ID Q72F79_DESVH Unreviewed; 530 AA.
AC Q72F79;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 98.
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 OrderedLocusNames=DVU_0335 {ECO:0000313|EMBL:AAS94818.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS94818.1, ECO:0000313|Proteomes:UP000002194};
RN [1] {ECO:0000313|EMBL:AAS94818.1, ECO:0000313|Proteomes:UP000002194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000313|Proteomes:UP000002194};
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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|RuleBase:RU365103};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC {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}.
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DR EMBL; AE017285; AAS94818.1; -; Genomic_DNA.
DR RefSeq; WP_010937642.1; NC_002937.3.
DR RefSeq; YP_009559.1; NC_002937.3.
DR AlphaFoldDB; Q72F79; -.
DR STRING; 882.DVU_0335; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR PaxDb; 882-DVU_0335; -.
DR EnsemblBacteria; AAS94818; AAS94818; DVU_0335.
DR KEGG; dvu:DVU_0335; -.
DR PATRIC; fig|882.5.peg.316; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_0_7; -.
DR OrthoDB; 9789797at2; -.
DR PhylomeDB; Q72F79; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000002194; 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.
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:UP000002194};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT DOMAIN 125..267
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT SITE 185
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT SITE 264
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 530 AA; 56061 MW; 3178EEABD3A61362 CRC64;
MPLRLHHRAL LALYGAVWRL ARPVLARNRR LAHRFEERLV PRQWATPVDV WVQSASGGES
YLAWELLKAL PVAVAQDAGV GMADRPGGRA EGGTQPGSCG DVHNGMGTAT PSGCRADGAG
MPPVRKVLLT SCTEQGLDVL HKAVAWAADE RPDLDVQVQV FPFDEPYLMG EALAQAKPRA
VVLLETELWP GLLAACTVAG IPVGVVNGRM TPPSLAAYLA IEGFWQAVGP CRVAAMSDDD
AMRFALLLGR RAGADGVDVM PNMKFDRVVP DVVASSGASS AEAHGNAAKC DAVPPCTGGG
ALSGTGGTVA GGRPDADAPG TPAPMGEVLR EGASLVVFGS VREEEETALL SVLLRLRDER
PRTDIAIAPR HMHRVEAWCH MMRHAGITPV LRSSLTTPPA PGAVIVWDTF GELGALYAAA
RAVFVGGSLA PLGGQNYLEP LARGVVPCVG PYLGNFEWIG DALRQQGLVQ VVPDADALAG
ALLGQLERPM PRDRVLERFM AWAEPRRGGA LRAVQVVEEL LAMPTQQGDR
//
