ID N9B7M4_9GAMM Unreviewed; 426 AA.
AC N9B7M4;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=F947_01662 {ECO:0000313|EMBL:ENV69602.1};
OS Acinetobacter towneri DSM 14962 = CIP 107472.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120929 {ECO:0000313|EMBL:ENV69602.1, ECO:0000313|Proteomes:UP000023781};
RN [1] {ECO:0000313|EMBL:ENV69602.1, ECO:0000313|Proteomes:UP000023781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107472 {ECO:0000313|EMBL:ENV69602.1,
RC ECO:0000313|Proteomes:UP000023781};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter towneri CIP 107472.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:ENV69602.1}.
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DR EMBL; APPY01000058; ENV69602.1; -; Genomic_DNA.
DR RefSeq; WP_004974270.1; NZ_KB849690.1.
DR AlphaFoldDB; N9B7M4; -.
DR PATRIC; fig|1120929.3.peg.1577; -.
DR HOGENOM; CLU_036146_2_0_6; -.
DR OrthoDB; 9789797at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000023781; Unassembled WGS sequence.
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 35..215
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT DOMAIN 264..405
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
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 426 AA; 48293 MW; 105AA03591D77DFD CRC64;
MATPFWYNAA LALLKPIYQS RIRKRAEHPE QLQQELLERF GPFQPAKNLH AIWFHVVSVG
ETNAAQPLIE HYLKAGHPVL VTNTTKTGQA RAKSLFLKAP YLDLFQAVYL PADQVHLIRE
FYQKYQPKLL ALVETELWPN LIDQAQHFQV PCLLINARLS EKSAKGYAKV KGLTRGMLQN
LQQLLAQDSA TQQRFIALGM PAERTNVVGN IKFDITAPED FVEQAAQLQQ TWQLAHRKII
TLASTHAPEE QQLLTALKPY FAQHPELLCI VVPRHPERFD EVAVQVKKLQ LNMQRRSLAE
AIQPETQVYL ADSMGEMWLW YALSQACYVG GSLNEPGGGH NILEPLALNV ATVLGKNYFN
FQSIVDEFVA AEAVYVVENA EQAVNTLTQL LFEPALRAQL NQNAQVIMYK NRGSLTEHIH
VMNQYL
//
