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Database: UniProt
Entry: W2UL36_9FLAO
LinkDB: W2UL36_9FLAO
Original site: W2UL36_9FLAO 
ID   W2UL36_9FLAO            Unreviewed;       416 AA.
AC   W2UL36;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ORFNames=P278_26610 {ECO:0000313|EMBL:ETN94718.1};
OS   Zhouia amylolytica AD3.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zhouia.
OX   NCBI_TaxID=1286632 {ECO:0000313|EMBL:ETN94718.1, ECO:0000313|Proteomes:UP000018850};
RN   [1] {ECO:0000313|Proteomes:UP000018850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD3 {ECO:0000313|Proteomes:UP000018850};
RA   Jin H., Jeon C.O.;
RT   "Draft genome sequence from a member of Zhouia, isolated tidal flat.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN94718.1, ECO:0000313|Proteomes:UP000018850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD3 {ECO:0000313|EMBL:ETN94718.1,
RC   ECO:0000313|Proteomes:UP000018850};
RX   PubMed=27151796;
RA   Jia B., Jin H.M., Lee H.J., Jeon C.O.;
RT   "Draft Genome Sequence of Zhouia amylolytica AD3, Isolated from Tidal Flat
RT   Sediment.";
RL   Genome Announc. 4:0-0(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETN94718.1}.
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DR   EMBL; AYXY01000023; ETN94718.1; -; Genomic_DNA.
DR   RefSeq; WP_038267561.1; NZ_AYXY01000023.1.
DR   AlphaFoldDB; W2UL36; -.
DR   STRING; 376730.SAMN04487906_1542; -.
DR   PATRIC; fig|1286632.3.peg.2653; -.
DR   eggNOG; COG0304; Bacteria.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000018850; Unassembled WGS sequence.
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:UP000018850};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          3..414
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        165
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ   SEQUENCE   416 AA;  44575 MW;  4327B8ACF62B8017 CRC64;
     MKFKRVVVTG LGALTPIGNN LQEYWDGLQK GVSGAAPITH FDASKFKTQF ACEVKNFQVT
     DFIDRKEARR LDKFAQYAMV ASDEAIVDSK LDLEKIDMDR IGVIWGAGIG GLETFQEEVL
     NFGRGDGTPR FNPFFIPKMI ADIAPGLISI KHGFRGPNFT TVSACASSAN AMIDALNYIR
     LGHADIIVTG GSEAAVTAAG IGGFNAMHAL STRNDDPKTA SRPFDANRDG FVLGEGAGAI
     ILEDYDHAVA RGAKIYCEIA GGGLSADAHH MTAPHPEGLG AKNVMRNCLK DAGLNPEDVD
     HINMHGTSTP LGDVAESKAI KEVFGEHTYN ININSTKSMT GHLLGAAGAI EAISSIMAIV
     HGVVPPTINH ETYDEKIDSK MNFTFNEAQK RDVKVAMSNT FGFGGHNACV LFKKLD
//
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