GenomeNet

Database: UniProt
Entry: A5G6H2_GEOUR
LinkDB: A5G6H2_GEOUR
Original site: A5G6H2_GEOUR 
ID   A5G6H2_GEOUR            Unreviewed;       467 AA.
AC   A5G6H2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 77.
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   OrderedLocusNames=Gura_3229 {ECO:0000313|EMBL:ABQ27390.1};
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ27390.1, ECO:0000313|Proteomes:UP000006695};
RN   [1] {ECO:0000313|EMBL:ABQ27390.1, ECO:0000313|Proteomes:UP000006695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rf4 {ECO:0000313|EMBL:ABQ27390.1,
RC   ECO:0000313|Proteomes:UP000006695};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000698; ABQ27390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5G6H2; -.
DR   STRING; 351605.Gura_3229; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   KEGG; gur:Gura_3229; -.
DR   HOGENOM; CLU_036146_2_1_7; -.
DR   OMA; FIKYEFW; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000006695; 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.
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:UP000006695};
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        26..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365103"
FT   DOMAIN          56..236
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   ACT_SITE        86
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            155
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT   SITE            233
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ   SEQUENCE   467 AA;  51046 MW;  BED5A536BB70B064 CRC64;
     MSALSPGKGP AVKLVAETRD ISMINLFYNL LALISIIFVV PYHLYRSITR GRPTAFAQRF
     GFIAASDLAK LAGSDVIWVH AVSVGETVAA IPLIKALRKR YPHSKLVISN VTETGRQVAG
     KIAGIDLCLY FPFDYPFAVN RVLRKVRPSL ILVMETELWP NFIRAARRLA IPMLLVNGRI
     SDKSFHRYLR LRWFFQPILR NLAALCMQSA EDARRITAIG APAESVHITR NLKYDIAVPA
     QTGQDRAELR NRYRIPADIL LFTAGSTHNG EEEMVIKAYT AVLAGGRNAI MVLAPRHPER
     AAQVAELLGR AGFPYTRRSA LDARQEPFSS GEVLLLDTVG ELLNVYAVSD LVFVGGSLVP
     NGGHNVLEPA SLRVPVLFGP HMNNFKEIAA LLIEFGAGVR VADGGELTAM LGSLLDDEAK
     RQEMGNNGAR LLAENSGSTE RHMAVIEQFL GSGIMGQGSS AAQLNQK
//
DBGET integrated database retrieval system