ID A0A3D9SHK5_9ACTN Unreviewed; 2262 AA.
AC A0A3D9SHK5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:REE95372.1};
GN ORFNames=DFJ69_0759 {ECO:0000313|EMBL:REE95372.1};
OS Thermomonospora umbrina.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=111806 {ECO:0000313|EMBL:REE95372.1, ECO:0000313|Proteomes:UP000256661};
RN [1] {ECO:0000313|EMBL:REE95372.1, ECO:0000313|Proteomes:UP000256661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43927 {ECO:0000313|EMBL:REE95372.1,
RC ECO:0000313|Proteomes:UP000256661};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:REE95372.1}.
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DR EMBL; QTTT01000001; REE95372.1; -; Genomic_DNA.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000256661; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0018580; F:nitronate monooxygenase activity; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; 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; 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; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 2.
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; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000256661};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:REE95372.1}.
FT DOMAIN 661..1102
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1632..1667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2262 AA; 236385 MW; F4754ECC69C7D0EE CRC64;
MAADVVGAHD GRGRDRIIGV TPFGRPVAGL AVAVARAGAL GALDLGHDRE AALAALELVT
RWWDGPFAVR IPAGCPVRPE ELPEAARTML VDAPALHHAQ PYMPGRRLLV EVVDADEAHA
AVRLGADGLI ARGCEAGGRV GELTTFVLLQ RLLGDPTVAR PVWAAGGVGP HTASAVVAGG
AEGVVLDAQL ALVRESDLPA DVAAAIAAMD GGETRVVAGH RVFTRPDLPV FHTADPREVE
ARLDALDLCT GLLPIGQEGA FARPLADRYK TAGGVVRAVR DRIDGHLDAA VRTAPLAPSQ
EGYPVFQGPM TRVSDRPAFA AVVAREGGVP FLALALMTGK ETRTLLTETA ERLGDRPWGV
GVLGFAPPEV RAAQLAAVQE ARPPYALIAG GRPAHAAPLE AAGIATFLHV PSPGLLERFL
AEGARRFVFE GSECGGHVGP RASLPLWEAQ VARLLEFTDE HPDAAEDMAV AFAGGVHDER
SAAMVAALAG PLADRGVRIR VLMGTAYLFT LEAVAAGAIM PGFQRAAVDC ERTVLLETSP
GHATRCAPTP YTDAFEQARQ DLTAAGASRR EIWAKLERLN LGRLRIASRG VRRENGDLVP
VDGDHQRREG LFMIGQVAGL RSSATTVAAL HEQVTMGATR FLTERADELG LETPGEAVPE
PVDIAVVGMD CVFPGARDAA RYWANVVGGV DAVTEVPADR WNPDVYWEPG AHTPGKTPSK
WGGFLPDVPF DALAHGIPPN SLGSIDPVQL LALEVASRAL ADAGYAERPF DRSRTAVFFG
AEAGTDLSTA YGTRALLPQY YGQVPPALDG RLPTLTEDSF PGLLANVIAG RIANRLDLGG
ANYTVNAACA ASLAALDAAC KELVSGAADM VLCGAADLHN SVHDYLLFAS VRALSPTGRC
APFDAKADGI ALGEGVACVV LKRLADAERD GDRIYAVVKS VAGASDGRSL GLTAPRAEGQ
RLALERAYRK AGVSPAQVGL VEAHGTGTVV GDRTELATLT ETFTAAGARP GRAVLGSVKS
QIGHTKCAAG LAGLIKAAYA LHTGIRPGTL HLRDPNPAWD ADDSPFAFAR TALPWAAGPG
ERYAGVSGFG FGGANFHAVL AGYDGAPEPV SGVSAWPAEL FLIRGADRAE ARAELDRLGA
LLDTRGPEVR LRDLARTVAG REERHAAGRA PVQVAIVATG PADLAAKIRQ AREFRAGAGV
FPAREGERGK IAFLFPGQGS QRPGMLADLF VAFPRLQRLL RLGDDRYAEA MYPPAAFTDE
VRRRQRAALT DTRIAQPALG IVGIAVHRLL TELGVRPDMA AGHSYGELVA LCAAGVFGET
DLVDLSAARA EAILRAVRDA GQGDPGTMAA VAGTLEEVRA AIDPLPDVVV AGHNAPRQVM
VSGPTEAVAN AVEALAARGL AAERIPVACA FHSPMATGAA LTLGVELARL RLYAPAFPVW
SNATAEPYDG TAERLGATLA DQVIAPVRFT EQIEAMYAAG ARVFVEAGPG RVLSRLVGRI
LGDRPHTVIA CDRSADGSAR GRGPAALQGL QGLLLALAEL AAAGAEVDAL PLFTGRDAVP
LSADAPDRPG WIVNGHLVRT ADGRYPDNGL RPAARIEEPG ISEDRDAAVL EFLRTSRELA
AAQRDVVLGY LGAPVPQPRQ DPHPKSPAPR VPPPRPRPSG DAPRPVRAAV TVPRTASEGG
IRAQVLAVIS ARTGYPQEML GSGLDLEADL SIDSIKRTEI IGDLADRVGL TAPGARVDEP
VVERLARIKT IDEMVTWLDG HLDERRGDAP TEGASSDGPS TEPMPAVAEP GPPRRHVVHL
VKAPALPTPP DDVLSGLSCL IVDDGRGIAP ALCALLERRG AKATTAAETD AHADVLIHLA
ALRPDCSPVL PDLYAGVRDA LLGGTTRLLF ATGSGGTFGH RYTDDGVGDP TAGAGLRGLA
RTLALEYPDV LVRAVDVDPD DAPTALAARL LNEVAAEPAA GPVVVGYEGE TRHTLDVMPE
ALLSDARLPL RPDGVVLLTG GARGITARIA HALAATTGCH IELAGRTPEP QGPEDPALAD
ARDATALRRA LALAGGREPV EIEAAVRRVL AEREIRATLA ALDGGAASVR YHSLDVRDAR
AVNALVEDVY ARHGRLDGVV HGAGVVEDRL VRDKDPDAFA RVYRTKVDGA RALAAAVRPD
LAFFVVLGSV SGVLGNRGQA DYAAANDACD TLVRVWRTRL RGRVLVADWG PWAGGGMVTP
DLAREYARRG LPLIDPDAAV RALLREIAGG VDPQVVFTGA AP
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