     ETQVYLGDTM GEMLVLIGAA DVCFMGGSLL GDKVGGHNVL EPAALGVPVI IGPSYYNFKE
     IVDTLRGEQG IVICEPTQLS NHIVKLIDDS TEYQLLQNSA SNVVQSNQGA LNRTIAISNI
//
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