ID Q8RSW9_YEREN Unreviewed; 425 AA.
AC Q8RSW9;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 47.
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 Name=waaA {ECO:0000313|EMBL:AAL78077.1};
OS Yersinia enterocolitica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630 {ECO:0000313|EMBL:AAL78077.1};
RN [1] {ECO:0000313|EMBL:AAL78077.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R102 {ECO:0000313|EMBL:AAL78077.1};
RX PubMed=12427940;
RA Izquierdo L., Abitiu N., Coderch N., Hita B., Merino S., Gavin R.,
RA Tomas J.M., Regue M.;
RT "The inner-core lipopolysaccharide biosynthetic waaE gene: function and
RT genetic distribution among some Enterobacteriaceae.";
RL Microbiology 148:3485-3496(2002).
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}.
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DR EMBL; AY075041; AAL78077.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RSW9; -.
DR CAZy; GT30; Glycosyltransferase Family 30.
DR UniPathway; UPA00958; -.
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; IPR001296; Glyco_trans_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; PF00534; Glycos_transf_1; 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 33..211
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT DOMAIN 301..398
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT SITE 130
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT SITE 208
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 425 AA; 47823 MW; 9C34F68758D0B149 CRC64;
MLLRLYQVLL YLIQPLIWLR LLLRSRKAPA YRKRWAERYG FCAGKVVPGG IMLHSVSVGE
TLAAIPLVRA LRHRYPALPI TVTTMTPTGS ERVQSAFGKD VHHVYLPYDL PGSMNRFLDQ
VNPKLVIIME TELWPNLINA LHQRQIPLVI ANARLSARSA AGYKKIGGFM RDMLRRITLI
AAQNQEDGDR FIELGLKRSQ LAVTGSLKFD ISVTPELAAR AVTLRRQWAP RRPVWIATST
HEGEETILLE AHRKLLEKHP DLREIFVPSH RERFPPAKEL AQKAGFRYTL RSSGEIPSGS
TQVVIGDTMG ELMLLYGIAD LAFVGGSLVE RGGHNPLEAA AHAIPVLMGP HTFNFKDICA
KLSQAEGLIT VTDVDSLVKE VETLLTDEDY RRYYGRHAVE VLYQNQGALQ RLLQLLEPHL
PPRSH
//
