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Database: UniProt/TrEMBL
Entry: A0A0U1RK18_NEIMA
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ID   A0A0U1RK18_NEIMA        Unreviewed;       378 AA.
AC   A0A0U1RK18;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=3-oxoacyl-(Acyl-carrier-protein) synthase II {ECO:0000313|EMBL:CAM09069.1};
DE            EC=2.3.1.41 {ECO:0000313|EMBL:CAM09069.1};
GN   OrderedLocusNames=NMA1957 {ECO:0000313|EMBL:CAM09069.1};
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587 {ECO:0000313|EMBL:CAM09069.1, ECO:0000313|Proteomes:UP000000626};
RN   [1] {ECO:0000313|EMBL:CAM09069.1, ECO:0000313|Proteomes:UP000000626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491 {ECO:0000313|Proteomes:UP000000626};
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C., Klee S.R.,
RA   Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P.,
RA   Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Mungall K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Simmonds M., Skelton J., Whitehead S., Spratt B.G., Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC       ECO:0000256|RuleBase:RU003694}.
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DR   EMBL; AL157959; CAM09069.1; -; Genomic_DNA.
DR   RefSeq; WP_002246375.1; NC_003116.1.
DR   AlphaFoldDB; A0A0U1RK18; -.
DR   EnsemblBacteria; CAM09069; CAM09069; NMA1957.
DR   KEGG; nma:NMA1957; -.
DR   HOGENOM; CLU_000022_69_2_4; -.
DR   Proteomes; UP000000626; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00834; KAS_I_II; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11712:SF325; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) SYNTHASE II FABF; 1.
DR   PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:CAM09069.1};
KW   Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:CAM09069.1}.
FT   DOMAIN          1..378
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   378 AA;  40262 MW;  52F2DF23ED1015A9 CRC64;
     MDWHERFPEL EAQLGAPIEN YAPPKHWTRK QLRSMGRVSY LCVDAAEQAL TDAGLLGDES
     ITDGRMGVAC GSSSGSTKDI GDVGELLLTG MSRNFSANTY VRMMPHTAAA NIGIFFGLKG
     RIIPTSSACS SGSQGIGYAY EAIKYGLTDM MLAGGGEEFF PSEVYVFDSL YAASRRNGEP
     EKTPRPYDAN RDGLVIGEGA GIFVLEELEH AKRRGAIIYA ELVGYGANSD AYHISTPRPD
     AQGAILAFQT ALQHADLAPE DIGWINLHGT GTHHNDSMES RAVAAVFGNN TPCTSTKPQT
     GHTLGAAGAI EAAFAWGIAD RKSNPEGKLP PQLWDGQNDP DLPAINLTGS GSRWETEKRI
     AASSSFAFGG SNCVLLIG
//
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