ID   Q3SWP0_NITWN            Unreviewed;       407 AA.
AC   Q3SWP0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   02-SEP-2026, entry version 120.
DE   RecName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I {ECO:0000256|PROSITE-ProRule:PRU10022};
DE            EC=2.3.1.41 {ECO:0000256|PROSITE-ProRule:PRU10022};
GN   OrderedLocusNames=Nwi_0033 {ECO:0000313|EMBL:ABA03301.1};
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA03301.1, ECO:0000313|Proteomes:UP000002531};
RN   [1] {ECO:0000313|EMBL:ABA03301.1, ECO:0000313|Proteomes:UP000002531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255
RC   {ECO:0000313|Proteomes:UP000002531};
RX   PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3Z)-decenoyl-[ACP] + malonyl-[ACP] + H(+) = 3-oxo-(5Z)-
CC         dodecenoyl-[ACP] + holo-[ACP] + CO2; Xref=Rhea:RHEA:54940, Rhea:RHEA-
CC         COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9927, Rhea:RHEA-
CC         COMP:14042, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78798, ChEBI:CHEBI:138410;
CC         Evidence={ECO:0000256|ARBA:ARBA00048121};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941;
CC         Evidence={ECO:0000256|ARBA:ARBA00048121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP]
CC         + holo-[ACP] + CO2; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00048506};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC         Evidence={ECO:0000256|ARBA:ARBA00048506};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; CP000115; ABA03301.1; -; Genomic_DNA.
DR   RefSeq; WP_011313372.1; NC_007406.1.
DR   AlphaFoldDB; Q3SWP0; -.
DR   STRING; 323098.Nwi_0033; -.
DR   KEGG; nwi:Nwi_0033; -.
DR   eggNOG; COG0304; Bacteria.
DR   HOGENOM; CLU_000022_69_2_5; -.
DR   OrthoDB; 9808669at2; -.
DR   Proteomes; UP000002531; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   FunFam; 3.40.47.10:FF:000005; 3-oxoacyl-[acyl-carrier-protein] synthase I; 1.
DR   FunFam; 3.40.47.10:FF:000006; 3-oxoacyl-[acyl-carrier-protein] synthase I; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR014031; KAS_C.
DR   InterPro; IPR014030; KAS_N.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   NCBIfam; NF005589; PRK07314.1; 1.
DR   NCBIfam; NF005935; PRK07967.1; 1.
DR   PANTHER; PTHR11712:SF306; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 1; 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:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:ABA03301.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002531};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          1..404
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10022"
SQ   SEQUENCE   407 AA;  42979 MW;  43BC7AE02B99D5F3 CRC64;
     MRRVVVTGMG IVSSIGNSTQ EVLSSLFEAK SGITRAEKYA ELGFRSQVQG APTLNPADVV
     DRRAMRFLAE GAAWNHVAME QAIRDSGLEP NEVSNERTGI IMGSGGPSAR TIVEAADITR
     SKGPKRVGPF AVPKAMSSTA SATLATWFKI KGVNYSISSA CATSNHCIGN AYETIQIGKQ
     DIIFAGGCEE LDWSLSVLFD AMGAMSSKYN DTPATASRAY DVSRDGFVIA GGAGVVVLEE
     LEHAKARGAR IYGEVAGYGA TSDGYDMVAP SGEGAERCMR MALSTVKTKV DYINPHATST
     PAGDPPEIEA IRKVFGAGDK CPPISATKSL TGHSLGATGV QEAIYSLLMM NNGFICESAN
     ITELDPVFAD MPIVRKRIDD ARIGTVMSNS FGFGGTNATL VFKRLDA
//