ID   E6WQ39_PSEUU            Unreviewed;       441 AA.
AC   E6WQ39;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   OrderedLocusNames=Psesu_0429 {ECO:0000313|EMBL:ADV26288.1};
OS   Pseudoxanthomonas suwonensis (strain 11-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV26288.1, ECO:0000313|Proteomes:UP000008632};
RN   [1] {ECO:0000313|EMBL:ADV26288.1, ECO:0000313|Proteomes:UP000008632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002446; ADV26288.1; -; Genomic_DNA.
DR   RefSeq; WP_013534118.1; NC_014924.1.
DR   AlphaFoldDB; E6WQ39; -.
DR   STRING; 743721.Psesu_0429; -.
DR   KEGG; psu:Psesu_0429; -.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_036146_2_0_6; -.
DR   OrthoDB; 9789797at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000008632; Chromosome.
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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000008632};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103};
KW   Transmembrane {ECO:0000256|RuleBase:RU365103};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU365103}.
FT   TRANSMEM        17..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365103"
FT   DOMAIN          47..224
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   ACT_SITE        73
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            143
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT   SITE            221
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ   SEQUENCE   441 AA;  49110 MW;  3F21F0FBAE90F693 CRC64;
     MSTPFPPKEP GERLVRWLYS LALYLLSPFT LYHLVSRGFR VREYFRRWDE RYGAYSTEQG
     RPCVWLHAVS VGEVNAAAPL VNALLRQNKG TRWVITTITP TGSQRVRSLW GGRVDHVYLP
     YDLPGSVDRF LQHFRPTVAL IMETELWPNM LFGCRDHRIP VYIINARLSA RSLRGYRLLR
     PLLGRALRTV RCVAAQSVTD GRRFQVLGAE PAQIQVLGNL KYDIEVPDGL EVLRSAFEDA
     LGRKRPVWIA ASTHEGEEEA VLALHRRLQA RWPDLLLVWA PRHPERFPRA QAAAVAAGWK
     VGTRSRDGWP GADDQVFLVD TLGELMAFYA CADVAFVGGS LQPIGGHNLL EPAAVGTAVV
     TGPHLHNFVD ISRRLDEAGA LRVGQDLDGV GDALETLLAD PQAREEMVAA GLALVDQGRG
     ALRRTLELIA PDLPEPDPVE E
//