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Database: UniProt
Entry: L2EMU9_9BURK
LinkDB: L2EMU9_9BURK
Original site: L2EMU9_9BURK 
ID   L2EMU9_9BURK            Unreviewed;       424 AA.
AC   L2EMU9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   ORFNames=D769_03705 {ECO:0000313|EMBL:ELA00696.1};
OS   Cupriavidus sp. HMR-1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1249621 {ECO:0000313|EMBL:ELA00696.1, ECO:0000313|Proteomes:UP000010442};
RN   [1] {ECO:0000313|EMBL:ELA00696.1, ECO:0000313|Proteomes:UP000010442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMR-1 {ECO:0000313|EMBL:ELA00696.1,
RC   ECO:0000313|Proteomes:UP000010442};
RX   PubMed=23409271;
RA   Li L.G., Cai L., Zhang T.;
RT   "Genome of Cupriavidus sp. HMR-1, a Heavy Metal-Resistant Bacterium.";
RL   Genome Announc. 1:E00202-E00212(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ELA00696.1}.
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DR   EMBL; ANKP01000029; ELA00696.1; -; Genomic_DNA.
DR   RefSeq; WP_008642216.1; NZ_ANKP01000029.1.
DR   AlphaFoldDB; L2EMU9; -.
DR   PATRIC; fig|1249621.3.peg.736; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000010442; Unassembled WGS sequence.
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   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;  46212 MW;  2619A8F0EA9A9289 CRC64;
     MLRFVYSLLW LLILPLALLR LVWRSRKEAG YIQHVGERLG RYGDLSAAGP WLWVHAVSVG
     ETRAAQPLID ALLAAYPRHR LLLTHMTPTG RQTGAQLYGA NPRVQQCYLP YDLPWLVRRF
     LAYFQPDAGL IMETEVWPNL VHVTRRVGVP LFLVNARLSP RSYRRTARFG SAAAALYNDF
     TMVLAQTAGD AERYRALGVK SVQVTGNLKF DMQPPEAGVA RGQLLRQAFG NRHVLAAAST
     REGEEPLILE AFSRWPGTDR PALLLVPRHP QRFDEVAAMA TRAGFSVQRR SALDVEQLAG
     PITADVVLGD SMGEMAMYYA ASDIAYIGGS LIPLGGQNLI EACAVGTPVL MGPHTFNFAQ
     ATEDAIAAGA CQRVADADEL IAAAAAILGD ATRLADMREH ALTFAGLHRG ATARTLGALA
     PVLR
//
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