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Database: UniProt
Entry: A0A2S2E3C5_9ALTE
LinkDB: A0A2S2E3C5_9ALTE
Original site: A0A2S2E3C5_9ALTE 
ID   A0A2S2E3C5_9ALTE        Unreviewed;       412 AA.
AC   A0A2S2E3C5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000256|ARBA:ARBA00014657, ECO:0000256|PIRNR:PIRNR000447};
DE            EC=2.3.1.179 {ECO:0000256|ARBA:ARBA00012356, ECO:0000256|PIRNR:PIRNR000447};
GN   Name=fabF {ECO:0000313|EMBL:AWL12022.1};
GN   ORFNames=HMF8227_01548 {ECO:0000313|EMBL:AWL12022.1};
OS   Saliniradius amylolyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saliniradius.
OX   NCBI_TaxID=2183582 {ECO:0000313|EMBL:AWL12022.1, ECO:0000313|Proteomes:UP000245728};
RN   [1] {ECO:0000313|EMBL:AWL12022.1, ECO:0000313|Proteomes:UP000245728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF8227 {ECO:0000313|EMBL:AWL12022.1,
RC   ECO:0000313|Proteomes:UP000245728};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Salinimonas sp. HMF8227 Genome sequencing and assembly.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the type II fatty acid elongation cycle.
CC       Catalyzes the elongation of a wide range of acyl-ACP by the addition of
CC       two carbons from malonyl-ACP to an acyl acceptor. Can efficiently
CC       catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP)
CC       to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in
CC       the thermal regulation of fatty acid composition.
CC       {ECO:0000256|PIRNR:PIRNR000447}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(11Z)-
CC         octadecenoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:55040,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:10800,
CC         Rhea:RHEA-COMP:14074, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:83989,
CC         ChEBI:CHEBI:138538; EC=2.3.1.179;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000447};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; 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         Evidence={ECO:0000256|PIRNR:PIRNR000447};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|PIRNR:PIRNR000447}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC       ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
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DR   EMBL; CP029347; AWL12022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2E3C5; -.
DR   KEGG; salh:HMF8227_01548; -.
DR   OrthoDB; 9808669at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000245728; 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:UniProtKB-UniPathway.
DR   CDD; cd00834; KAS_I_II; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
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   NCBIfam; TIGR03150; fabF; 1.
DR   PANTHER; PTHR11712:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   PIRSF; PIRSF000447; KAS_II; 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:0000256|PIRNR:PIRNR000447};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW   ECO:0000256|PIRNR:PIRNR000447};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|PIRNR:PIRNR000447};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245728};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          3..411
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        164
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ   SEQUENCE   412 AA;  43094 MW;  E6A2D35A9135EC23 CRC64;
     MSKRRVVVTG LGMLSPLGLD TQTSWRNVLA GKSGIGDITR FDVSDFATRF AGEVKDFDVE
     QYMSRKESKK MDLFIQYGIA AGKQALADSG LDINEANAKR VGVAIGSGIG GLGLIEENHK
     KLLNSGPRKM SPFFVPSTIT NMISGFLSIM EGLKGPNLNI VTACTTGVHN IGVAARNIAY
     GDADAMLAGG AEAAITPLGL GGFAAARALS SRNDDPQAAS RPWDKDRDGF VMGEGAGVVM
     LEEYEHAKAR GATIYAELSG FGMSGDAFHM TSPPENGEGA ADAMENALND AQITPGQVGY
     INAHGTSTPA GDIAEVRAVH SVFKDAAKDV LVSSTKSMTG HLLGAAGSVE AIFTMLALRD
     QVAPPTINLE TPSEGCDLDF VPGQARDVSM EYALCNSFGF GGTNGSLLFK KI
//
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