ID A0A0F0HEJ8_9ACTN Unreviewed; 1605 AA.
AC A0A0F0HEJ8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KJK54079.1};
GN ORFNames=UK14_03480 {ECO:0000313|EMBL:KJK54079.1};
OS Streptomyces sp. NRRL F-4428.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609137 {ECO:0000313|EMBL:KJK54079.1, ECO:0000313|Proteomes:UP000033569};
RN [1] {ECO:0000313|EMBL:KJK54079.1, ECO:0000313|Proteomes:UP000033569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4428 {ECO:0000313|EMBL:KJK54079.1,
RC ECO:0000313|Proteomes:UP000033569};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KJK54079.1}.
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DR EMBL; JYJI01000015; KJK54079.1; -; Genomic_DNA.
DR RefSeq; WP_045320941.1; NZ_JYJI01000015.1.
DR PATRIC; fig|1609137.3.peg.4212; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000033569; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06454; KBL_like; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
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; IPR009081; PP-bd_ACP.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000033569};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..457
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1074..1149
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 949..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1056
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 167841 MW; 10CECF678221BB4A CRC64;
MNDIAIVGLG CRFPGARDIR AYWKLLMGGE RQFSAVPADR WNHDPFYDPG NPSAPHTAYT
DQVAFLDDVD RFDALHYGVP PARARAMDPQ HRLMLDVTRE ALDDAGLGRG DFDRENTGVF
CAMSVSDYKD VMTAPIRAIA LADQARRSAS DDGLGALDAV REHAGRLGTV QPFSLPGSLL
NMAAGTASRQ FDLGGPSFAV DAACSGSLVA LDQAVAQLRQ GRCRIAVVGG VYVNLTPDSL
IGFSTLRALS ATGVCRPFDE EADGFVLGEG AGAVVVRPLR DALAAGDRVY AVIKGVGSAN
DGASPGPLAP APEGQLRALR RAYDDAGVSP SSVGFLEAHG TATRSGDRAE VEALRRLRTE
WPDEDPSLCY LGAGKALIGH SLAAAGMAGL IKTALVVHHR TIVPQPGTRP HPDLGVGAAG
LRFAETARPW PRTGGPRRAA VSSFGFGGTN VHVVLEAAPA PAAGARTAAP AAPPATAGGA
GGSGGTPQVL LLSAGDAQLL DLHIGEVLDA VERAPGTPVG ALAHTLGGRA PLKARLAIVA
RDTYEFARRL RRARARLADG ARGDLGEGAY AEDAPMPAAR RRIAFVFPGQ GSQRPGMMRD
LYEGFAGYRA AFDALGSVAR GEADLDLAEL LYGGPAAADG HGEVDGGRGG ERGRRLADTE
VCQPLLGTVQ IAATRLLAAC GVTPDLALGH SAGEFAAAAA AGALTAEEAV RLLAQRGEAL
RRAESGLRGG MVAVQTDWET CRQLTVGIDD VWPACFNQPR QVVVSGTRQG LDALRRACAE
AGVVTVRLEV SHAFHSPRLA SAEEAVRAAL AERRVSAPVL PFVSSVNAEP CSDPAQLREL
WARHASVPVR FGEAVRASYD AGARLFLQVS GGRTLLDPVR RNLADRADVH VVAASGTAPD
GGRDFVRALA RLAVLGVPVD PRALVPAEDR MLVDLPVARL AAQSYWAGRP TPAHEAPAQE
APAQEATAEV PAQEGQAHEA PANKVTAQEG RAHAAPAPDV PAHEAPADPV LHPMDDLRQM
VRRQVDLMSR LSAAESAAPP TGPAVAEPPA AAEPSVPPVS AVPEAAPAVA GDVREVTEAV
YAHIARISAF PVGHLRHEQL LVDDLGFDSL MLTDLFTALR RQWPLWTFDE QAADRPTVGG
VAAAVADAAG DPAPGPVPQQ RAAGGVPRGP AVPEPAPEPA PERVLKPAPE PVPQPAALPE
QHTRIDRFPE VTAHAERFGT LSAAGLSNPY FLVHEGGMSD TTVVEGRRLL SFSGYNYLGL
ATHPRVTEAA REAVAAYGTS VSASRLLSGS RPLHLELEAE LADLLGCEAA LTLANGHATN
VTVIGHLLGP GDLVVHDALA HDSILQGCRL SGATRRPFPH NDAAALDALL HRVRGQFRRV
LVVVEGVYSM DGDIADLPAL VEAKRRHGAL LMVDEAHSLG TTGATGAGVG EVFGIDREAV
DLWSGTLSKA LAGCGGYVAA NRAVVEYLRY TAPGFVYSAG MTPADTAACL ASLRLLREEP
ERVARLAENA ALFLRLAREA GVDTGDSHGT PVVPCIVGDS LKALRLAEAL FRRGVSVNPI
LHPAVPEEMA RLRFFITRDH SSGQIRHTVA ALAQELGRLD AVRAA
//
