ID D9VVV5_9ACTN Unreviewed; 429 AA.
AC D9VVV5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 2 {ECO:0000313|EMBL:EFL17221.1};
GN ORFNames=SSNG_04473 {ECO:0000313|EMBL:EFL17221.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL17221.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL17221.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL17221.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) 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 ECO:0000256|RuleBase:RU003694}.
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DR EMBL; GG657750; EFL17221.1; -; Genomic_DNA.
DR RefSeq; WP_007266150.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VVV5; -.
DR STRING; 253839.SSNG_04473; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
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:SF322; POLYKETIDE BETA-KETOACYL SYNTHASE 2-RELATED; 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; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 5..427
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 429 AA; 44590 MW; 71BA1D52FE19E15E CRC64;
MSGIGRQVVI SGIGLLTALG EGGEANWKAI VDGRSGVRQI QAYDTSRLQT TLGAEIDGFD
PSRFATRRQL NTMNRGDQLG LAAASLALAD AGIDTGTELG LRTGLFLGGN KSMGRMDQLI
KGLRTVRRPD GTADMKALGE KADTIMPPLF FVEGLQPGAV FHISQTFGIR GANAFFAGTA
DAGATAIARA VRAIQRGDAD RIIAGGYEDA TSWWSMTHMD RMGVLTTRND LGETAFRPYD
QTRSGAVLGE GGALLVLEEK EAALARGARI YAELRGVGNG HDGRTPPATD PEGRGLVRAV
RRALDDARLN PADLGYIASH GAATKIGDRS ETAALRTALG DASRSVPISS IKPQTGHLVG
GAGALNVAVS ALALHYGAVP ATANLETPDA ACDMDLVRGE ARDTRPDTAL ALARGLEGQA
VALALGRAA
//