ID A0A2Z2LEQ9_9BURK Unreviewed; 453 AA. AC A0A2Z2LEQ9; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 02-DEC-2020, entry version 10. 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:ARBA00018668, ECO:0000256|RuleBase:RU365103}; GN ORFNames=BA022_04950 {ECO:0000313|EMBL:ASI67982.1}; OS Diaphorobacter polyhydroxybutyrativorans. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Diaphorobacter. OX NCBI_TaxID=1546149 {ECO:0000313|EMBL:ASI67982.1, ECO:0000313|Proteomes:UP000250185}; RN [1] {ECO:0000313|EMBL:ASI67982.1, ECO:0000313|Proteomes:UP000250185} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL-205 {ECO:0000313|EMBL:ASI67982.1, RC ECO:0000313|Proteomes:UP000250185}; RX PubMed=26012582; DOI=10.1099/ijs.0.000353; RA Qiu T., Zuo Z., Gao J., Gao M., Han M., Sun L., Zhang L., Wang X.; RT "Diaphorobacter polyhydroxybutyrativorans sp. nov., a novel poly(3- RT hydroxybutyrate-co-3-hydroxyvalerate)-degrading bacterium isolated from RT biofilms."; RL Int. J. Syst. Evol. Microbiol. 65:2913-2918(2015). 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|ARBA:ARBA00000183, 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 inner membrane CC {ECO:0000256|RuleBase:RU365103}. CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC {ECO:0000256|RuleBase:RU365103}. 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; CP016278; ASI67982.1; -; Genomic_DNA. DR KEGG; dpy:BA022_04950; -. DR UniPathway; UPA00958; -. DR Proteomes; UP000250185; Chromosome. 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|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103, KW ECO:0000313|EMBL:ASI67982.1}. FT DOMAIN 38..222 FT /note="Glycos_transf_N" FT /evidence="ECO:0000259|Pfam:PF04413" SQ SEQUENCE 453 AA; 49421 MW; B577A96609ECF002 CRC64; MHQLILWLYS LAVWLATPLL LRKLRRRALT EPGYAVAVPE RFGHYPPPMD SLSPSSETEA DEQFIWIHAV SLGETRAAAI LLKELRPLLP GMRLLLTHGT ATGRAEGEKL LLPGDVQVWQ PWDTPGAVRR FLRQFRPSIG ILMETEIWPN LVAACRRRRI PLVLANARLN EKSRAGARRL GWLSRPAYAG LSAVWAQTED DAARLRDVGA HVAGVFGNLK FDVVPSPALQ AQGRTWRAAS ARPVVLLASS REGEEAMWLE VLKQKTPRAP ASQAPAAINS GVNQSVQWLV VPRHPQRFDE VQRLCEAAGL RVSRRSQWTA QPDSADVWLG DSLGEMALYY GLAHVALLGG SFAPLGGQNL IEAAAGGCPV VMGPHTFNFA EAARLAIDAG AALRVADMAE GVAAAAALAQ DPQRRRALSE RCVAFTEEHR GAALDTALAV LQRLREAVDD RPD //