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Database: UniProt
Entry: A0A1H3HZD1_9RHOB
LinkDB: A0A1H3HZD1_9RHOB
Original site: A0A1H3HZD1_9RHOB 
ID   A0A1H3HZD1_9RHOB        Unreviewed;       409 AA.
AC   A0A1H3HZD1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=SAMN05444486_101758 {ECO:0000313|EMBL:SDY20820.1};
OS   Lentibacter algarum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Lentibacter.
OX   NCBI_TaxID=576131 {ECO:0000313|EMBL:SDY20820.1, ECO:0000313|Proteomes:UP000199026};
RN   [1] {ECO:0000313|EMBL:SDY20820.1, ECO:0000313|Proteomes:UP000199026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24677 {ECO:0000313|EMBL:SDY20820.1,
RC   ECO:0000313|Proteomes:UP000199026};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNPR01000001; SDY20820.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3HZD1; -.
DR   STRING; 576131.SAMN05444486_101758; -.
DR   OrthoDB; 9808669at2; -.
DR   Proteomes; UP000199026; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000199026};
KW   Transferase {ECO:0000256|RuleBase:RU003694}.
FT   DOMAIN          1..406
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
SQ   SEQUENCE   409 AA;  42239 MW;  FA144A0BDF1EEAEF CRC64;
     MRRVVVTGLG VVSSIGNNAE EVLASLKAGT SGITFNEDMA EHGFRSRIAG NVKLNVADHV
     DKRTLRFMGP GAAYAHIAMG QAIADAGLEP SDVINERTGL VAGSGGPSTS AMLAAHQAVL
     NSGATKRIGP FAVPKTMCST VSANLSTAYQ IKGINYSITS ACSTSLHCIG NAAEQIMMGK
     QDIMFAGGGE ELDWTLSCLF DAMGAMSSKY NDTPERASRA FDANRDGFVI GGGGGILVLE
     ELSHALARGA KIYAEVTGYG ATSDGADMVA PSGEGGMRAM KLALSTLPEG RQVDYINAHG
     TSTPVGDVGE VEAVRAVFEG IKQPVISSTK SMTGHSQGAT GAQEAIYCLL SLEHDFIIPS
     INVETLDPAI KAGEIATARV DNAGLDSVMT NSFGFGGTNG SMILSKFKG
//
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