ID U2QV88_9FUSO Unreviewed; 409 AA.
AC U2QV88;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=HMPREF1984_01478 {ECO:0000313|EMBL:ERK66835.1};
OS Leptotrichia sp. oral taxon 215 str. W9775.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1321779 {ECO:0000313|EMBL:ERK66835.1, ECO:0000313|Proteomes:UP000016640};
RN [1] {ECO:0000313|EMBL:ERK66835.1, ECO:0000313|Proteomes:UP000016640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W9775 {ECO:0000313|EMBL:ERK66835.1,
RC ECO:0000313|Proteomes:UP000016640};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-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|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:ERK66835.1}.
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DR EMBL; AWVR01000052; ERK66835.1; -; Genomic_DNA.
DR AlphaFoldDB; U2QV88; -.
DR STRING; 1321779.HMPREF1984_01478; -.
DR PATRIC; fig|1321779.3.peg.1401; -.
DR eggNOG; COG1519; Bacteria.
DR HOGENOM; CLU_036146_2_0_0; -.
DR OrthoDB; 9789797at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000016640; 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:UP000016640};
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..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365103"
FT DOMAIN 34..209
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
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 207
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 409 AA; 47858 MW; D9D12DC0261044B6 CRC64;
MIIVYNILRY FLYGIIGIVS IFNKKLRIFF NKRLKQDFSK RKFSNNKNEA ILIHMSSVGE
FNLSRELIDR LILKGENVIL SIMTDTGKAA AEKGYGNNEN VAIFYFPLDD YVCLANLFKT
YKIKKTVIIE TEIWPNLYSV ASEKSELYII NGRLTEKKMK SYLKIKGFIK KLLNKAEKIM
VQSDEDRKRY VSLGLTDEKV KVYKNLKYSI KYEKISEEAE EKYIENNIQK DKKIIVCGST
RPGEEKIWLE VFKEINEEKE YQLVLVLRHL DRIDEVINEI HQVFPEGENS KISYSLMSED
KKTDILVVDK MGVLRDFYQL ADFVFVGGTL VDIGGHSILE PLYYGKKPII GNYYQNIAEI
VEDAKKMSFI KIVENKNEIV EYLKKSEKVD TSEFFRKNNE IDKILEELE
//
