ID Q1LJT9_CUPMC Unreviewed; 424 AA.
AC Q1LJT9;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
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:ABF09587.1};
GN OrderedLocusNames=Rmet_2714 {ECO:0000313|EMBL:ABF09587.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF09587.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF09587.1; -; Genomic_DNA.
DR RefSeq; WP_011517286.1; NC_007973.1.
DR AlphaFoldDB; Q1LJT9; -.
DR STRING; 266264.Rmet_2714; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR KEGG; rme:Rmet_2714; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_0_4; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000002429; 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:UP000002429};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT DOMAIN 34..212
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT SITE 133
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 424 AA; 46321 MW; 04640AA9FB5A4A2D CRC64;
MLRFVYSLLW LLILPLALLR LVWRSRKESG YIQHVGERLG RYGDLSAAGP WLWVHAVSVG
ETRAAQPLID ALLAAYPRHR LLLTHMTPTG RQTGAQLYGA NPRVQQCYLP YDLPWLVRRF
LAYFQPDAGL IMETEVWPNL VHVTRRMGVP LFLVNARLSP RSYRRTARFG GAAAALYNDF
TMVLAQTAGD AERYRALGVK SVQVTGNLKF DMQPPEAGVA RGQLLRQAFG NRHVLAAAST
REGEEPLILE AFSRWPGTDR PALLLVPRHP QRFDEVAAMA TRAGFSVQRR SALDIEQLSA
PITADVVLGD SMGEMAMYYA ASDIAYIGGS LIPLGGQNLI EACAVGTPVL MGPHTFNFAQ
ATEDAIAAGA CQRVADADEL MVAAAAILGD ATRLADMREH ALTFAGLHRG ATARTLGALA
PVLR
//
