KDTA_HAEIN
ID KDTA_HAEIN Reviewed; 427 AA.
AC P44806;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=3-deoxy-D-manno-octulosonic acid transferase;
DE Short=Kdo transferase;
DE EC=2.4.99.12 {ECO:0000269|PubMed:10952982, ECO:0000269|PubMed:9195966};
DE AltName: Full=Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase;
DE AltName: Full=Monofunctional Kdo transferase;
GN Name=waaA; Synonyms=kdtA; OrderedLocusNames=HI_0652;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd, and I69 / Serotype B;
RX PubMed=10952982; DOI=10.1074/jbc.m005204200;
RA Brabetz W., Mueller-Loennies S., Brade H.;
RT "3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA) and Kdo
RT kinase (KdkA) of Haemophilus influenzae are both required to complement a
RT waaA knockout mutation of Escherichia coli.";
RL J. Biol. Chem. 275:34954-34962(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PH DEPENDENCE, AND SUBCELLULAR LOCATION.
RC STRAIN=722;
RX PubMed=9195966; DOI=10.1074/jbc.272.26.16555;
RA White K.A., Kaltashov I.A., Cotter R.J., Raetz C.R.;
RT "A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a
RT Kdo kinase in extracts of Haemophilus influenzae.";
RL J. Biol. Chem. 272:16555-16563(1997).
RN [4]
RP DOMAIN.
RX PubMed=20394418; DOI=10.1021/bi100343e;
RA Chung H.S., Raetz C.R.;
RT "Interchangeable domains in the Kdo transferases of Escherichia coli and
RT Haemophilus influenzae.";
RL Biochemistry 49:4126-4137(2010).
CC -!- FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes
CC the transfer of a single 3-deoxy-D-manno-octulosonate (Kdo) residue
CC from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-
CC bisphosphate precursor of lipid A. Is strictly monofunctional, i.e. is
CC capable of adding only a single Kdo residue to the acceptor lipid.
CC {ECO:0000269|PubMed:10952982, ECO:0000269|PubMed:9195966}.
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:0000269|PubMed:10952982, ECO:0000269|PubMed:9195966};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:9195966};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:9195966};
CC Single-pass membrane protein {ECO:0000305|PubMed:9195966}; Cytoplasmic
CC side {ECO:0000305|PubMed:9195966}.
CC -!- DOMAIN: The N-terminal half of KdtA, especially the first 30 amino acid
CC residues, is responsible for determining the number of Kdo residues
CC that are transferred to lipid IVA. {ECO:0000269|PubMed:20394418}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 30 subfamily. {ECO:0000305}.
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; AJ277814; CAC07178.1; -; Genomic_DNA.
DR EMBL; AJ277815; CAC07179.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22311.1; -; Genomic_DNA.
DR PIR; F64084; F64084.
DR RefSeq; NP_438812.1; NC_000907.1.
DR RefSeq; WP_005694491.1; NC_000907.1.
DR AlphaFoldDB; P44806; -.
DR SMR; P44806; -.
DR STRING; 71421.HI_0652; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR EnsemblBacteria; AAC22311; AAC22311; HI_0652.
DR KEGG; hin:HI_0652; -.
DR PATRIC; fig|71421.8.peg.681; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_0_6; -.
DR OMA; FIKYEFW; -.
DR PhylomeDB; P44806; -.
DR BioCyc; HINF71421:G1GJ1-687-MON; -.
DR BRENDA; 2.4.99.12; 2529.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043842; F:Kdo transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IBA:GO_Central.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11720; -; 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 PANTHER; PTHR42755; PTHR42755; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF04413; Glycos_transf_N; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..427
FT /note="3-deoxy-D-manno-octulosonic acid transferase"
FT /id="PRO_0000080289"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 270..271
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 311..313
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT BINDING 337..340
FT /ligand="CMP"
FT /ligand_id="ChEBI:CHEBI:60377"
FT /evidence="ECO:0000250"
FT SITE 132
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 48743 MW; 2B007E5B47EDD17D CRC64;
MWRFFYTSLL LICQPLILCF IGLLSVKSPR YRQRLAERYG FYGNASCPPP QGIFIHAASV
GEVIAATPLV RQLQQDYPHL SITFTTFTPT GSERVKATFG DSVFHYYLPL DLPFSIHRFI
NFVQPKLCIV METELWPNLI HQLFLRNIPF VIANARLSAR SAHRYGKIKA HLQTMWSQIS
LIAAQDNISG KRYATLGYPK EKLNITGNIK YDLNTNDELL RKIDSLRTLW KQDRPIWIAA
STHNGEDEII LKSHRALLAK YPNLLLLLVP RHPERFNVVA DLLKKEKFQF IRRSTNELPN
ENTQVILGDS MGELMLMYGI SDIAFVGGSL VKHGGHNPLE PLAFKMPVIT GKHTFNFPEI
FRMLVEVQGV LEVNSTADAL ERAVEALLNS KESRERLGNA GYEVLMENRG ALQRLLDLLK
PYLERNV
