ID D2R442_PIRSD Unreviewed; 421 AA.
AC D2R442;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ADB18891.1};
GN OrderedLocusNames=Psta_4243 {ECO:0000313|EMBL:ADB18891.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB18891.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB18891.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
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; CP001848; ADB18891.1; -; Genomic_DNA.
DR RefSeq; WP_012913150.1; NC_013720.1.
DR AlphaFoldDB; D2R442; -.
DR STRING; 530564.Psta_4243; -.
DR KEGG; psl:Psta_4243; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_0; -.
DR OrthoDB; 292158at2; -.
DR Proteomes; UP000001887; Chromosome.
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; -; 1.
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:SF336; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE, MITOCHONDRIAL; 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; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001887};
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 12..417
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 421 AA; 44520 MW; 7844874AA9DB84F1 CRC64;
MTAPACEQLP DSQRIVITGI GLTSPNGNNL TEFRAALLAG KSGVVQYEIR YVGDTLAGVC
SFDALRYQSK KDIRRGTRAG SVAIYACNES VRDAGIDLAA IDRSKVGIYL GVTEHGNVET
ENEIYALKGY DYDVTYWSHH HNPRTVANNP AGEAALNMGI TGPHYTIGAA CAAGNAGLVQ
GAQMLRLGDC DLALAGGVSE SIHTFGIFAS FKSQGALATH TDPTKASRPF DVARNGIVVA
EGGCVFTLER LSDAKARGAK IYAELAGYAI NTDATDFVLP NPERQAECVE LALKRAGLTA
SDIDIVSTHA TGTGQGDTQE CEALRKVFAS SNRTHFNNTK SFIGHAMGAA GALELAGNLP
SFVDGICHPT INVDELDPDC ALTTLVSGTP REIGKVRYIL NNSFGMLGIN SVVIVARYDD
K
//
