ID A0A062XUI8_9BACT Unreviewed; 415 AA.
AC A0A062XUI8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ORFNames=EG19_11035 {ECO:0000313|EMBL:KDA54498.1};
OS Thermoanaerobaculum aquaticum.
OC Bacteria; Acidobacteriota; Thermoanaerobaculia; Thermoanaerobaculales;
OC Thermoanaerobaculaceae; Thermoanaerobaculum.
OX NCBI_TaxID=1312852 {ECO:0000313|EMBL:KDA54498.1, ECO:0000313|Proteomes:UP000027284};
RN [1] {ECO:0000313|EMBL:KDA54498.1, ECO:0000313|Proteomes:UP000027284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP-01 {ECO:0000313|EMBL:KDA54498.1,
RC ECO:0000313|Proteomes:UP000027284};
RA Stamps B.W., Losey N.A., Lawson P.A., Stevenson B.S.;
RT "The Genome Sequence of Thermoanaerobaculum aquaticum MP-01, The First
RT Cultivated Group 23 Acidobacterium.";
RL Submitted (APR-2014) 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|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}.
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:KDA54498.1}.
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DR EMBL; JMFG01000007; KDA54498.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A062XUI8; -.
DR STRING; 1312852.EG19_11035; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000027284; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000027284};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT DOMAIN 36..208
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT SITE 127
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT SITE 205
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 415 AA; 44465 MW; 58F2FE9BEA7FF686 CRC64;
MLLYRLVLHL ALPLAAPFLW VADRRTGKRR PPLRMRLGLG LPPVPQGGVL VHAVSVGEVT
VARALLSELR RRAPQVPLLL SATTATGLEL ASGAQVADAT LPFPLDLPAP TRRFLAATQP
RLLVLVETEL WPEMLAACSE AGIPVVLVNA RISDRSFPRY QLFAPLLRPL LAPLTLALAQ
TEGDAARLVA LGVPQEKVRV TGNIKFDVKP ARPLAEDLKA RLCQLASGRA VLVAGSTMPG
EEKQVLSAWM KLPDRPFLIL APRHPERAQE VLELCRQLGL AAVRRSPLPA AHATADVVVL
DTVGELAALY QLATVAFVGG SLVPTGGHNP IEPARFAVPV VSGPHVRNFA AVYRELEVHG
GVKLVHNVRE LQETLAHLLV HPQQAQALGQ NAQAVLAKHA GATAKTVEAL LPFLP
//
