UniProt: A0A1H4XX17

Database: UniProt
Entry: A0A1H4XX17_9PSEU

LinkDB:  A0A1H4XX17_9PSEU 
Original site:  A0A1H4XX17_9PSEU

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Ontology (4)   
   GO (4)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (42)   
   InterPro (23)   
   Pfam (9)   
   PROSITE (4)   
   SMART (6)   
All databases (47)   

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ID   A0A1H4XX17_9PSEU        Unreviewed;      1990 AA.
AC   A0A1H4XX17;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SED10077.1};
GN   ORFNames=SAMN04489727_6410 {ECO:0000313|EMBL:SED10077.1};
OS   Amycolatopsis tolypomycina.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=208445 {ECO:0000313|EMBL:SED10077.1, ECO:0000313|Proteomes:UP000199622};
RN   [1] {ECO:0000313|EMBL:SED10077.1, ECO:0000313|Proteomes:UP000199622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44544 {ECO:0000313|EMBL:SED10077.1,
RC   ECO:0000313|Proteomes:UP000199622};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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DR   EMBL; FNSO01000004; SED10077.1; -; Genomic_DNA.
DR   STRING; 208445.SAMN04489727_6410; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000199622; 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd08956; KR_3_FAS_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; 3.40.50.1820; alpha/beta hydrolase; 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   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; 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; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
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; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SED10077.1}.
FT   DOMAIN          33..461
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1629..1704
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1990 AA;  207280 MW;  DBA0650AD6E0EABD CRC64;
     MAEQDQLRTY LKRAVTEARD ARRKQRELEE RAREPIAIIG TACRFPGGAE SPERLWRLVA
     DGVDAVGEFP ADRGWDLGGL FDPDPDHPGT STTAAGAFLP GAAEFDAGFF GISPREALAT
     DPQHRLLLET AWEAVERARI DPASLRGTRT GVFAGVIYTE YGARVWNGRA PEGLEGFLGT
     GSAGGVASGR IAYTLGLEGP AITVDTACSS ALVALHLASE SLRRGECTLA LAGGVTVLAT
     PAAFLEFSRQ RGLAPDGRCK PFAAAADGTG WAEGAGILLL ERLSEARRRG HPVLAVIRGS
     AVNSDGASSG LTAPNGPAQQ RVIRAALANA GLSASDVDAV EAHGTGTKLG DPIEAQALLA
     TYGRDRPGDR PLWLGSVKSN IGHTQAAAGV AGVIKMVEAL RRGVLPRTLH VDEPTPQVDW
     TAGAVRLLTE AVAWPETGRP RRAGVSAFGL SGTNAHVIVE QVPADEEPAP GPETGVVPWV
     LSGRTAQAVR DQAARLASFV AERPELSVVD VARSLAVTRS RFGYRAVAAG ADRTALLDAL
     ARAQAEPAAE GKVAFLFSGQ GAQRAGMGRA LYDRFPVYAE AFDAVCARFP LPVREVVFED
     AEALDRTEYA QPALFAVEVA LFRLLESWGL LPDALAGHSI GEIAAAHAAG VLSLDDAATL
     VAARGALMQA LPAGGAMTAV EAAEAEVRPH LGDTTGIAAV NGPRAVVVSG ARADVERIAE
     TFARQGRRTK ALAVSHAFHS PLMEPMLAEF RRVVEGLTFA QPRIPVHSTV SRAADMSTVD
     YWVTHVRATV RFADAVEQLR TAGVTTCLEL GPGGVLSGMG PACTGDIRFV PGLRDGRPEP
     ETLFGALTTL APDWAAVVAE GRTVDLPTYA FQREHFWLRE PPRAGDVEAA GLTAIGHPLL
     TACVPVPSTG ELVLTGRLPA AAGSWPADHE VLGKRLLPGA AVVELVLRAA EEAGCGQLEE
     LTLEAPLVLP DEATRVQVVL GAPEPSGRRT VGVHAQTGEG PWTRHATGSV VVAAGEEPGE
     APDWPPAGEE LSVPELHDDL AAAGLGYGPA FQGLDAAWRA GEEVFAEVTL PVDADGFGIH
     PALLDAALHA AARLASAAEP GVPRLPFAWS GVRLHAVGAT SLRVRLAPAG GEAFSLVAWD
     PAGRPVLTVE SLVLRPAGGL GDRPRAGELL RVDWPRLPLA AAEQAAWPVV GPAPEHVTVS
     AKYGDPAELG RALDAGAAVP PVVLATVPAG GTGTGTVRAA DVRDAVQRTL ALARSWVEDA
     RFDGSKLVLV TGNAVATPAP DLVQAPLWGL LRSAQAEHPD RFVLVDSDAT EASAEALAGA
     VATGEPQLVL RDGVARVPRL TAAVPGAGPV AFDRDGTVLL TGGSGDLARV LARHLVRGHG
     VRHLLLAARR PERAADLAAE LTGAGADVTV AACDVADREA VRALLAGVPA AHPLSAVLHT
     AGVLDDGVLT SLRPGQLDAV LRPKVDGGLV LDELTRDLGL AAFVLFSSAA GQVGAPGQAG
     YAAANAFADA LARRRRADGL PATALAWGLW QQDDGMAGGL GAADRNRMAR AGVVALSEED
     GLRLFDAALA GEEAVVVPIG LDRAALRNSG ERVPALLRGL VRAPVRPAAK TAPDSAGAFA
     GLSEEDRRAR VLELVRQEAA VVLGHASADA ITAGQPFLEA GFDSLTAVEL RNRLAAATGT
     RLPVSVVFDL ATPAALAARL AGELAPGHPA APADAGDTVN ALYRQAWERR DIAAGNEFLR
     AAARLRPKYD DAAYLAELPP PVTLATGPAR PRLICIPTLA ASSSPLHYAR FAAELQGVRD
     VSVVYLPGYA DAREKLPASF DAMAGLLADS VERAAGAEPF ALVGYSAGGW LATAAALRLE
     DRGRTPAGVV LVDTYFFDAD LPLIEPTLAD EMFAREDFFG RIGHARLTGM GGHLNVLDTF
     TPRATKAPML FVRALDPLPS EADGVGPDHP IWRHEIPFAD ETVEVPGNHM NVMEQENARE
     VARVVDRWLA
//

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