ID F0REQ9_CELLC Unreviewed; 384 AA.
AC F0REQ9;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I {ECO:0000313|EMBL:ADY28864.1};
DE EC=2.3.1.41 {ECO:0000313|EMBL:ADY28864.1};
GN OrderedLocusNames=Celly_1035 {ECO:0000313|EMBL:ADY28864.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY28864.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY28864.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
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; CP002534; ADY28864.1; -; Genomic_DNA.
DR RefSeq; WP_013620612.1; NC_015167.1.
DR AlphaFoldDB; F0REQ9; -.
DR STRING; 867900.Celly_1035; -.
DR KEGG; cly:Celly_1035; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_715488_0_0_10; -.
DR OrthoDB; 1141849at2; -.
DR Proteomes; UP000007487; 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:UniProt.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR007110; Ig-like_dom.
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; PS50835; IG_LIKE; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:ADY28864.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487};
KW Transferase {ECO:0000256|RuleBase:RU003694, ECO:0000313|EMBL:ADY28864.1}.
FT DOMAIN 1..382
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 127..222
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 384 AA; 41637 MW; 904791ACD0999776 CRC64;
MSIYITALAS ISPLGTSLNE VWESYKNDAH LLQEKNIGNQ KSWVAALSDE AKQEIETLKN
SDLKYKSLDD TVLFAMYASR KALEQAGWTS KDNFGVNFGS SRGATALFEK YHREFLEKDK
ASTLSSPTTT LGNISSWVAH DLQTQGPEIS HSITCSTALH SLLNGVAWVK SGMANKFLVG
GSEAPLTPFT IAQMKALKIY ARGADTYPCK AFDLAKDQNT MALGEGAAVI GIENGNKENA
LAEIIGVGYA TEVLKHNISI SSDAVCFQRS MKMALEGIDP DDVDVIVMHA PGTIKGDLSE
IEAIKKIFCN KIPALTTNKW KIGHSFGASG MLSIELAIAM LQKQEFIKVP FVDYTEIPKS
IKKVLINAVG FGGNAVSILL QKTF
//
