UniProt: G6F1W6

Database: UniProt
Entry: G6F1W6_9PROT

LinkDB:  G6F1W6_9PROT 
Original site:  G6F1W6_9PROT

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (4)   
   InterPro (3)   
   Pfam (1)   
All databases (10)   

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ID   G6F1W6_9PROT            Unreviewed;       429 AA.
AC   G6F1W6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ORFNames=CIN_16120 {ECO:0000313|EMBL:EHD13420.1};
OS   Commensalibacter intestini A911.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1088868 {ECO:0000313|EMBL:EHD13420.1, ECO:0000313|Proteomes:UP000005939};
RN   [1] {ECO:0000313|EMBL:EHD13420.1, ECO:0000313|Proteomes:UP000005939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A911 {ECO:0000313|EMBL:EHD13420.1,
RC   ECO:0000313|Proteomes:UP000005939};
RA   Lee W.-J., Kim E.-K.;
RT   "Genome Sequence of Commensalibacter intestini A911, isolated from
RT   Drosophila gut.";
RL   Submitted (OCT-2011) 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:EHD13420.1}.
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DR   EMBL; AGFR01000009; EHD13420.1; -; Genomic_DNA.
DR   RefSeq; WP_008854602.1; NZ_AGFR01000009.1.
DR   AlphaFoldDB; G6F1W6; -.
DR   STRING; 1088868.CIN_16120; -.
DR   PATRIC; fig|1088868.3.peg.1620; -.
DR   eggNOG; COG1519; Bacteria.
DR   OrthoDB; 9789797at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000005939; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT   DOMAIN          43..221
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            146
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT   SITE            221
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ   SEQUENCE   429 AA;  49288 MW;  35898813B0C69784 CRC64;
     MSSHYHSPTP LLFAWKVIGT ALPPLLKPYL RCRCKKGKEI QTRLPERMGI ASLPRQSGSL
     VHFHAASVGE VISIFPIITE LYKIDPEQNF LITTGTVASF HIVQQHFANH PEISDHIQHQ
     FVPLDVPHWV DRFVSYWQPS LSVIVESELW PNLIDTFYKH HVPIALMNGR LSDRSFTTWY
     RFQKTAQALL SKFDWIAARS RHDQHNFERL GVNATYWGDI KQIAPELSYD SKALQQLQEL
     FKDKPIWLAA STHPTEEVTI VKAHNILREK WPELITIIVP RHPERHIEII EQVGTIPQRS
     LNQFPDERGL WLCDTLGELG LFYRLCDIVF IGNSFDSTPK GGGHNPFEPA KLQCAMATGD
     QIHNFKQAYT LLKEAVTVTP DVESLTVWVD EMLSDPQKRE EYAQKALQIM DQQSQLAQDI
     ASHLYHLKS
//

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