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Database: UniProt
Entry: C6XF54_LIBAP
LinkDB: C6XF54_LIBAP
Original site: C6XF54_LIBAP 
ID   C6XF54_LIBAP            Unreviewed;       423 AA.
AC   C6XF54;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 80.
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   OrderedLocusNames=CLIBASIA_02100 {ECO:0000313|EMBL:ACT57006.1};
OS   Liberibacter asiaticus (strain psy62).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=537021 {ECO:0000313|EMBL:ACT57006.1, ECO:0000313|Proteomes:UP000002744};
RN   [1] {ECO:0000313|EMBL:ACT57006.1, ECO:0000313|Proteomes:UP000002744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX   PubMed=19589076; DOI=10.1094/MPMI-22-8-1011;
RA   Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L.,
RA   Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y.,
RA   Gottwald T.;
RT   "Complete genome sequence of citrus huanglongbing bacterium, 'Candidatus
RT   Liberibacter asiaticus' obtained through metagenomics.";
RL   Mol. Plant Microbe Interact. 22:1011-1020(2009).
RN   [2] {ECO:0000313|EMBL:ACT57006.1, ECO:0000313|Proteomes:UP000002744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX   PubMed=21784907; DOI=10.1128/AEM.05111-11;
RA   Zhou L., Powell C.A., Hoffman M.T., Li W., Fan G., Liu B., Lin H., Duan Y.;
RT   "Diversity and plasticity of the intracellular plant pathogen and insect
RT   symbiont, 'Candidatus Liberibacter asiaticus', revealed by hyper variable
RT   prophage genes with intragenic tandem repeats.";
RL   Appl. Environ. Microbiol. 77:6663-6673(2011).
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; CP001677; ACT57006.1; -; Genomic_DNA.
DR   RefSeq; WP_015452625.1; NC_012985.3.
DR   AlphaFoldDB; C6XF54; -.
DR   STRING; 537021.CLIBASIA_02100; -.
DR   GeneID; 66286255; -.
DR   KEGG; las:CLIBASIA_02100; -.
DR   eggNOG; COG0304; Bacteria.
DR   HOGENOM; CLU_000022_69_2_5; -.
DR   OrthoDB; 9808669at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002744; 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; -; 2.
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   Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          1..418
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        171
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ   SEQUENCE   423 AA;  44539 MW;  626E3069A3CA4341 CRC64;
     MRRVVVTGLG MITPLGCGVD VSWSRLIAGE VGIRHLDQKF DLEGLSSKIA GLIPVGNGSD
     GTFNYEDWIL SSDLRKIDQF ILYGMVASDM ALADSGWAPK TDKDRNSTGV VFGSGMGGLN
     RIVESSNVLR DGGPRKISPF TVPGSIISLL SGNISIRNQL RGPNHAVTTA CSSGAHAIGD
     ASRLIAFGDA DVMVAGGAEA PICRLGVASF AACRALSTRF NDDPTRASRP FDQDRDGFVM
     GEGAGALVLE DLEHAKARGA KIYSEIIGYG LSGDAFHITM PPEDGNGAYR CMSSAIARAK
     LLPSDIDYIN AHGTSTIADT IELGAVERLM GDSCYHVSMS STKSAMGHLL GAAGAVEAAI
     CNLAIRDGIV PATLNLDNPA KKTFIDLVPH RAIKKNVNVA MSNSFGFGGT NVSLVFRKFQ
     DNI
//
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