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Database: UniProt
Entry: A0A0D7E830_RHOPL
LinkDB: A0A0D7E830_RHOPL
Original site: A0A0D7E830_RHOPL 
ID   A0A0D7E830_RHOPL        Unreviewed;       407 AA.
AC   A0A0D7E830;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 1 {ECO:0000256|ARBA:ARBA00039450};
DE            EC=2.3.1.41 {ECO:0000256|ARBA:ARBA00013191};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase I {ECO:0000256|ARBA:ARBA00041620};
DE   AltName: Full=Beta-ketoacyl-ACP synthase I {ECO:0000256|ARBA:ARBA00042143};
GN   ORFNames=OO17_24445 {ECO:0000313|EMBL:KIZ36675.1};
OS   Rhodopseudomonas palustris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ36675.1, ECO:0000313|Proteomes:UP000032515};
RN   [1] {ECO:0000313|EMBL:KIZ36675.1, ECO:0000313|Proteomes:UP000032515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL398 {ECO:0000313|EMBL:KIZ36675.1,
RC   ECO:0000313|Proteomes:UP000032515};
RA   Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT   "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT   isolated from estuarine surface water.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3Z)-decenoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxo-(5Z)-
CC         dodecenoyl-[ACP] + CO2 + holo-[ACP]; 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:ARBA00035917};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54941;
CC         Evidence={ECO:0000256|ARBA:ARBA00035917};
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         EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00023389};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC         Evidence={ECO:0000256|ARBA:ARBA00023389};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC       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:KIZ36675.1}.
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DR   EMBL; JXXE01000566; KIZ36675.1; -; Genomic_DNA.
DR   RefSeq; WP_044416683.1; NZ_JXXE01000566.1.
DR   AlphaFoldDB; A0A0D7E830; -.
DR   STRING; 1421013.GCA_000504425_02836; -.
DR   PATRIC; fig|1076.23.peg.5861; -.
DR   OrthoDB; 9808669at2; -.
DR   Proteomes; UP000032515; 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:InterPro.
DR   CDD; cd00834; KAS_I_II; 1.
DR   Gene3D; 3.40.47.10; -; 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   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:0000313|EMBL:KIZ36675.1};
KW   Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:KIZ36675.1}.
FT   DOMAIN          1..404
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   407 AA;  43029 MW;  77DE2B83C0A34FFA CRC64;
     MRRVVVTGMG IVSSIGNNTQ EVLASLHEAK PGITRADKHV ELGFRSQVQG APTLNPADFV
     DRRAMRFLGE GAAWNHVAMD QAILDAGLEP SDISDPRTGI IMGSGGPSAR TIVEAADITR
     TKGPKRVGPF AVPKAMSSTA SATLATWFKI KGVNYSISSA CATSNHCIGN AYEMIQWNKQ
     DIVFAGGCEE LDWSLSVLFD AMGAMSSKYN DTPSTASRPY DVSRDGFVIA GGAGVIVLEE
     LEHAKARGAK IYGEIVGYGA TSDGYDMVAP SGEGAERCMK MALATVDTKV DYINPHATST
     PAGDPPEMEA IRKVFGTGDK CPPISATKAL TGHSLGATGV QEAIYSLLMM QNGFICESAN
     ITELDPAFAD MPIVRKRIDN AKVGTVLSNS FGFGGTNATL VFKRMDA
//
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