ID A0A0W0WS85_9GAMM Unreviewed; 1190 AA.
AC A0A0W0WS85;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Non-ribosomal peptide synthetase/polyketide synthetase {ECO:0000313|EMBL:KTD35187.1};
DE EC=5.1.1.11 {ECO:0000313|EMBL:KTD35187.1};
GN ORFNames=Lisr_0002 {ECO:0000313|EMBL:KTD35187.1};
OS Legionella israelensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=454 {ECO:0000313|EMBL:KTD35187.1, ECO:0000313|Proteomes:UP000054761};
RN [1] {ECO:0000313|EMBL:KTD35187.1, ECO:0000313|Proteomes:UP000054761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD35187.1,
RC ECO:0000313|Proteomes:UP000054761};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTD35187.1}.
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DR EMBL; LNYH01000001; KTD35187.1; -; Genomic_DNA.
DR RefSeq; WP_058500399.1; NZ_UGOE01000002.1.
DR AlphaFoldDB; A0A0W0WS85; -.
DR STRING; 454.Lisr_0002; -.
DR PATRIC; fig|454.4.peg.2; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000054761; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0047462; F:phenylalanine racemase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR049490; C883_1060-like_KR_N.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:KTD35187.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054761};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..428
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1104..1179
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1190 AA; 133266 MW; 2BBCC76A67BE27D2 CRC64;
METENKIAII GYNCQVAGAD DPQAFYEIVS QNKSGLSRSS PEDQSNFLDE AIYQDSNFIN
VGGGPKDFQC FDARFFGYSP KEAELLDPQI RKALECAYHT VEAAGYAPES LKGDTSCYVA
SSVNSYFNDN LKGHYQTGNE STKSHLIFLN EPDFLSTRIA YHFNWQGASF SVKSGCSGSM
LAIHEACKSL LHFECDNALA GGVNIKTLSQ FGYIYEQDGI LAADGRCCPF SEDATGTVFA
NGIGFVLLKR LEDAINDGDT IHAAIIASYA NNDGKDKVGY MAPSVSGQLK AMETALAYAD
IQPQQVSYIE SHGTGTYVGD PIEYKGLQKV YNDCPPQSIA LRSVKANIGH TDCASGVTAL
IKVLEDLKHQ TISPNHNFTK VNEKCDLSNS PFYFNTSLQP WEPIEGRRIA AISSFGIGGT
NVQLIIEEFI QEPSKMNVPQ NKALVFAAKS PAALEKRIQK CVEMLQKNPD LNLHDLSATL
LLGQNNFEYR FGIVASHVQE AIDKLSVFNY PSEAKQVNLK TPSTLNQEIF ENPQAVLKNY
LSGAVYTLDR ENPIPFRHVP LPKYPFEKEC FWVDQNENKN QKIQDISRWF YLPYWQRRQS
PLPPLKEYKK TILLFENEAT LVKEYKQELE VLGATIITVN AAESFSQSSE INFRLNPRKK
EDYEHLFTRL KSQSLMPETM IHCWSLSNED KDQESCLDKG LYSLLYTIQS LEATSMTFPR
LVQIITNHTA NVSGNEIVIP INAMMQSMSQ VLPKEYDDLA CQLIDVDNLN SKQILPALME
ELHRKENAEL ALRGKSRFIK AYQPTRIDDN TIGKISIAKG KNYLVIGGLG NFGIELAEFI
GGQHQGQVFL TTRMQFPNRA EWQTWQLQKP NHAITEKINL ITNIEKQGIQ IEILTADVLD
ITSLQNVKKH IENQYGPLSG VVHAAGVVDS GMIRHKTVNS LEQVFAPKVI GTNNVCSTFL
NHSLDFLILC SSMNSIIGGL GQLDNTAANA YIDAYAEHCL NRGFNNVLAI NWGAVNEARA
RNYSAQVQFA KLSEEHIKNK MEKSEIFEVY RRLFSSQLGP RVVVSTIDFN QVIENWSRVG
SLQSLISTKA QQKQKRTLDP YLTEPDSDME KSIARTWEDL LGIDKVVLED DFFTLGGNSL
IAIQFISELT KNYPIKMHAM AIYEYPTLAA FAKYVERLVK DAEDKQALMV
//
