ID A0A0Q8ZG90_9ACTN Unreviewed; 1489 AA.
AC A0A0Q8ZG90;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KRD05433.1};
GN ORFNames=ASE41_32330 {ECO:0000313|EMBL:KRD05433.1};
OS Streptomyces sp. Root264.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD05433.1, ECO:0000313|Proteomes:UP000051177};
RN [1] {ECO:0000313|EMBL:KRD05433.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD05433.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD05433.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD05433.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:KRD05433.1}.
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DR EMBL; LMIZ01000043; KRD05433.1; -; Genomic_DNA.
DR STRING; 1736503.ASE41_32330; -.
DR Proteomes; UP000051177; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.50.11460; -; 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; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 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; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF13602; ADH_zinc_N_2; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051177};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1329..1404
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1489 AA; 155410 MW; A23066E9B9C4C641 CRC64;
MFALEATEDE VLTLLEGIRD AGIAAVNGPR SVVVSGAEEP VARIAAALAA DGRRTTRLRV
SHAFHSPLMD PMLDAFREVA AGIAYEAPRM SVISNVTGNT AGAELQDPEY WVRHVREAVR
FADGVRRLAE HGVDRFLEVG PDGTLTAMAQ SCLPDAEGAL LVPSLRKDRA ERETLLHAVA
QAFTHGLPVD WPRLFDGAAA RTVQLPTYPF QRRRFWPGPP LLLGDVTSAG LGASSHPLLG
AAVELADGDT HVLTGRLALG SSPWLKDHAL TSTALFPATG FLDLALHAGA RTGCEQVAEL
TILAPLTLPA QGGVQVQVRV EAPDATGARP LTVHGRPDAA EAGTPWTLHA GGLLTAAEPA
AAPYDFTVWP PEHGTEVPLD GFYEAFADRG HLYGPLFQGL TRVWTRGEEV FAEVELPADA
APAADAFDLH PALLDAALHA VMFVPMKDAG RLPFSWSDVR LDAVGASALR LRMVQEGPEA
VGLALADPTG RPVGSVGSLT LRELTGDLAG STVGAPDRQG LYELDWQPVA AVNAVAPAAW
TIVGAEEAEA LAGALRAAGR TVRRVPGLDA LAGAGEVPDT VLYAVPVTAD VPGDAGGLVD
ATRATLAEAL AVVRQWADDP VFAHARLAVV TRDAVPAGPR PADPAQAAVW GLVRAARTEN
PGRFVLADTD GGDASAGALP AALGDAAFEL VVRDGTVAAP HIVPLAADRA LLPPAGTAAW
RLGVEHRGSL DGLRLEACPE VDAALAPNEV RISMRAAGVN FRDVLTALGM YPGDATAIGL
EGAGVVTGVG AEVTALAPGD RVMGMFAGAF GPVAVADARM VTRIPKGWSF AEAATVPIAY
LTAYYALVDL GGLEPGESVL VHAAAGGVGS AAVQLARHLG AEVYGTASPA KWDALRAAGL
DDAHTASSRD LGFEERLRNA TDGRGFDVVL DSLAREFVDA SLRLLPRGGR FLEMGKTDVR
DTGQIAADHP GVVYRAFDLI EAGPDRIGEI LTDLADLFGR GVLRPLPMAV WDVRRAPDAF
RFVSQARHIG KVVLTLPAEL DPAGTVLLTG GLGGLGRITA RHLVAEHGVR HLLIAGRRGP
DAPGAAELRD ELAQLGADVT VAACDVADRT ALAALLAGVP ADRALTAVIH TAGVLADGVL
SSMTPDRLDE ALRPKVDAVV ALHELTRDLD LARFVVFSSV AGTFGGAGQA NYSAANAFLD
AFAHRRRAQG LPAVSLAWGT WLPEAGMTGE LGDADRERHA RTGMAPLDAT TGMRLLDAAA
GTDRAALLPM DLDPAALREH HDVLPVLLRG LVRTPARRRA TAAGTAPVTA APQSLADRLA
PLPSADRDQL LLDVVAEQAA AVLGHGSAAD IDPEQTFQEL GFDSLTAVEL RNRLGAATGL
RLPATLVFDY PTALAQARYL LNELSLPEPP GTAQALLAEM DRLEGSLADA DMAGEDHEKV
TARLRELLSR WQGEPLVTAA VPAARDDELA DVETAGDLFD LIDRELGDA
//
