ID I4SIV3_ECOLX Unreviewed; 425 AA. AC I4SIV3; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 17-JUN-2020, entry version 23. DE RecName: Full=3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|RuleBase:RU365103}; DE Short=Kdo transferase {ECO:0000256|RuleBase:RU365103}; DE EC=2.4.99.12 {ECO:0000256|RuleBase:RU365103}; DE AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase {ECO:0000256|RuleBase:RU365103}; GN ORFNames=EC54115_16880 {ECO:0000313|EMBL:EIL50394.1}; OS Escherichia coli 541-15. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=752785 {ECO:0000313|EMBL:EIL50394.1, ECO:0000313|Proteomes:UP000004544}; RN [1] {ECO:0000313|EMBL:EIL50394.1, ECO:0000313|Proteomes:UP000004544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=541-15 {ECO:0000313|EMBL:EIL50394.1, RC ECO:0000313|Proteomes:UP000004544}; RA Suzuki H., Richards V., Lefebure T., Pavinski Bitar P., Lang P., RA Stanhope M.; RL Submitted (APR-2010) 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 + CMP + H(+); Xref=Rhea:RHEA:28066, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364, CC ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12; CC Evidence={ECO:0000256|RuleBase:RU365103}; CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis. CC {ECO:0000256|RuleBase:RU365103}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {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:EIL50394.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJWQ01000186; EIL50394.1; -; Genomic_DNA. DR RefSeq; WP_000891564.1; NZ_AJWQ01000186.1. DR SMR; I4SIV3; -. DR EnsemblBacteria; EIL50394; EIL50394; EC54115_16880. DR PATRIC; fig|752785.3.peg.3268; -. DR BioCyc; ECOL752785:G10ZY-3283-MONOMER; -. DR UniPathway; UPA00958; -. DR Proteomes; UP000004544; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. 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; -; 1. DR InterPro; IPR007507; Glycos_transf_N. DR InterPro; IPR038107; Glycos_transf_N_sf. DR InterPro; IPR039901; Kdotransferase. DR PANTHER; PTHR42755; PTHR42755; 1. DR Pfam; PF04413; Glycos_transf_N; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|RuleBase:RU365103}; KW Cell membrane {ECO:0000256|RuleBase:RU365103}; KW Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103}; KW Membrane {ECO:0000256|RuleBase:RU365103}; KW Transferase {ECO:0000256|RuleBase:RU365103, ECO:0000313|EMBL:EIL50394.1}. FT DOMAIN 33..211 FT /note="Glycos_transf_N" FT /evidence="ECO:0000259|Pfam:PF04413" SQ SEQUENCE 425 AA; 47291 MW; B063850A1FF392AF CRC64; MLELLYTALL YLIQPLIWIR LWVRGRKAPA YRKRWGERYG FYRHPLKPGG IMLHSVSVGE TLAAIPLVRA LRHRYPDLPI TVTTMTPTGS ERVQSAFGKD VQHVYLPYDL PDALNRFLNK VDPKLVLIME TELWPNLIAA LHKRKIPLVI ANARLSARSA AGYAKLGKFV RRLLRRITLI AAQNEEDGAR FVALGAKNNQ VTVTGSLKFD ISVTPQLAAK AVTLRRQWAP HRPVWIATST HEGEESVVIA AHQALLQQFP NLLLILVPRH PERFPDAINL VRQAGLSYIT RSSGEVPSTS TQVVVGDTMG ELMLLYGIAD LAFVGGSLVE RGGHNPLEAA AHAIPVLMGP HTFNFKDICA RLEQASGLIT VTDATTLAKE VSSLLTDADY RSFYGRHAVE VLYQNQGALQ RLLQLLEPYL PPKTH //