ID A0A2Z2LEQ9_9BURK Unreviewed; 453 AA. AC A0A2Z2LEQ9; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 28-JUN-2023, entry version 18. 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=BA022_04950 {ECO:0000313|EMBL:ASI67982.1}; OS Diaphorobacter nitroreducens. OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Diaphorobacter. OX NCBI_TaxID=164759 {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 (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 --------------------------------------------------------------------------- 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 AlphaFoldDB; A0A2Z2LEQ9; -. DR EnsemblBacteria; ASI67982; ASI67982; BA022_04950. DR KEGG; dpy:BA022_04950; -. DR UniPathway; UPA00958; -. DR Proteomes; UP000250185; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}. FT DOMAIN 38..222 FT /note="3-deoxy-D-manno-octulosonic-acid transferase N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF04413" FT ACT_SITE 74 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1" FT SITE 144 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2" FT SITE 220 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2" 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 //