ID A0A0Q2UJK6_MYCGO Unreviewed; 2101 AA.
AC A0A0Q2UJK6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KQH80928.1};
GN ORFNames=AO501_29400 {ECO:0000313|EMBL:KQH80928.1};
OS Mycobacterium gordonae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778 {ECO:0000313|EMBL:KQH80928.1, ECO:0000313|Proteomes:UP000051677};
RN [1] {ECO:0000313|EMBL:KQH80928.1, ECO:0000313|Proteomes:UP000051677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CTRI 14-8773 {ECO:0000313|EMBL:KQH80928.1,
RC ECO:0000313|Proteomes:UP000051677};
RA Ustinova V., Smirnova T., Blagodatskikh K., Varlamov D., Larionova E.,
RA Chernousova L.;
RT "Mycobacterium gordonae draft genome assembly.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQH80928.1}.
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; LKTM01000002; KQH80928.1; -; Genomic_DNA.
DR RefSeq; WP_055576189.1; NZ_LKTM01000002.1.
DR STRING; 1778.A9W97_30355; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000051677; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd05195; enoyl_red; 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; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
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; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; NF041183; Pks2_ls1_myc; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 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; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051677};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..429
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2019..2101
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2101 AA; 222970 MW; 3D7A187C2007798E CRC64;
MEKARVTPVA VIGLACRLPG GINSPEQLWQ ALLRGEDFVT EVPLDRWDID EYYDPEPGVP
GRSHCKWGAF MDNLGDFDPE FFGISEREAI AMDPQHRLLL ETSWEAMEHA GLTPTQMADS
LTGVFVGFTH ADYQFVQAET GALEGPYGNT GTNSCMASGR VSYALGLRGP AVTVDTACSS
GLFAAHLAAR SLSEGESDLA FAGGVYAMLE PRRFASGSAN GMLSRSGRCH AFDVEADGFV
SGEGAVVLLL KRLPDAQRDG DRILAVIRGT AANQDGHTVN IVTPSADAQE AVYRAALAAG
GVDPATVGMV EAHGPGTPVG DPLEYASLAA VYGIDGPCAV GSVKTNFGHT QSTAGALGLL
KAILAVQHGV VPQNLHFQTM PDQMAEIDTN LFIPQEVTPW PISDTEKPRR AAVSSYGMSG
TNVHAIVEQA PAQAPVAQTV SPDGSTGLEG TLVFPVSASS EEALRETAGR LADWIDSQPD
VALEDLAYTL ARRRGHRTVR TALLADTATE LSEALRELAG GELPLPPAVS QDDRRPVWVF
SGQGSQWAEM GKDLLATEPV FADTIAEIEP LIAAESGFSV TEAMTAPEKV TGIDRVQPTL
FAMQVALAAT MKHYGVTPGA VIGHSLGESA ASVVAGALSL EDGVKVICRR SKLMTRISGA
GAMASVELPA QQVFSELLGS GITDVTVAVV ASPQSTVIGG ATDAVRELIA AWEERDVMAR
EVAVDVASHS PQVDPILDDL TEALEEISAQ EFEVPYYSST SFDPREEPYF DAYYWADNLR
HTVRFAAAVQ AALEDGFRVF TELSPHPLLT HAVDQTARGI DMTAAALASV RREQPLPHGL
RGLIGDLYAA GAAVDFAVLY PGGNLVETPL PAWTHRRLLL EESTDRLAHA NTVAVHPLLG
AHVRLPEEPE RHVWQGDVGT EAQPWLGDHQ IHRAAALPGA AYCEMALAAA RTVFGDDAEV
RDIRFEKLLL LDEVSPVGAT ATVEAPGVVP FLVETMENGA NGERSRRASA MLHAADTDSA
PPAPHDIEAL LASHTNPADG DDLRHEFDSR GIQYGPAFSG LTAAHVTEEA GDTVLAEVAV
PSSIRAQQGA YGVHPALLDA CFQSVAAHPG VGNAGVGGLL LPLGVSRLRA YASARHARYC
LTTVTPDATG VTADIDILDE HGTVLVAVRG LQMGTGASPG SERDRVLAER LLTIEWQQRD
LSDKAVTEPG NWLLVSTSDA ADMMATQLTD TLKMHDSDST TISWLLHDDH QAQAAVLREQ
LSANAFSGVV VLTAPKSADT EGGSPVDRGR EYVEHVVRIA RELPDIEGQT ARLYVVTRNA
QTVLADDCPN LEQGGLRGLL RVISAEHPHL KVTYIDVDEH TGAEQVTRQL LLTESEEDET
AWRNDEWYTA RLSPTPLGPD ERQTTVVEHE HQGMRLQIRN PGDLQTLEFA AFQRVAPGPG
EVEVAVGASS INFADVLVTF GRYQTADGQQ PQLGTDFAGV VTAVGPDVTD LKVGDRVGGL
SASGCWATFV TCDARLATPI PDALTDAQAA AITTASATAW YGLQDLARIR AGDKVLIHSA
TGGVGQAAIA IARAAGAQIY ATAGSESRRE LLRGMGIEHV YDSRSVEFAE QIRNDTDGYG
VDIVLNSVFG AAQLAGIKLL ARGGQFVEIG KRDIYGDTKL GLYPFRQNLS FHGLDLGLLS
ATDPGAVREL LTTVYNASAE GVLPIPESTS YPLADAATAI RVMGAAEHTG KLILEVPHAG
RSSVVLPPEQ SRAFRSDGAY IITGGLGGLG LFLAEKMAAA GAGRIVLSSR SAPSEKASET
IELIRSIGSD VVVECGDIAE AGTAPRLVSA ATATGLPLRG ILHGAAVVED ATLPNITDEL
IQRDWAPKVD GAWHLHEATQ GHELDWFCSF SSAAALVGSP GQGAYAAANS WLDAFTHWRR
AQGLPATSIA WGAWEEVGRA TTFAEQSGEG EAIGADEGAY AFEALLRHNR AYTGYAPVIG
SPWLSAFAQR SPFAELFKSS KGRSGTNKLV AKLMELPVEE WPGQLRRVIS EGVSLILRRA
VDPDWALSEY GLDSLGNLEL RTHIQTETGV RLTSNEITTV RDLADRISER LAAAQDVPAS
A
//