ID V6KVT6_STRNV Unreviewed; 1516 AA.
AC V6KVT6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Ketosynthase family 3 (KS3) domain-containing protein {ECO:0000259|PROSITE:PS52004};
GN ORFNames=M877_02325 {ECO:0000313|EMBL:EST33104.1};
OS Streptomyces niveus NCIMB 11891.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST33104.1, ECO:0000313|Proteomes:UP000017971};
RN [1] {ECO:0000313|EMBL:EST33104.1, ECO:0000313|Proteomes:UP000017971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST33104.1,
RC ECO:0000313|Proteomes:UP000017971};
RX PubMed=24407644;
RA Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT Aminocoumarin Antibiotic Novobiocin.";
RL Genome Announc. 2:e01146-e01113(2014).
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:EST33104.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWQW01000022; EST33104.1; -; Genomic_DNA.
DR STRING; 193462.BBN63_01870; -.
DR PATRIC; fig|1352941.4.peg.478; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_31_5_11; -.
DR Proteomes; UP000017971; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion 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; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 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; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR001227; Ac_transferase_dom_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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
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; PF01648; ACPS; 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; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..468
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1486..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1516 AA; 161714 MW; D524A4E47BCA984B CRC64;
MTSVDSRTPV AVVGMAVYFP GANDLESYWH NIVSGVDSIT EVPAGRWDEE FYAPGGPPRS
DRVYCRRGGF VDQSAEFDVT RFGIMPTSVA GTEPDQLIAL DVAHQSITDA GGDSVLPVDR
QRAGIVLGRG GYLTPGLVRL DQRVRTANQL VRTLRELAPE LGDDRLEEVR SAFAGQLGPE
QPESAIGLVP NLAASRVANR LDLRGPAYTV DAACASSLVA VDHAVRELAG GRCDVMLAGG
VHHCHDITLW SVFSQLGALS PSERIRPLHQ GADGVLIGEG TGIVVLKRLA DAERDGDRVY
AVVSGTGVAS DGRSASLFNP DPGGQVRAVR QAWDAAGLDP RAADAIGLLE AHGTATPAGD
RAELTTLAEV FGPAVGARAA IGSVKSMIGH TMPAAGIAGL IKAALALHHG VLPPTLHCED
PHPALEATRF TPLARSAPWE SPASGAPRRA GVNAFGFGGI NAHVVLEQAA SAPVGGRTTP
RTATTTVTEP ERVLRLAAPD HATLAALLDA DDRAVLAAGL DERAPADGPV RLGIVDPTAR
RLKLARKAVT KGAAWRGRSD VWFSPRPLLG PGGGTTAFVF PGLEAEFEAQ VDSLAERFGL
TWAPGHDARV GDVGRHGAAV FQLGRLLDTA LRRLSVVPDA LAGHSVGEWT AMACGGIHAA
DEVDTFLAGF DPDALRVPGA AFAVLGMPAD RVLAELAGRD DVVLSHDNAP NQSMICGPQD
AVGELVHRFR TQGVIGQVLP FRSGFHTPML APYLDPIRRA AETYTLHPQS TPVWSATTAA
LYPHDPAAVR ELFVRHLLEP VRFRQLITTM HDAGHRAFIQ LGAGQLGSLI DDTLAGKDRL
VVSAHSSARD ALAQLRRVVT ALWVEGAAPD AGPLLGSTPA ATGTRTSAAG GRPGVRLDLG
GALVSLPEQA KKLLADSIGH PPAPRLVGDG NALDRLDALG RAGAGFPIAA ELSALISDTA
AVADELIAAR ATYRTPAAPT PPPEPAVPAA LRVDVAEMPY LLDHCFFRQR PGWPDEADRW
PIVPATTVIG HLMEIAERVV PGTRAVAVHD VRLLKWIEAM PAVDVPVEVR QLGADRVEVS
LTGYSRAVVE LAAVHPAPPA AWPVDRAAER VPGLRAEQLY DERWMFHGPR FQGVSELSAI
GDRWVRGVLT TPEAPGALLD NVGQLLGYWI MATLTERTTV FPVRMEHIRF HGPHPRPGER
LTCLIRITEV TDLTLTADMQ LIGADGLVWA EFTGWQDRRF DTDANIRAVD RFPGENTLSE
ARPGGWAIVH ERWPDLATRE LIMRNMLGGA ERARYEGLPP VRRRQWLLGR IAAKDAVRRL
LWHEGAGELY PAEISVRNDA SGRPWAEGVH GRALGELTVS IAHRRETGVA VAARGTCGID
IEEITDRPRT TVETSCDTSE LTLLDALVAR SPGSGALWFT RFWAAKEAVA KARGTGLRGR
PAEYRVVAAD ANRARVVTGG RLYEVRLQET ANPPGLPERR YVVAWTTTED TAQTDPTDQT
DRTDETDRTD LTGDSA
//
