ID E5BF95_9FUSO Unreviewed; 412 AA.
AC E5BF95;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 Name=waaA {ECO:0000313|EMBL:EFS20776.1};
GN ORFNames=FSBG_00273 {ECO:0000313|EMBL:EFS20776.1};
OS Fusobacterium gonidiaformans 3-1-5R.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=469605 {ECO:0000313|EMBL:EFS20776.1, ECO:0000313|Proteomes:UP000002975};
RN [1] {ECO:0000313|EMBL:EFS20776.1, ECO:0000313|Proteomes:UP000002975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_5R {ECO:0000313|EMBL:EFS20776.1,
RC ECO:0000313|Proteomes:UP000002975};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA Nusbaum C., Galagan J., Birren B.;
RT "The Genome Sequence of Fusobacterium sp. 3_1_5R.";
RL Submitted (FEB-2009) 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}.
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DR EMBL; GG657971; EFS20776.1; -; Genomic_DNA.
DR AlphaFoldDB; E5BF95; -.
DR HOGENOM; CLU_036146_2_0_0; -.
DR OrthoDB; 9789797at2; -.
DR UniPathway; UPA00958; -.
DR Proteomes; UP000002975; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000313|EMBL:EFS20776.1};
KW Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103};
KW Membrane {ECO:0000256|RuleBase:RU365103};
KW Reference proteome {ECO:0000313|Proteomes:UP000002975};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT DOMAIN 35..205
FT /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF04413"
FT COILED 364..391
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT SITE 125
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT SITE 202
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ SEQUENCE 412 AA; 48191 MW; EB59C18C0740D093 CRC64;
MRLMYSLLHS FLVKMISLLG KEKQKDFIHK RIFQEYKALP KTIEIWIHAS SVGEVNLLER
FLLGCLEAFE GEILLTVFTD TGKEAALQKY GKYERVHILY FPLDDKVSIQ KILTQISLKN
LYIIETELWP NLIRFCKKEA RVVVLNGRIS NRSFGRYQKI KFLLTPLLQK IDYYYLQTEE
DKKRYIALGA KEEYCNIVGN LKFDISMPSY SQEEKEAYRK ELKLNTRKLW VAGSTRTGEY
EILLEAFQQL EDYTLVIVPR HLERVPEIES LLKEKKISYQ KYTDEEKRED IAVLLVDKMG
VLRKLYSIAD VTFVGATLVN IGGHSLLEPL AYGKTPIFGP YTQNVKEIAK EILEKKIGYQ
VVDAKTMLEA IDMIEQQSQE VREKVECFLK ENKEVGKKIL EREAQWNTKK KK
//
