ID Q93NW8_9ACTN Unreviewed; 1412 AA.
AC Q93NW8;
DT 01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Acyl transferase domain-containing protein/acyl carrier protein {ECO:0000313|EMBL:MBB4789911.1};
DE SubName: Full=AmphA {ECO:0000313|EMBL:AAK73512.1, ECO:0000313|EMBL:AJE44523.1};
DE SubName: Full=Type I polyketide synthase {ECO:0000313|EMBL:QEV37643.1};
GN Name=amphA {ECO:0000313|EMBL:AAK73512.1};
GN ORFNames=BJY54_000523 {ECO:0000313|EMBL:MBB4789911.1}, CP978_03005
GN {ECO:0000313|EMBL:QEV37643.1}, SNOD_02605
GN {ECO:0000313|EMBL:AJE44523.1};
OS Streptomyces nodosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=40318 {ECO:0000313|EMBL:AAK73512.1};
RN [1] {ECO:0000313|EMBL:AAK73512.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11451671; DOI=10.1016/S1074-5521(01)00046-1;
RA Caffrey P., Lynch S., Flood E., Finnan S., Oliynyk M.;
RT "Amphotericin biosynthesis in Streptomyces nodosus: deductions from
RT analysis of polyketide synthase and late genes.";
RL Chem. Biol. 8:713-723(2001).
RN [2] {ECO:0000313|EMBL:AAK73512.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16079135; DOI=10.1074/jbc.M506689200;
RA Carmody M., Murphy B., Byrne B., Power P., Rai D., Rawlings B., Caffrey P.;
RT "Biosynthesis of amphotericin derivatives lacking exocyclic carboxyl
RT groups.";
RL J. Biol. Chem. 280:34420-34426(2005).
RN [3] {ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|Proteomes:UP000031526};
RA Sweeney P., Stephens N., Murphy C., Caffrey P.;
RT "Sequence of the Streptomyces nodosus genome.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AJE44523.1, ECO:0000313|Proteomes:UP000031526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:AJE44523.1,
RC ECO:0000313|Proteomes:UP000031526};
RX PubMed=26497174;
RA Sweeney P., Murphy C.D., Caffrey P.;
RT "Exploiting the genome sequence of Streptomyces nodosus for enhanced
RT antibiotic production.";
RL Appl. Microbiol. Biotechnol. 100:1285-1295(2016).
RN [5] {ECO:0000313|EMBL:QEV37643.1, ECO:0000313|Proteomes:UP000325763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14899 {ECO:0000313|EMBL:QEV37643.1,
RC ECO:0000313|Proteomes:UP000325763};
RA Lee N., Cho B.-K.;
RT "Streptomyces genome completion.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:MBB4789911.1, ECO:0000313|Proteomes:UP000544950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40109 {ECO:0000313|EMBL:MBB4789911.1,
RC ECO:0000313|Proteomes:UP000544950};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; AF357202; AAK73512.1; -; Genomic_DNA.
DR EMBL; CP009313; AJE44523.1; -; Genomic_DNA.
DR EMBL; JACHMR010000001; MBB4789911.1; -; Genomic_DNA.
DR EMBL; CP023747; QEV37643.1; -; Genomic_DNA.
DR RefSeq; WP_052453973.1; NZ_JACHMR010000001.1.
DR STRING; 40318.SNOD_02605; -.
DR KEGG; ag:AAK73512; -.
DR KEGG; snq:CP978_03005; -.
DR HOGENOM; CLU_000022_35_7_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000031526; Chromosome.
DR Proteomes; UP000325763; Chromosome.
DR Proteomes; UP000544950; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
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; 3.10.129.110; 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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
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; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 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; 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; 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.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031526};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:MBB4789911.1}.
FT DOMAIN 7..430
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1257..1332
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 435..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 146129 MW; 81349B6315B3F94D CRC64;
MTIGANDDPV VVVGMACRFP GGVEGPEDLW ELVRDGRDAT GPFPGDRGWD LAALTGDGPD
HSVTHRGGFL AAAADFDAGF FGMSPREAVS TDPQQRLVLE TSWEALEHAG IDPHTLRGTR
TGVFVGTNGQ DYATVTNASR EDLTGHALTG LSPSIASGRL AYFLGLEGPA VTLDTASSSS
LVALHYALRS LRSGECTTAL AGGVTVMSTP VGFIAYTRQG GLAADGRCKV FSDDADGTTW
AEGAGMIVLE RLSTARAAGH RVLAVLRGSA VNQDGASDGL TAPSGPAQER LVREALADAG
LGPADIDLVE AHGTGTRLGD PIEARALLAT YGQDRDGGQP LRLGSLKSNI GHAQAAAGIG
GLIKAVQALR HGLMPETLNL STPTRHVDWS AGAVELLTEA LPWPGTGRPR RAAVSSFGIS
GTNAHVIVEE APTTDPAAAV PAGPAHRDVA SAADSAARPA ALAGEPADTS APAAVDAGPA
DRPVTPAARL AALVPAADAV AWPVSGASPE ALDAQVERLT SFVRDHPGAD PLDIGHSLAT
GRAALRHRAV LVPSGDGVVE IARGEAAPRT TAVLFSGQGS QRLGMGRELA ARFPVFAKAL
DTVLAALDPQ LERPVRSVMW GEDPAELDRT GWTQPALFAF EVALYRLAES FGLRPDAVGG
HSVGEIAAAH IAGVLSLEDA ARLVAARATL MQALPEGGAM SAVEASEDEV LPLLDGDVSL
AAVNGPTAVV VSGAEDAVER VSAHFAAQGR RTSRLAVSHA FHSPLMEPML DAFRDVVAGL
TFHEPTLPVM SNLTGELAGA EIATPEYWVR HVRGTVRFAD GVTALREHGT DLLVELGPGS
VLTALARTVL GPDTPGAPVD VVPTLRKDQP EERALTAALG RLHVLGATVD WSALYTGTGA
RRTDLPTYAF QHARYWPAPG RPGTGTAGGG HPLLGPAVEL ADGGTVSGAT LSVATHPWLA
DHVVAGRVLL PAAVLVELAV RAGDDTGCDV LHELALVEAP VLEAGDTLDL QVRVGSADEA
GRRTLTVHSR PGNSPAEPWT QRAGGLLGTA PRTAAAPDTS FAVAWPPPGA EPLDLGDHYE
RLVDDGFDLG PAFRGLRTAW RHDGAFLAEV ELPAGTTDDP GAYGVHPALL DAARHAALTT
TGTLPVAWHG VRLHAVGATA LRVRIHSADD GALTLTAADV TGAPVFTAEA VVVRQLTEQE
RTAPRPLTRA WHQDTATPRR TRPVAAAPGA AAEPSASSAP DSFAAEAAAL APAERERRLI
GLVRTQAAAV LGHQGPDAVG PRAVFKELGF DSLAGVELSD RLTALTGLRL PATLVFNFPT
PELAARRIGE LLVVSGSSPQ GSCDDELTRF EAVVQTLSAD DPGRQAVADR LDALVASLRR
NSAPQENFSD EDIESVSVDR LLDIIDEEFE IS
//
