ID A0A1N6VSX5_9GAMM Unreviewed; 405 AA.
AC A0A1N6VSX5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN05421647_10994 {ECO:0000313|EMBL:SIQ80878.1};
OS Marinobacterium stanieri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=49186 {ECO:0000313|EMBL:SIQ80878.1, ECO:0000313|Proteomes:UP000186895};
RN [1] {ECO:0000313|EMBL:SIQ80878.1, ECO:0000313|Proteomes:UP000186895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7027 {ECO:0000313|EMBL:SIQ80878.1,
RC ECO:0000313|Proteomes:UP000186895};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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 -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
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; FTMN01000009; SIQ80878.1; -; Genomic_DNA.
DR RefSeq; WP_076464876.1; NZ_FTMN01000009.1.
DR AlphaFoldDB; A0A1N6VSX5; -.
DR STRING; 49186.SAMN05421647_10994; -.
DR eggNOG; COG0304; Bacteria.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000186895; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
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; 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 Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Reference proteome {ECO:0000313|Proteomes:UP000186895};
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1..402
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 405 AA; 43115 MW; E69AC5F21F2478FA CRC64;
MRRVVVTGMG IVSCLGNDQE TVLESLKLGR SGIKFQPEYK ELGFRSQVAG SIDIDLDSLI
DRKLRRFMGN ASAYTYLAMK QAIEDSGLSE DQVSNVRTGL IAGSGGASSA DIVETADILR
SKGVRRVGPY RVTRTMGSTV SACLATPFKI KGVNYSITSA CATSAHCIGN AMEQIQLGKQ
DVIFAGGGEE LHWSLSVMFD AMGALSSKYN ETPEKASRAY DANRDGFVIA GGAGMLVLED
LEHAKARGAK IYAELVGYGA TSDGYDMVAP SGEGAIRCMQ QAMSTVDGDI DYINSHGTST
PAGDIQELKA MKQTFGDDMP PVSSTKSLTG HSLGATGVQE AIYSILMQQN NFICASANIE
ELDPEAEGMP VVTERKDGVD LKRVMSNSFG FGGTNSTLVF EKFEG
//
