ID A0A0F5K230_9BURK Unreviewed; 534 AA.
AC A0A0F5K230;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=WM40_09290 {ECO:0000313|EMBL:KKB63944.1};
OS Robbsia andropogonis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Robbsia.
OX NCBI_TaxID=28092 {ECO:0000313|EMBL:KKB63944.1, ECO:0000313|Proteomes:UP000033618};
RN [1] {ECO:0000313|EMBL:KKB63944.1, ECO:0000313|Proteomes:UP000033618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP2807 {ECO:0000313|EMBL:KKB63944.1,
RC ECO:0000313|Proteomes:UP000033618};
RA Lopes-Santos L., Castro D.B., Ottoboni L.M., Park D., Weirc B.S.,
RA Destefano S.A.;
RT "Draft Genome Sequence of Burkholderia andropogonis type strain ICMP2807,
RT isolated from Sorghum bicolor.";
RL Submitted (MAR-2015) 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}.
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:KKB63944.1}.
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DR EMBL; LAQU01000007; KKB63944.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F5K230; -.
DR STRING; 28092.WM40_09290; -.
DR PATRIC; fig|28092.6.peg.2187; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000033618; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000033618};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT DOMAIN 34..210
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT DOMAIN 409..511
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 271..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 61
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 207
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 534 AA; 57396 MW; 0FBE3997F77CA7FA CRC64;
MLREMYRLLW WIAAPVAVCR LVWRSRREPG YIRHIGERFG FVPRRQSAAP LIWVHAVSVG
ETRASQPLVD ALRQAHPDAE LLVTCMTPAG RATSVTVFGD RVARCYLPYD MRGAVRRFLA
RQRPALGVVM ETEVWPTLID ECAHAGVPLV MVNGRMSEKS FRRAQRFGAA ARSVFAGLSA
VLAQTEADAH RLEELGARRT AVLGNLKFDV PCDTALIDAG ARWRLAIGDR PVWVAASTRE
GEEALVLDAF ARQREAARAW REASGVVGEA SAQSQSVRRG SPKQSVQAAR LATPPQTARV
EDVIEAGVEP VGVTSAAPVA VAQAAVLEGG NAQASEEDIP AVTAKPFKAV DAGAFDERTD
AERALLILVP RHPQRFNEVS ALVASRYKTV RRSEWAEAAP SRAPRDVLPE DVDVLIGDSM
GELPAYYGAS DLAFIGGSLV PTGGQNLIEA AAAGTPVLLG PHTYNFTQAS ANAIGVGAAM
RVATPDALGD AVASLLRDHS RRQAMGLAAR QFAEKDRGAT ARTVAFLAEF LRPA
//
