ID A0A0X3UVE0_9ACTN Unreviewed; 1115 AA.
AC A0A0X3UVE0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KUL36097.1};
GN ORFNames=ADL22_25605 {ECO:0000313|EMBL:KUL36097.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL36097.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL36097.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL36097.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL36097.1}.
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DR EMBL; LLZI01000253; KUL36097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X3UVE0; -.
DR STRING; 1609095.ADL22_25605; -.
DR Proteomes; UP000053256; 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:0009058; P:biosynthetic process; IEA:InterPro.
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; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
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; 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; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000053256};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..439
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 529..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..703
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 116749 MW; 0DAA1F33CD0C150B CRC64;
MACRFPGARH VTAYWRLLTA PEPQFAPVPD TRWRRAAFLT DSFRDTAAAY TDTMALLPDV
DRFDAAHYGI PPRRARSMDP QARLLVDLAR EAIQDAGWEA GGFDREETSV ITALTESGYR
ELSTLRVRMR QLAGGEFGAR AADPGWAEMV RGVDGLHGTS VAGLLLNMGP NTISSVFDLH
GESYALDSAC SGGLMAVANA VHALRAGRCR IALAGGAQLT LTPDLLVGLC RIGALSRSGR
CLPFGADADG FVLGEGAGVL ALRPLSDALA AGDRVYAVIR GVGTANDGTV QGGLHPQEAG
QLRALRRAYR DAGLPPDAVD YLEAHGTGTP VGDPVELAAL RALRGERAAP AYVGAVKAVV
GHALNAAGIA GLIKTVLAVH RGVIPPQPAY APADRAALDA AGLTVPAAPV RWPASGRPRR
AGVSAFGFGG TGVHLVVESY EPEPVTGPDP AARPAVEAGP YRLVLSARDR AGLARYAREV
ADTLAADRPP LAAVAATLAG RAPLEERLSV LAGDTDDALA RLTEAASAVE AGDAPEIGPD
ADSDGGPGAG PAHPPVPPPG GRIPPCTLPP SPLAPRRHWA VDEAAREAGD PPPAPATRED
APAPTPAATA SAAALVREEV ARTGVYPPAD IDEAMTLTTD LGFDSLMLQE LEVGIGKRAP
GFRTDEMFAP GLTVARLTAL VGAHLTEPPA PGAPLPPEAA PYTATPQNPA DPYAGTARID
DFPEVRDFEE RLRAVAGSGA EFPYFRVHQG TLRDTTEIGG RPYLSFGSYN YLGLSGHPAV
NEAVHRAVER YGSSVSASRV LSGERDLTVR LERALADFLG VEDCLALVSG HATNVTAIGH
LVGAGDLVLH DSLAHDSILQ GCALSGAARR PFAHNDTGQL EYLLRRNRPR FRRVLIAAEG
AYSMDGDLLD LPAVIELKKR YGALLMVDEA HSIGTVGERG RGVGEFFGTD RSDVDVWMGT
LSKSLASCGG YLGGSARMVR WLRHTLPGFV YSVGLSPANA AAALAATELI TAEPHRVRTL
RRNAGLFLRL ASEAGLATGA SAHTPIVPCL LGDSARTLRV ADRLFRRGVT ADPIFHPAVA
EGLARLRFFV TSEHREEDIR RAVAILAEEV AAAGG
//
