ID   A8LSD7_DINSH            Unreviewed;       409 AA.
AC   A8LSD7;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   02-SEP-2026, entry version 87.
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   Name=fabB {ECO:0000313|EMBL:ABV92751.1};
GN   OrderedLocusNames=Dshi_1009 {ECO:0000313|EMBL:ABV92751.1};
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rhodobacterales; Roseobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV92751.1, ECO:0000313|Proteomes:UP000006833};
RN   [1] {ECO:0000313|Proteomes:UP000006833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC   {ECO:0000313|Proteomes:UP000006833};
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA   Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA   Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA   Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA   Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA   Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT   a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
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; CP000830; ABV92751.1; -; Genomic_DNA.
DR   RefSeq; WP_012177682.1; NC_009952.1.
DR   AlphaFoldDB; A8LSD7; -.
DR   STRING; 398580.Dshi_1009; -.
DR   KEGG; dsh:Dshi_1009; -.
DR   eggNOG; COG0304; Bacteria.
DR   HOGENOM; CLU_000022_69_2_5; -.
DR   OrthoDB; 9808669at2; -.
DR   Proteomes; UP000006833; 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: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; 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:ABV92751.1}; 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:UP000006833};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          1..406
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10022"
SQ   SEQUENCE   409 AA;  43107 MW;  60FAD7C40542CC6E CRC64;
     MRRVVITGMG IVSPIGNTVS EVEASLRAGR SGITFAETYA ENGFRSQVHG VPDIVLEDHI
     DKRNLRFMGP GAAFNFIAMQ QAIADSGLED SNVSNERSGL IMGSGGPSTS NFFQAFKTVK
     EKGAPKRMGP FMVTRCMSST NSACLATPFK IKGVNYSITS ACSTSAHCIG NGVELIQMGK
     QDIVFAGGGE EIDWTLSCLF DAMGAMSSKY NDTPTTASRT FDATRDGFVI AGGGGVLVLE
     ELEHAKARGA KIYAEVTGYG ATSDGYDMVA PSGEGGERSM RQAIATLPEG RSVDYINAHG
     TSTPVGDVTE IEAVRRVFGE GTTPPVASTK SLTGHSLGAT GVHEAIYSLI MMNKGFIAAS
     ANITELDPAI HPEEIVTELR EGVTLDSVLS NSFGFGGTNA TLLMSRYLD
//