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Database: UniProt
Entry: G4SXZ7_META2
LinkDB: G4SXZ7_META2
Original site: G4SXZ7_META2 
ID   G4SXZ7_META2            Unreviewed;       406 AA.
AC   G4SXZ7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
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   Name=fabB {ECO:0000313|EMBL:CCE24298.1};
GN   OrderedLocusNames=MEALZ_2623 {ECO:0000313|EMBL:CCE24298.1};
OS   Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS   B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylotuvimicrobium.
OX   NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE24298.1, ECO:0000313|Proteomes:UP000008315};
RN   [1] {ECO:0000313|Proteomes:UP000008315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC   {ECO:0000313|Proteomes:UP000008315};
RX   PubMed=22207753; DOI=10.1128/JB.06392-11;
RA   Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA   Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA   Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA   Trotsenko Y.A., Kalyuzhnaya M.G.;
RT   "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT   Methylomicrobium alcaliphilum 20Z.";
RL   J. Bacteriol. 194:551-552(2012).
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; FO082060; CCE24298.1; -; Genomic_DNA.
DR   RefSeq; WP_014149067.1; NC_016112.1.
DR   AlphaFoldDB; G4SXZ7; -.
DR   STRING; 1091494.MEALZ_2623; -.
DR   KEGG; mah:MEALZ_2623; -.
DR   PATRIC; fig|271065.3.peg.2690; -.
DR   HOGENOM; CLU_000022_69_2_6; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000008315; 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; 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:CCE24298.1};
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:UP000008315};
KW   Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:CCE24298.1}.
FT   DOMAIN          1..403
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   406 AA;  43217 MW;  8FB18051295E9BE9 CRC64;
     MKRVVVTGLG IVSSIGNNRE EVVDSLKQGR SGISFANDYQ ELGFRSHVRG AINIDLNEFI
     DRKVKRFMGD GAAFNYVAMQ QAIEDSGLEE SEISNFRTGL VMGSGGPSTS NLVDAADILR
     EKGIKKVGPY MVPRTMSSTN TACLATPFKI KGVNYSISSA CATSAHCIGH AMELIQMGKQ
     DVVFAGGGEE VHWTMSLLFD AMGALSSKYN DAPETASRPY DATRDGFVIS GGGGVLVIEE
     LEHAKARGAK IYAELTGYGA TSDGYDMVQP SGEGAIRCMQ QAMATVDAEI DYINAHGTST
     PVGDTKELEA LRTVFGQGNV PKVSSTKSLT GHALGAAGVN EAIYSLLMME EGFLSASANI
     TELDPDATDI PIVREFKDNV TLNTIMSNSF GFGGTNATLI FQRYNG
//
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