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Database: UniProt
Entry: Q07V19_RHOP5
LinkDB: Q07V19_RHOP5
Original site: Q07V19_RHOP5 
ID   Q07V19_RHOP5            Unreviewed;       408 AA.
AC   Q07V19;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 86.
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   OrderedLocusNames=RPE_0256 {ECO:0000313|EMBL:ABJ04215.1};
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ04215.1};
RN   [1] {ECO:0000313|EMBL:ABJ04215.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53 {ECO:0000313|EMBL:ABJ04215.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) 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}.
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DR   EMBL; CP000463; ABJ04215.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07V19; -.
DR   STRING; 316055.RPE_0256; -.
DR   KEGG; rpe:RPE_0256; -.
DR   eggNOG; COG0304; Bacteria.
DR   HOGENOM; CLU_000022_69_2_5; -.
DR   OrthoDB; 9808669at2; -.
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:ABJ04215.1};
KW   Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:ABJ04215.1}.
FT   DOMAIN          1..405
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   408 AA;  43092 MW;  517164F6CD788C02 CRC64;
     MRRVVVTGMG IVSSIGNNTQ EVLASLHEAK SGITRAEKHA ELGFRSQVYG LPTLNSADLV
     DRRAMRFLGE GAAWNHVAMD QALLDSGLEQ DDISNIRTGI VMGSGGPSAR TIVEAADITR
     TKGPKRIGPF AVPKAMSSTA SATLATWFKI KGVNYSISSA CATSNHCIGN AYELIQWGKQ
     DVMFAGGCEE LDWSLSNLFD AMGAMSSKYN DTPATASRPY DVSRDGFVIA GGAGVVVLEE
     LEHAKARGAK IYGEIIGYGA TSDGYDMVAP SGEGAERCMK MALETTGGIK IDYINPHATS
     TPAGDPPELQ ALRNVFGTGD KCPPISATKA LTGHSLGATG VQEAIYSLLM MQNGFICESA
     NITELDPAFA DMPIVRKRVD NAKLGAVLSN SFGFGGTNAT LVFKRMDA
//
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