ID A0A2I0SAT6_9ACTN Unreviewed; 844 AA.
AC A0A2I0SAT6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:PKT67048.1};
DE Flags: Fragment;
GN ORFNames=CW362_42615 {ECO:0000313|EMBL:PKT67048.1};
OS Streptomyces populi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2058924 {ECO:0000313|EMBL:PKT67048.1, ECO:0000313|Proteomes:UP000236178};
RN [1] {ECO:0000313|EMBL:PKT67048.1, ECO:0000313|Proteomes:UP000236178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A249 {ECO:0000313|EMBL:PKT67048.1,
RC ECO:0000313|Proteomes:UP000236178};
RA Wang Z.;
RT "Streptomyces populusis sp. nov., a novel endophytic actinobacterium
RT isolated from stems of Populus adenopoda Maxim.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:PKT67048.1}.
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DR EMBL; PJOS01000238; PKT67048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0SAT6; -.
DR Proteomes; UP000236178; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.50.11460; -; 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; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
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; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000236178}.
FT DOMAIN 104..400
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT DOMAIN 464..627
FT /note="Polyketide synthase dehydratase"
FT /evidence="ECO:0000259|SMART:SM00826"
FT REGION 578..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKT67048.1"
FT NON_TER 844
FT /evidence="ECO:0000313|EMBL:PKT67048.1"
SQ SEQUENCE 844 AA; 89610 MW; A6D5A867558AF9C8 CRC64;
EQTPDVLRTP GLAGTEPWLL SAKSADALRE QARRLAALVR DDTTASPAEI GHALATTRSC
FEHRAAVVAT TREEFLTGLA ALADDTTAAG VVRGRARQGK VAFVFPGQGS QWHGMAAELL
ETSPVFAQRM TECAQALAPH TDWDLLEVVR GTDSGWLTRV DMVQPALFAV MVSLAQLWHS
HGVRPAAVIG HSQGEIAAAC VAGALSLKDA AKVVALRSRA LIALAGKGGM LSVALSADDL
APLLRRWQGS LWLAAVNGPQ ASVVSGDPAA LSELETHCRA QKVRTRTIPV DYASHSAHVE
EIRERLLAEL ADVTPRRARI TFCSTVTGAP LDTTGLDADY WYRNLRGTVL LETATRTLLE
QGYRTFIEAS PHPGLTIALQ DTIAEAAADA VALETLRRQD GGPHRFLTSL AQAHAHGVQV
EWDYAGAPRT ALPTYAFQRE RHWLDAPAPA AADAGSLGVG PLGHPLLKAA LPAATGGELV
LTGRLSARAQ PWLPDHQVAA RPVVPGTAVV EMALAAGAQA GCDTVDELTL RRPLVLPEDG
GLQLQLRITG PEPDLTRRAE LYARPDDAPA WTHHASAVLA PSPPAPDDGP GPLAAWPPPG
AQPVDTTGFY DALAERGYHY GPAFRALRGA WRSGEELFAE VALDAAHRTD AASYLLHPAL
LDAALHVIAV HDTTRLRLPF SWNGVRLRAT AATSLRVRIT PRTADSYAVE LADTQGTVGS
VEDLTLRTVD PRQLEAGHAG HALLRLDWTP LALPAAPAAP QTLAVLGPRP LLAHTPHYPD
LAAVPQDVTT VVADLTEPLP GPRPTAHRAL ALLQAWLADE RFGDARLVLL VGPAEDPAHA
PVWG
//