ID A0A1Q5CNL4_9ACTN Unreviewed; 1455 AA.
AC A0A1Q5CNL4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:OKI85200.1};
GN ORFNames=A6A27_15560 {ECO:0000313|EMBL:OKI85200.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI85200.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI85200.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI85200.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI85200.1}.
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DR EMBL; LWLS01000013; OKI85200.1; -; Genomic_DNA.
DR RefSeq; WP_073833228.1; NZ_LWLS01000013.1.
DR STRING; 1718947.A6A27_15560; -.
DR OrthoDB; 3406074at2; -.
DR Proteomes; UP000186700; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR049490; C883_1060-like_KR_N.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; PF00698; Acyl_transf_1; 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; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186700};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..433
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1358..1433
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1455 AA; 152114 MW; 9EF6CFEF4D3C4709 CRC64;
MTNETVEPIA IVGLSLRVPG ASSAEEFWRN LVDGTESFTR FSRAELLARG VSEDELDDPA
YVPVAAVLDQ FDCFDAGLFG MSPRDAELAD PQQRLFLEHA HAALLDAGCD PARYDGEIGV
YAGSNADLYQ WLNVRRNPQA LAGAGELRVS LGNKPDYLAS TVSFRLNLRG PAMTVQTACS
SSLVAIHLAS EALRNGECDT ALAGGVCVEL PHAVGYVADD GYTSADGHCR PFDAHANGTV
YGSGVGVVVL KRLSDALADG DDIRALIIGN AVNNDGMTKA SFTAPSVTGQ LEVVVQALAV
AGIAPRSVSY VEAHGTGTVL GDSIEIAALT AAYGRRTTER GWCGVGSTKA NIGHLSAAGG
VIGLIKTVLS MQHRLIPPNI NYDRPHPEID FDASPFYVVS TLTKWEPEEQ RPLRAGVSSL
GLGGTNAHLV LQEPPPPAPA APPDHDGGEL IQVSAATPAA LAAACAQVAT RLTDRPELQL
RDVAYTLREG RPVYPHRAAV VAVDRAQAAA ALADPKRRAS GDAATVPRVG LLFSGQGSQH
PGMGARLAAT EPIFAAAVDE CARILGWDPH ELIFSTTPGA DERLAEPPVL QPALFTVEYA
TAMLWRHWGV TPAAMIGHSI GELAAATVAG VFDLPDALRL AAARGRLVQA APQGRMLAVQ
RGADEISPLL PAGVAVAISN GPHTCVLAGA PEPVTAFADT LREHGVSCTL LRTPYAMHVP
LLDPVRDEFA ALVAAVPRRA PNLPVWSTAT AAPFTDGQIT DPAYWGEQLC RPVRFRATVA
GLAATGAADE WLLLECGPGR QLAGLARLSL PQGARAPLRT LPTPGEKLTD RQTAYEAAGR
LWTAGVPVRV PTPDKPRRVP LPGYPYQRTR HWIDPAPMAA PAEPAADRRY DDGIVEVPVW
HQLPATAPAE APAQLLLFAS GERGTALAAR LREHGTDVTV IRPGAAFAVR PGGYQLRATN
AADYQRLLDE CADDGRAARI VHAWALDGDP ADSDVDAVSA AQEHGYYALL TLLDALPAAA
GVQLDVVTAG VADVTGADLV RPEHATVAGV VRSVPLERPQ VCCHWVDADP GDPGVDAVVD
ELLGTERAEA VALRLGGRRW TREFAPVRPG GRTTSGLGIR DGGRYLITGG LGRVGGAFAA
ELARRGAQLV LVSRTAQPPL ATIEALEQAG ARVRHLTADV ANVAAMRAVR AEVLRDLGGL
DGIIHAAKLP DTGLSAGSRL AEAAAELRPK VTGTLVLREV FGDLPLDFVA LTSSVTALAG
GLGRADDTAA NAFLDAYARS PHGWPARLVS LAWGAWQEEG VPEHDGLPPA AAVAAGQRVL
AEGRTGSVAI GAYTVAAVAG HERRLGSAAA TVTSTVAAAD GDLTATIARI WGDVLGVTEV
SPHDNFFRLG GTSLVAAQLV LRIRQAVGAR LSMRVLFDAP TVAAMAARIE SLRGAPPAAD
AEAPIPRLRR PGQPA
//
