ID A0A1K1SEL8_9PSEU Unreviewed; 2306 AA.
AC A0A1K1SEL8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SFW82833.1};
GN ORFNames=SAMN04489730_5513 {ECO:0000313|EMBL:SFW82833.1};
OS Amycolatopsis australiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW82833.1, ECO:0000313|Proteomes:UP000182740};
RN [1] {ECO:0000313|EMBL:SFW82833.1, ECO:0000313|Proteomes:UP000182740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW82833.1,
RC ECO:0000313|Proteomes:UP000182740};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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DR EMBL; FPJG01000006; SFW82833.1; -; Genomic_DNA.
DR RefSeq; WP_072478985.1; NZ_FPJG01000006.1.
DR STRING; 546364.SAMN04489730_5513; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000182740; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
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; IPR013785; Aldolase_TIM.
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; IPR004136; NMO.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF03060; NMO; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFW82833.1}.
FT DOMAIN 634..1074
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1611..1694
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1799..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2306 AA; 236757 MW; 6D603BDEDFC495C5 CRC64;
MRVSKADRGS ADLVVAVSPL RWPSARGVAA AARGGGLGVL DLTGGAAGEE LALLGEWNVP
VFGVRLTRSA VDLPEAAATV LLTEDTPCTA RDFPGRRVLA EVGSAASAAR AVAGGAHGLI
ARGHECGGRT GDLSTFVLLQ ALLADETLDV PVWAAGGIGP HTAAAAVAGG AAGVVVDTQL
ALLPEAELPA RLTAGLTGLD GSETTVVDGV RVLARRGAEP VEAGQDVFLA ARFRDRWGTV
TAAVRGIADA VGEALRGETP VLGPGTAGSR ALGTALPIAQ GPMTRVSDQP AFAAEVAAAG
ALPFVALALS GPQQTRDVLE RTREAVGGAP WGVGVLGFAA EDVKAAQLAV IRELRPSHAI
IAGGRPAQAA ALEDAGIATF LHVPSPGLLK QFLEAGARKF VFEGAECGGH VGPRSSFPLW
EAQLGVLADF LAAAPDAAAD LQLLFAGGIH DARSAAMVAA LAAPVAARGA AAGVLMGTAY
LFTREAVGAG AVLPGFQRQL LAARHTDLLE TAPGHATRCV RSPFTEEYAA LKAQLAERGV
PSRDAWEQLE QLNVGRLRLA SKGVERVGDE LRDVGEDRQL AEGMFMAGEV AVLRSAVTTI
ADLHTAVGEG AAAFLRERAA AFGAVTPEPP APAPLDIAIV GMACMFPQAP DLATFWANVL
AGTDAVTEVP PQRWDTALYY DPEGQGERTP SRWGGFLPEI GFDPLRYGIP PSSLASIEPV
QLLALEAAHR ALADAGYAGR AFDRARTSVV FGAEAGSDLS NAMTLRTVLP SYVGELPSEL
DERLPRITED SFPGVLANVI AGRIANRLDL GGANYTVDAA CASSLTAVDV ACKELAAGTS
DLVLCGGADL HNGINDYLLF ASAHALSPTG RSATFDSAAD GIALGEGVAC VALKRLADAE
RDGDRVYAVI KGVGAASDGR ALGLTAPRPE GQHTALTRAY RNAGVSPARV GLVEAHGTGT
VVGDRTELAT LTKVFTEAGA APGGCTIGSV KSQIGHTKCA AGLAGLIKTA LALHTGVKPP
TLHLSAPNPA WDPATSPFVF QSAAQPWAAP PAERIAGVSA FGFGGTNFHV VLGAYDGGLP
PAQAGDEWPA ELFTFTTESA ARALLALASE VPAGHEPWRL RDLALSASRR TEAAGGRVRL
AVVASTVDDL VTVLRKALAG EPAPGVYLAG EDEPGEVAVL FPGQGSQRPG MFAELFVTFP
ELQRFLRLDP PTADVVFGPA VFGEAARQAA AGRVTDTRVA QPALGLAGLA AFRLLSRAGV
RPAMLGGHSY GELTALAAAG ALTPEALLHA SHARAGAIVD AIPDGDPGAM AAVSASAAEV
RAVLTGSGVV LANHNSPRQT VISGPTPDVE AAVTQLRAAG LGTKRIPVAC AFHSPLVAPA
GEAFGRALEA IGVVRTAVPV YGNRTAGPYP DDPDGIRDEL AAQLGAPVRF VEQVEAMYAA
GARVFVEAGP GTVLAGQVDA ILGDRPHRTV GFERGRRGLP GFLDALAELA VAGVPVETGW
LFRGRDAVDA ATASRPKRPG WTVDGHLLRA ADGTIPAGAL RPAERVSLGV TAEAPTSEAM
VADFLRTSRE MIAAQRDVLL GFLGAPAGPE RPNAALVASD APKAALVASD APNVALGRSV
LETVVGVIGE RTGYPVEMIE PDLDLEADLS VDSIKRAEIA GELASRLGLT GGDVEEFAKA
RTAAGIVELI GAERPNAALV ASDAPKAALV ASDAPNVALG RSVLETVVGV IGERTGYPVE
MIEPDLDLEA DLSVDSIKRA EIAGELTARL GAGEVEELAK ARTAAGIAEL LVAPTAASPA
PVERQPVDAG PGGLGGAGAA PEGHDPGRTG TGGVGAAPTG HVPNAEPRPV IVAPRRYLMA
ESALAPTPDP DVAGCRFLLL GTGSFAEAVR AELTSLGAHV ETGHDVRPGF DGYLHLPGND
PVLPAAFPLY QAALAGQPRW LLTAGPADGL RGFYRCVARE YPGTVARVVE GADARGFVAE
LSTADREPVV IRDGDARTGL KPVETDLGLL GRSGAGPAGD GVAEAAAIGL DRQSVVLLVG
GAKGITARFA ETLVGATRCR VELLGRTPVP PADDQYPHAK DAQDLRAALI ADGLKRPAEI
ERAVRRIQGE REVRATLRQL EALGSPVRYQ SVDVLDAEAV HRAVKEIHAE HGRLDGIVYA
AGVIEDKLVA EKAPESFARV YRTKVDGAGT LLEATADLPG EPKFVVLFGS IAAALGNRGQ
ADYAAANDAL EALGRRWPAG RAVTVHWGPW APTGEHDGMV TPELMRDYAR RGIELIDPEE
GTLGLLRELA WGRPDVCAVV HTASGW
//
