ID   A1SRT3_PSYIN            Unreviewed;       414 AA.
AC   A1SRT3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
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=Ping_0332 {ECO:0000313|EMBL:ABM02198.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM02198.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM02198.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM02198.1,
RC   ECO:0000313|Proteomes:UP000000639};
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   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-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|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; CP000510; ABM02198.1; -; Genomic_DNA.
DR   RefSeq; WP_011768757.1; NC_008709.1.
DR   AlphaFoldDB; A1SRT3; -.
DR   STRING; 357804.Ping_0332; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   KEGG; pin:Ping_0332; -.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_036146_2_0_6; -.
DR   OrthoDB; 9789797at2; -.
DR   UniPathway; UPA00958; -.
DR   Proteomes; UP000000639; 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   CDD; cd01635; Glycosyltransferase_GTB-type; 1.
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:UP000000639};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365103}.
FT   DOMAIN          36..209
FT                   /note="3-deoxy-D-manno-octulosonic-acid transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04413"
FT   ACT_SITE        58
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-1"
FT   SITE            128
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
FT   SITE            206
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR639901-2"
SQ   SEQUENCE   414 AA;  47356 MW;  37C7FAA8738F04C5 CRC64;
     MLFILYQLLQ FLFFPFICFT LIKKAKGKLP LSKLLEYLGI AKKQPFPVTC FHCVSVGEVL
     TALPLIKQYQ VQYPEQKLLI TTTTFTGYQE VKKAFGDNIE HRFLPLDFIL FSKLFFSCHN
     IQRINIIETE LWPSLLQQAK RHNVQVSLIN ARLSKRSAKR YLKFPRSACW LVSHLDKVLA
     QHQDDADRFI QLGVSKDKIT ITGSIKFDIK IDPEKQQKGE LLKKKCSHFP IILAASTHKG
     EDEIMLTAFK TLQQTEKNAL LIIVPRHPER FDSVFHLAEK KQFKTCRKTE YSQPPQDCQV
     YIGDTMGEMI IYLSLADLVI MGGSFVPVGG HNLLEPAALK KPAITGPFNF NFTDITEQLI
     NVKHTIKAEN PQQLTQLLLK QCWDPDKLTE QGEQGLKVVK NNQGALEKTL TLLI
//