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Database: UniProt
Entry: B7KT04_METC4
LinkDB: B7KT04_METC4
Original site: B7KT04_METC4 
ID   B7KT04_METC4            Unreviewed;       434 AA.
AC   B7KT04;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
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   OrderedLocusNames=Mchl_3196 {ECO:0000313|EMBL:ACK84034.1};
OS   Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS   extorquens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK84034.1, ECO:0000313|Proteomes:UP000002385};
RN   [1] {ECO:0000313|Proteomes:UP000002385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT   CM4.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACK84034.1, ECO:0000313|Proteomes:UP000002385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RX   PubMed=22887658; DOI=10.1128/JB.01009-12;
RA   Marx C.J., Bringel F., Chistoserdova L., Moulin L., Farhan Ul Haque M.,
RA   Fleischman D.E., Gruffaz C., Jourand P., Knief C., Lee M.C., Muller E.E.,
RA   Nadalig T., Peyraud R., Roselli S., Russ L., Goodwin L.A., Ivanova N.,
RA   Kyrpides N., Lajus A., Land M.L., Medigue C., Mikhailova N., Nolan M.,
RA   Woyke T., Stolyar S., Vorholt J.A., Vuilleumier S.;
RT   "Complete genome sequences of six strains of the genus Methylobacterium.";
RL   J. Bacteriol. 194:4746-4748(2012).
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}.
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DR   EMBL; CP001298; ACK84034.1; -; Genomic_DNA.
DR   RefSeq; WP_015951376.1; NC_011757.1.
DR   AlphaFoldDB; B7KT04; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   KEGG; mch:Mchl_3196; -.
DR   HOGENOM; CLU_036146_1_1_5; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000002385; Chromosome.
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   Lipopolysaccharide biosynthesis {ECO:0000256|RuleBase:RU365103};
KW   Membrane {ECO:0000256|RuleBase:RU365103};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT   DOMAIN          41..214
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            136
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT   SITE            212
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ   SEQUENCE   434 AA;  47324 MW;  56FA0803B8C8D33B CRC64;
     MRVPKLPVAL RAYRYGLYLG EPAVAGLLAW RSRRGKEDPV RLSERRGLPG RARPVGHLVW
     MHGASIGEAL SLVGLIEGMI ARGCSVLVTT GTRSAADLLS KRLPPGAVHQ YMPLDAPRWI
     ERFLAHWQPD LAVVAESEIW PNTIVSLHRR GIPLVLVNGR MSERSFKAWT RSPDTARALL
     ARIAVCLVQT REDGERFARL GAPRINVVGN LKYDSAVPPA DSQQLAYLGD MIGDRPVWVA
     ASTHAGEDEV VARVHAGLKA RFPRLLTVIV PRHPRRGEEA ARIATAAGLR VSRRAKGGRP
     LPSIDLYVAD TIGELGLFYR LCPLVFLGGS LVPHGGQNPI EPVRLDSAIL HGPHVHNFHE
     PYGALDTRGG ARRVADEAEL QKAVGELVAD PRALAAMWAK GQAALLPFEG AVGRTFAVLE
     PYVAQMKLSA RERD
//
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