ID K2ADB8_9BACT Unreviewed; 417 AA.
AC K2ADB8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=ACD_60C00105G0001 {ECO:0000313|EMBL:EKD54243.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD54243.1};
RN [1] {ECO:0000313|EMBL:EKD54243.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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:EKD54243.1}.
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; AMFJ01025430; EKD54243.1; -; Genomic_DNA.
DR AlphaFoldDB; K2ADB8; -.
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};
KW Transmembrane {ECO:0000256|RuleBase:RU365103};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365103}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365103"
FT DOMAIN 32..208
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT DOMAIN 235..398
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT SITE 128
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT SITE 206
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 417 AA; 46984 MW; 1F7431423AA71344 CRC64;
MRYLYSLLFY LALPFIFLRL LWRSRKNPLY RKRLAERLGF CPHRLNQCIW VHAVSLGETI
AAHPLIKALK IKYPHIPILV TNMTLTGSVR VAASLGDSVL NAYIPYDVPD AVARFIDRVH
PKILVIMETE LWPNLFAACK KRNIPIVLTN ARLSNQSAKG YHRIKPLVSD MLTAITVLSA
QAEPDASRFI ELGMEKNRVK MTGSLKFDLE ILPEVITKGK ALRNQLGDTR LIWVAASTHN
GEEEIILAAH RIIHQKLPNV LLILVPRHPE RFDDVAKKIK EQGFHLVRRS EKNPCSENTA
VYLGDTMGEM LLMYAASDVT FVGGSFVPIG GHNVIEPAAL HKPVITGPYL FNFAEVSDLM
LAANGMIKVE DAEQLSEKVI HFFMDEETRK KTGDNAFQVV EKNRGALKRQ VDLINLG
//
