ID A0A0P7WVF7_9RHOB Unreviewed; 398 AA.
AC A0A0P7WVF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=kdtA {ECO:0000313|EMBL:KPP91604.1};
GN ORFNames=HLUCCA05_00410 {ECO:0000313|EMBL:KPP91604.1};
OS Roseibaca calidilacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Roseibaca.
OX NCBI_TaxID=1666912 {ECO:0000313|EMBL:KPP91604.1, ECO:0000313|Proteomes:UP000050413};
RN [1] {ECO:0000313|EMBL:KPP91604.1, ECO:0000313|Proteomes:UP000050413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-91 {ECO:0000313|EMBL:KPP91604.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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|ARBA:ARBA00003394,
CC 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:KPP91604.1}.
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DR EMBL; LJSG01000013; KPP91604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WVF7; -.
DR STRING; 1666912.Ga0058931_2614; -.
DR OrthoDB; 9789797at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000050413; 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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU365103};
KW Glycosyltransferase {ECO:0000313|EMBL:KPP91604.1};
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 40..205
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT ACT_SITE 67
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 205
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 398 AA; 43629 MW; FC89214A74B00707 CRC64;
MTPRRPLLLQ AYLGLSRMLP SLWHGLAKQI HRHQAAKRDR FRERLGHSSI PRPSGRVIWV
HAESVGEVST VASLLHDIAE HGHIVITTTT QSGAERVESL GSERILHQFK PADTPVAIGR
FLDHWRPRAA VFVESDMPPV ALSILRQRGI ARALLAARPS GTRRRAPKIA AALLAEFDLV
TASSQSVADE LEGLKVKVHH VEDLKAYQSA VTEPLPWSEA QRTRPIWLAV SAHPEEYDLL
FAAHDHLQAR EPTALMVIAP RHPVSSRAWA PKRFAPVFFS DGHQPKDDTG LFVMDAFGHV
PQLHLLSHVS FIGGSLGKRG GHSPWEAARA GSYILTGPDI ANNAPAYNGL AHEIITTPNA
LADAVCKAWA APRPAPILRS AKNSQTTRAV LDMLQAQC
//
