ID G2NJK2_STREK Unreviewed; 3603 AA.
AC G2NJK2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:AEN13367.1};
GN ORFNames=SACTE_5576 {ECO:0000313|EMBL:AEN13367.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN13367.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN13367.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN13367.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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; CP002993; AEN13367.1; -; Genomic_DNA.
DR RefSeq; WP_014049317.1; NC_015953.1.
DR STRING; 862751.SACTE_5576; -.
DR KEGG; ssx:SACTE_5576; -.
DR PATRIC; fig|862751.12.peg.5786; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_57_0_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000001397; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine 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 GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd08956; KR_3_FAS_SDR_x; 2.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 3.30.70.3290; -; 2.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 2.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 3.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00827; PKS_AT; 2.
DR SMART; SM00826; PKS_DH; 2.
DR SMART; SM00822; PKS_KR; 2.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 3.
DR SMART; SM01294; PKS_PP_betabranch; 2.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 4.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 2.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..102
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 119..545
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1738..1813
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1833..2259
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 3452..3527
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 544..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2808..2837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2810..2828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3603 AA; 375617 MW; 78DF194627CD880E CRC64;
MNGPGSESAL ARLLAQAAPT QHRRLVTDLV RTAVTEAVEA ARPGTSRTLD PAVPLAEQGL
DSLAAVDLHR RLTERTGLDL PVGLAYDCPT VRDLADRLLA GERVPDGTAP EPAGDGHSDE
PVAIVGIGCR FPGGIGTPAD LWRLLADGGE VLSDFPRDRG WDLEQLFDED PDAPGSSYAR
TGGFLDTATE FDADFFGISP RESLAMDPQQ RLVLETSWLA LEDAGIDPGT LRRTAAGMFF
GAEVQEYGPR LHDAPDGLDA HLLAGNASSV ISGRVAYVLG TEGPAVTVDT ACSASLVAVH
LARRSLQQGE SSLALAGGVA VMGGPGVFTA FSRQRGLSAD GRCKAFAAAA DGTGFAEGVG
VLVLERLSDA RRNGHRVLAV VRSSAVNQDG ASNGLTAPNG TAQQKLIRRA LAEAGLGPAD
VDVVEAHGTG TRLGDPIEAT ALLATYGQDR PADAPLLLGS VKSNLGHTQA AAGVAGVIKT
VLAMRHGRIP ATLHVDAPTP HAAWESGSVE LVTEPRPWPE TGRPRRAGVS SFGVSGTNAH
VILEQPEADD RDEVPDEAPS DTGEAHTAPV PLVFPLSARG EAALRARAAD LLPLADTTQP
ADLAHALATT RAALPDRAVL VAADRDELRE ALSAVASGSA PVPGRAGGEL GFLFTGQGSQ
RLGMGRELAA ALPAFADALD EVCGHFDLQL PQPLKSVLFA RPGTPDAELL HRTEYAQPAL
FAVEVALYRL LESWGVRPDH LAGHSVGEIA AAHVAGVLTL QDATILVAAR GRLMQGLPEG
GAMAAVRAAE SDVAPLLTER TGIAAVNGPA SVVISGDVDD VERIAGELAA RGHDTKRLRV
SHAFHSPLME PMLAEFRRVA RVLDYAEPTV PVVSTVTGAP VGAELCDPEY WVDHVRAQVR
FHDAVRWLAD AGVRTFLEIG PDAVLTAMGP DCTDAPGTAF LPVLRRGRPE VREAVTALAA
AHARGVPVDW ARHYAGQEAR RVELPGYPFQ RRRFWLEPGA PADATGLGQI TAGHPLLAAV
VAVGAEGVVL TGRLSTRTHP WLADHVIAGR VLLPGTAFVE LALRAGDHVG ATGLEELTLG
APLVLAPDEH VAVQVAVGEA DDTGRRTVSV HSRAGEDTPW TRHAAGVLTD AAPPAGGTDA
GVGTEAEAWP PPDAEPLDVT EVYADLADQG YAYGPVFQGL RAAWRHGEHI LAEVALPEDA
TADATRFRLH PALLDAALHA ADLDAPPRGE VLLPFAWTGV RLHATGATAL RVRITRGDGD
TVGLHLADTT GAPVADVEAM TSLPVPDTDV LYTVRWSPHP RPATTAPLRT TVLDGAAHPA
GPPHDGPGEE ALAAAVDALF GATAPDAVVY RPAGPAGADA AEARAHVLGT LRLLRIWQAD
ERAAATRLVV VTGPHSPAHA AVRGLVRSAQ AENPGRYVLL EHDGLPSEAE LRQALATGEP
ELSLAGGRFA VARLAAEPAA APRPAADWGT VLITGGTGGL GALLARHLVR THGVRRLVLA
GRRGHAPELH AELTALGAEV TVAACDVGDR EALRELLDRH PVDSVVHAAG TVRDGIVESL
TDGMVDEVFH AKAAGAWHLH ELTLDRDLSH FVLFSSLAAV LDGPGQGNYA AANAYLDALA
AHRAAHGLPA TALAWSLWAT GTGMGAALDA AALERVAAYG VPGLSAEHSL RLFDVAVRSG
GPHLVPVEID AAAVRRRPDG PPPLLSSLVR PVTRRAAAHA APQPERGMAQ LPAADRERAL
LELVRTEVAA VLRHDSPSAV DPGRAFTELG FDSLAAVELR NRLNTVTGLR LPATLVFDHP
TSRALADHIR DALFGTSRPA AEPVAGPRPA DESDPVVIVG MGCRYPGGVR SPEDLWRLVA
DGVDAVGDFP ADRGWDTDTL YDPEPGTPGR TYTREGAFLH DAADFDPGFF GIGPREATAM
DPQQRLLLEV SWEALERSAI DPAVLRGSRT GVFAGVMYHD YGTWLTEVPD DLAAYLGNGS
LGSVVSGRVA YALGLEGPAV TVDTACSSSL VTLHLAAQAL RQGECDLALV GGVTVMSTPD
TFVDFARQRG LAADGRCKSF AAAADGTGWG EGVGVLVVER LSDALRNGHR VLATVRGSAV
NQDGASNGLT APNGPSQQRV IRAALAAAGL TPADVDAVEA HGTGTTLGDP IEAQALLATY
GQERPDDAPL WLGSVKSNMG HTQAAAGVAG IIKMVMAMGH GTLPRTLHVD APSPQVDWTA
GAVRLLTDER PWHTPDRPRR AGISSFGISG TNAHVILEEF TGAEAEPAEP DPATVPPVSA
LPVSARSPEA LRGQAARLRE LTGTAPADLG LALATTRGTH PHRAVVLATD ERHTAEALEA
LARGHEAPGL LVTGTATDGT LAHLFSGQGA QRPGMGRDWY DTYPVYAEHF DRIAELFAKH
LERPLAEVVF GEHPDVLEQT AYTQAALFTT QVALHRLLES FGIRPAWLAG HSVGEFAAAH
VAGVWSLQDA VTAVAARGRL MQALPPGGAM ASVQASEEEV APLLDERCGI AAVNGPRAVV
VSGEEDAVAT VAAHFATTRR LRVSHAFHSP LMEPMLDEFR QVMAALPAAE PVLPIVSTLT
GVQATAAELG SADYWVRHVR QTVRFADAVG TLAAQGVDTF LELGAAPVLT ALGPDCVPDA
AETVFVPTAR KDTAQVPGLL AALAAVHTRG TDVDWAVLYE GYAGRRTELP TYAFEHRPYW
LPTAAARGDA AGHGLATADH PLVSARLDLP GDAGTLLTGR ISTATHPVLS QHAVLGSVLV
PGAALVDLAL HAGRLTGRPV LEELTLQAPL ALPGDEAVRL QVAARPDGSV EIHSRPENAP
EDEDWTRHAT GTLTGTGTDA PATTAQAGAW PPPGAVPLDT AGLYPRLHGE GYDYGPVFRG
VRTAWRLGDT VLAELELPDE ARQDAARHTL HPALLDSALH ATSLTDEGPG DDTPAGTIAL
PFAWTGVTAH GTGALAARVR VTRGEDGTRL DLTDTEGRPL ATVESYVTRP VDADRLTGRV
RSLYVTEGEP LPESAGRPDR RTWAVLGPDD AGLGAPAHPG LAAIGGPVPD VVVLPVRAPH
TEGEELPKAV RGTLDATLAT VQEWLGDERW AGSVLLVLTA GTLADAAVHG LVRAAQAEDP
GRIVLVGRAG PDSPVPDLAA LAAVLDSGEP EVLWRDGRAH APRLTRAAEP DTPRTKLPWG
TVLVTGGTGA LGALVARHLV TRHGVTRLLL VGRRGADAPG AAELARELAA LGARTDLVAC
DVADRTALAA LLEAHPVDSV VHTAGVLDDG LVTSLTPERL DTVLRPKADA AWHLHRLTLD
RGLSHFVLFS SAAGTVDASG QGNYAAANVF LDALAAHRAS HGLPATSLAW GLWAGGGMGA
GLDQGDAQRV ERSGIGALDP AEGLELFDAA LESGLPALVP VRLDTAALRR RGDDVPAVLR
TLAGVTARAA QDDRTRTLGE RLAGLPEADH AHTVLEAVRT EVAAVLGHDG PAAVAPRRAF
TELGFDSLAA VELRNRLNAV SGLRLPSTLI FDYATPTALA DHLLDRLAPD SGPEPADPRA
DDEVRDLIAR IPVARIREAG LLEGLLELSA PAPARAAAEQ PLDIKSMGVA DLVRAALNRS
SPE
//
