UniProt: A0A291QMU3

Database: UniProt
Entry: A0A291QMU3_9ACTN

LinkDB:  A0A291QMU3_9ACTN 
Original site:  A0A291QMU3_9ACTN

All links

Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (49)   
   InterPro (27)   
   Pfam (11)   
   PROSITE (4)   
   SMART (7)   
All databases (58)   

Download RDF

ID   A0A291QMU3_9ACTN        Unreviewed;      2689 AA.
AC   A0A291QMU3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Malonyl CoA-acyl carrier protein transacylase {ECO:0000313|EMBL:ATL33041.1};
DE            EC=2.3.1.39 {ECO:0000313|EMBL:ATL33041.1};
GN   ORFNames=KY5_8023c {ECO:0000313|EMBL:ATL33041.1};
OS   Streptomyces formicae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL33041.1, ECO:0000313|Proteomes:UP000221011};
RN   [1] {ECO:0000313|EMBL:ATL33041.1, ECO:0000313|Proteomes:UP000221011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY5 {ECO:0000313|EMBL:ATL33041.1,
RC   ECO:0000313|Proteomes:UP000221011};
RA   Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT   "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT   producer.";
RL   Submitted (AUG-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   ---------------------------------------------------------------------------
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; CP022685; ATL33041.1; -; Genomic_DNA.
DR   KEGG; sfk:KY5_8023c; -.
DR   Proteomes; UP000221011; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
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; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
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; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
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; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
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; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 2.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000313|EMBL:ATL33041.1};
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:UP000221011};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ATL33041.1}.
FT   DOMAIN          536..611
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          634..1057
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2295..2370
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1621..1644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2183..2203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1621..1635
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2689 AA;  283617 MW;  E989EBD946A35F15 CRC64;
     MTRHELIRPV PELLKEHAER AAGRIAYADS SRRVTYAELE RRTRALAAHL TGTGLRRGDR
     VAILLGNCVE AVESCFAVVR AGMVGVPLNP RSSDAELTHF LQDSGAAFVI TDAAHLAQLR
     GLHAPFGHLG ALVTGAGPVP DGARLFEHAA AGERSAEIDR LGLDEPAWML YTSGTTHRPK
     GVLSTQRAAL WSVAACYAPL FGLSPEDRVC WPLPLFHSFS HSMAIMGVTA VGASAGLVGD
     PLSSGGLRQE LLTADEALGG PFTMMAGVPA TYHRLVESAG ARPRALRMCV VAGAPSGPAL
     HEAVEAALGA PLLDVYGSTE TCGVITANRP EGARVEGSSG PPVPGMDVRV VAPDSLTYVP
     DGAEGEVWVR GPSLMTKYHE RPEATAAALR EGWYRTGDLG RIGEHGHLLL TGRLSELIIR
     GGENIHPTEI EQVLTECPGV SDAVVVGLPH EVLGEVPVAF VVPGPDGLDA RRVLAECRAL
     LADYKVPTGI HEIDAVPRTA SGKIARHRLV VPAPAPSAGA SPHERLLALP RDERERALRE
     TVLTCTAEVC GFEQEELPDA DSPFADLGMT SLGAVELVDR LGALTGLRLP STLVFDHPTP
     AEAARHLLAT LFADEPTERR PRASGGQGRS EVDDDPVVIV AMGCRYPGDV NSPEDLWELV
     THGRDAISEF PTDRGWDLAA LYDPDPDRIG TSYTRHGGFL HRAAEFDAGL FGISPREALA
     TDPQQRLLLE TSWEVWERAG IDPASLRESD TGVFVGQMYT DYASRFTRRH ELEAQLGLGS
     AGSVTSGRIS YVYGLRGPAI TLDTACSSSL VALHLAAGAL RSGECSLALA GGVTVMATPH
     PFLAFSRQRG LAPDGRCKSF SAHADGTAWA EGVGLVLLER LSDARRNGRQ VLAVLRGSAV
     NSDGASNGLT APHGPAQRRL ITRALADAGL RAADVDAVEA HGTGTRLGDP IEAQAILATY
     GQGRERPLWL GSVKSNLGHT QAAAGVAGVI KMVQAMRHGE LPRTLHADSP TPHVDWPSGR
     VELLTAARPW PEPGRPRRAG VSAFGIGGTN AHVILEEAPD DRAEIPRRAS STWSAPWLLS
     AADAPALRAQ ARRLASHVAD GTRVLTADVA RSLTVSRSAL AHRALVPADD DPTRMLDALG
     ALAEGRDAPG VVRGLAAPQL RTALLFTGQG AQRPRMGAEL RAAFPVFAEA FDEVCRHLDD
     HLPHPLSSVL AAEPGSPDAT LVDRTDFAQA GLFAFEVALF RLVESWGVRA DHLVGHSVGE
     LAAAHVAGVL DLPDAARLVA ARGRLMQGLP DGGAMVALDA PEDEVRFAIA ELEDDQVAIA
     SVNGPRSVVV SGAAGAVLAV ATAFEARGRR AVRLRVSHAF HSPLVEPMLD DFLRVAREVT
     FHLPRIPIVS TVTGRPADAA ELCSPEYWVR HARRPVRFAD AVRTLADDGV SAYLELGPGP
     VLTAAGTDCL ATPASDGGSV LAVATRGGEH EPETLLSAVS RLHVAGAAVD WASVYASSDA
     RHVDLPTYPF QRQRYWLDAP RTTAADAPPL LGPAFPVPGT ARTVLSGLLS LPTHPWLADH
     VVAGRVIVPA TVFVEMAVRA GDAVDRGTVD DLVILRPLAL PDASAVCVQV VVGGPDDAGR
     RPVDLYTRPE ESTEDTPWTR NVSGQLVRSR AAQDGARHEG LTPWPPQAAE AVDLTDAYAV
     LADAGLAYGP AFQGVDTVWR CGDDVLAEVR LPASHTSDAD RFGLHPALLD AALHAPLLAA
     PAELAALRVP FAWSGVSLHA SGATELRVRV TRTGTDTASL TLADPHGRIV ARVDSLTTRE
     LPPTAQTDST DDVVRHALLR PEWADAAFPE PSTGSAGHTW VVRGRDRLGL AGYLPCGKDP
     QFIVVAAVAR ATDSDTGRTD SDPLTDVHEM TDTVLETLRD WQGDPDTAGT RLVVVTRDAT
     APVPDLAGAA VWGLVRVAQS ELPGRVVLVD VDGRPESLSL VPDAVATGEP QLRVREGRVT
     VPRLGLVGDT TEGEATVFDP DGTVLITGGT GALGAELARH LVTAHGVRHL LLTGRRGPRA
     PGADELRGDL TRLGAQVDIV ACDAADRAAL AEAIKRCEPP LTGVVHAAGV LDDGVLESLT
     PERMAAVLRP KADAAWNLHE LTRDMGLSAF VVFSSVSGLL GPAGQGNYAA ANAFLDALAR
     RRTAEGLPTV SLAWGPWEHA DGMGAAPDAT ASLPDSGPSR QRPQARDVLV PLSTRQGLAL
     FDAALRSTEP VLAPILLDRG ALRSSAGLVP PLLRGLVRRN RPTAAATASD SDRNAEAPGA
     WRKRLNQLPV EARESALAEL LRADVASVLG YPGADALPEG KSLGELGFDS LTAVQIRNRL
     SMALTVRLPV AVVFEHRTAD GLAHHLLGLL EDEADADTTA GAATAAEEVH SVEQPAYTLS
     SLFRAVSAAG QPVAAMHLLV TASWAVPSFT AVQSAEHALP PIRRSHGRPG TDGPTVVYFP
     AFQPSFAPPG AGDFPRFHGA FHDDLDVLEF PYPGLGASAS TERAVPEDRA ALARTQAESV
     LRYAGNGPFV IVGRSAGGNV AHLVAQHLEN TGRAPAGLVL LDTYHITPDN NGTDWLLSLA
     APPTRSGDLW GNVSGDGDSV LAAMGAYHRI LLDWEPEPIT TPTLLVRASL PTPAMAAAAE
     AESWRTSWPS AHEVVDVPGD HLTMMREHAE STASAVRDWI RARTTGNHR
//

DBGET integrated database retrieval system