UniProt: A0A014NR91

Database: UniProt
Entry: A0A014NR91_9GAMM

LinkDB:  A0A014NR91_9GAMM 
Original site:  A0A014NR91_9GAMM

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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   A0A014NR91_9GAMM        Unreviewed;       424 AA.
AC   A0A014NR91;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=BG55_05620 {ECO:0000313|EMBL:EXU76355.1};
OS   Erwinia mallotivora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU76355.1, ECO:0000313|Proteomes:UP000019918};
RN   [1] {ECO:0000313|EMBL:EXU76355.1, ECO:0000313|Proteomes:UP000019918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU76355.1,
RC   ECO:0000313|Proteomes:UP000019918};
RA   Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA   Mat Amin N.;
RT   "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT   pathogen.";
RL   Submitted (FEB-2014) 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|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:EXU76355.1}.
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DR   EMBL; JFHN01000029; EXU76355.1; -; Genomic_DNA.
DR   RefSeq; WP_034935153.1; NZ_VFIK01000010.1.
DR   AlphaFoldDB; A0A014NR91; -.
DR   STRING; 69222.BG55_05620; -.
DR   PATRIC; fig|69222.5.peg.1164; -.
DR   OrthoDB; 9789797at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000019918; 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:UP000019918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT   DOMAIN          32..210
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   ACT_SITE        59
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            129
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   424 AA;  47602 MW;  24C6E4D9C660F423 CRC64;
     MTTLYTVLLY LIQPLIWLRL WLRGRKAPAY RKRWAERYGY CAGKVKPDGI LLHSVSVGET
     LAAVPLVRAL RHRYPAMPIT VTTMTPTGSE RAASAFGKDV HHVYLPYDLP GSMQRFLDNV
     SPRLVIIMET ELWPNMIAEL HARNIPLVIA NARLSERSAR GYKKLGKFMQ RLLRQITLIA
     AQNAEDGERF ISLGLKRTQL TITGSLKFDI SVTPELAARA VTLRRQWAPR RPVWIATSTH
     DGEESVILDA HRRLLQRFPT LLLILVPRHP ERFATARDMA QKNGFSFILR SSGEIPSGST
     QVVIGDTMGE LMLLYGIADL AFVGGSLVER GGHNPLEAAA HAIPVLMGPH TFNFKDICAR
     LSQADGLITV TDASSLDKEI GTLLTDEDYR LYYGRHAVEV LHQNQGALQR LLQLLEPYLP
     QRNH
//

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