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Database: UniProt
Entry: A0A0K8MAM3_9PROT
LinkDB: A0A0K8MAM3_9PROT
Original site: A0A0K8MAM3_9PROT 
ID   A0A0K8MAM3_9PROT        Unreviewed;       421 AA.
AC   A0A0K8MAM3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   13-SEP-2023, entry version 35.
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:GAO97546.1};
GN   ORFNames=Cva_00182 {ECO:0000313|EMBL:GAO97546.1};
OS   Caedimonas varicaedens.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales;
OC   Caedimonadaceae; Caedimonas.
OX   NCBI_TaxID=1629334 {ECO:0000313|EMBL:GAO97546.1, ECO:0000313|Proteomes:UP000036771};
RN   [1] {ECO:0000313|EMBL:GAO97546.1, ECO:0000313|Proteomes:UP000036771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Suzuki H., Dapper A.L., Gibson A.K., Jackson C., Lee H., Pejaver V.R.,
RA   Doak T., Lynch M.;
RT   "Caedibacter varicaedens, whole genome shotgun sequence.";
RL   Submitted (MAR-2015) 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}.
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:GAO97546.1}.
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DR   EMBL; BBVC01000008; GAO97546.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K8MAM3; -.
DR   STRING; 1629334.Cva_00182; -.
DR   OrthoDB; 9808669at2; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000036771; 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; 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; 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:UP000036771};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000447, ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          1..419
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   ACT_SITE        170
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000447-1"
SQ   SEQUENCE   421 AA;  44431 MW;  6A4690C92F05458F CRC64;
     MRRVVVTGLG LVTPLGGNTQ TTWDNLIAGK SGVRKIERFD VSDLPAKIAG LIPVGDSSQG
     CYNPDDWLDP KEQRKVDTFI AYGVAAACQA FQDSGWEAKS DEDQFRAGVM IGSGIGGLQK
     IYEASIALEK GGPKRVSPFF IPSALINEIS GNVSIKFGLK GPNHANVTAC STGAHAIGDA
     ARLIQIGDAD VMAAGGAESA VTRLGIAGFA SMKALSTEYN ETPEKASRPW DRDRDGFVMG
     EGAGVVILEE LEHAKKRGAR IYAEVIGYGL SGDAYHIAAP APDGSGVLRC MQNTLNRAEI
     NADQIDYINA HATSTPAGDE LELMAIQRLM GARARDISVS STKSSIGHLL GAAGGVEAIF
     AILSIRYKII PPTLNLDNPS DSAREMDLVP HTAKEKKVKI ALSNSFGFGG TNASLAFREL
     A
//
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