ID H3KA92_9FIRM Unreviewed; 825 AA.
AC H3KA92;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Tetraacyldisaccharide 4'-kinase {ECO:0000256|HAMAP-Rule:MF_00409};
DE EC=2.7.1.130 {ECO:0000256|HAMAP-Rule:MF_00409};
DE AltName: Full=Lipid A 4'-kinase {ECO:0000256|HAMAP-Rule:MF_00409};
GN Name=lpxK {ECO:0000256|HAMAP-Rule:MF_00409};
GN ORFNames=HMPREF9454_02165 {ECO:0000313|EMBL:EHR33591.1};
OS Megamonas funiformis YIT 11815.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Megamonas.
OX NCBI_TaxID=742816 {ECO:0000313|EMBL:EHR33591.1, ECO:0000313|Proteomes:UP000005963};
RN [1] {ECO:0000313|EMBL:EHR33591.1, ECO:0000313|Proteomes:UP000005963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11815 {ECO:0000313|EMBL:EHR33591.1,
RC ECO:0000313|Proteomes:UP000005963};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Megamonas funiformis YIT 11815.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers the gamma-phosphate of ATP to the 4'-position of a
CC tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form
CC tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
CC {ECO:0000256|HAMAP-Rule:MF_00409}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+);
CC Xref=Rhea:RHEA:67840, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:176343, ChEBI:CHEBI:176425, ChEBI:CHEBI:456216;
CC EC=2.7.1.130; Evidence={ECO:0000256|HAMAP-Rule:MF_00409};
CC -!- PATHWAY: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A)
CC from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-
CC acetyl-alpha-D-glucosamine: step 6/6. {ECO:0000256|HAMAP-
CC Rule:MF_00409}.
CC -!- SIMILARITY: Belongs to the LpxK family. {ECO:0000256|HAMAP-
CC Rule:MF_00409}.
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:EHR33591.1}.
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DR EMBL; ADMB01000093; EHR33591.1; -; Genomic_DNA.
DR RefSeq; WP_008539760.1; NZ_JH601092.1.
DR AlphaFoldDB; H3KA92; -.
DR STRING; 437897.GCA_900128435_00786; -.
DR PATRIC; fig|742816.3.peg.2100; -.
DR HOGENOM; CLU_019506_0_0_9; -.
DR OrthoDB; 9789797at2; -.
DR UniPathway; UPA00359; UER00482.
DR Proteomes; UP000005963; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009029; F:tetraacyldisaccharide 4'-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 HAMAP; MF_00409; LpxK; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR007507; Glycos_transf_N.
DR InterPro; IPR038107; Glycos_transf_N_sf.
DR InterPro; IPR039901; Kdotransferase.
DR InterPro; IPR003758; LpxK.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00682; lpxK; 1.
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 Pfam; PF02606; LpxK; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00409};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00409, ECO:0000313|EMBL:EHR33591.1};
KW Lipid A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00409};
KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00409};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00409};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00409};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00409}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..215
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT DOMAIN 253..404
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT BINDING 511..518
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00409"
FT SITE 134
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT SITE 212
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 825 AA; 93547 MW; 39035C4152145964 CRC64;
MQILYNIVAI LLVILLIPYF IVRTIREKGF LKRMIQSFGF LPEHALDKVA GKNCIWIHAS
SVGEIVATSP IIKEFRREFP DTPILVSVVT NTGYTMANRI IKDADSIIYF PLDLPWLPER
FIKKIRPRVF LPVETELWPN FLKATRKYNI PVMMVNGRIS DKSVKRYKYM FSILSDMIGT
VRKFAMQSEI DASYIIRLGA DENLVTVTGN TKFDQTYTNV DEKERNNMLK ELCLDKAKGI
FLAGSTHKGE EEAVLEAYSE LKKQHPNVKL LIAPRSILRK DEIASICHKH GFKTNFRTVL
KEKPSYEQDV VILDTIGELG KVYSVGDVIY VGGSLIKHGG HNILEPAAHG KAIIVGPNMF
NFKDTHVLFS KRDACITVKN SKELTEAVLE LFNCPEKRHQ MERETLQIIE DNRGASRRSA
VILHELLDEY EKVNPVQVRS TEKIENLQTY LYKLVHDKNK KSIPAKLFLG VLYSFSLIYR
SLVNFQLNLY KWGIAKQVKL DCFVISIGNI TVGGTGKTPT AKLLARYIRD LGYKVAILNR
GYRAKWKGEV GIVSDGNQIF MSADQAGDEA YLLARSLPDI PVLIGTDRTI TGKYAVDNFN
VDVVILDDGY QHWQLKRDLN ILLVDAINIF GNGHMLPRGT LREPLNHLNR ADVCLLTKVD
QASKSACKEI RDTLAKYNDH ALVVESTHKP LGFVEIGNLF SRKPNEILSV DMMKGHKVIA
MSAIGNPASF EQTLNDIGAV ITESLRFPDH HDYTEEEIRD VMHQAEEQGA EAIIITDKDA
VKIPETLLCK KRPIPIYIIS IEVTFIDETQ VLFEYLKEKL PRLKG
//
