UniProt: A0A1A3QAQ3

Database: UniProt
Entry: A0A1A3QAQ3_9MYCO

LinkDB:  A0A1A3QAQ3_9MYCO 
Original site:  A0A1A3QAQ3_9MYCO

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Ontology (4)   
   GO (4)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (43)   
   InterPro (23)   
   Pfam (10)   
   PROSITE (4)   
   SMART (6)   
All databases (49)   

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ID   A0A1A3QAQ3_9MYCO        Unreviewed;      2092 AA.
AC   A0A1A3QAQ3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:OBK43411.1};
GN   ORFNames=A5655_16760 {ECO:0000313|EMBL:OBK43411.1};
OS   Mycobacterium sp. 1081908.1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1834066 {ECO:0000313|EMBL:OBK43411.1, ECO:0000313|Proteomes:UP000092324};
RN   [1] {ECO:0000313|Proteomes:UP000092324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1081908.1 {ECO:0000313|Proteomes:UP000092324};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA   Lopez-Varela E., Palencia S.;
RL   Submitted (JUN-2016) 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:OBK43411.1}.
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DR   EMBL; LZLY01000158; OBK43411.1; -; Genomic_DNA.
DR   RefSeq; WP_067015515.1; NZ_LZLY01000158.1.
DR   STRING; 1834066.A5655_16760; -.
DR   Proteomes; UP000092324; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08955; KR_2_FAS_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
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; 3.90.180.10; 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; 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; 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; PS00606; KS3_1; 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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..427
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2010..2086
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2092 AA;  222491 MW;  81D656B18427B1A4 CRC64;
     MDKAGVTPVA VIGMACRLPG GINSPDLFWE ALLRGDDLVK EIPAERWDVD YYYDPEPGVP
     GRSVCKWGSF LDNVGDFDPE FFGITEKEAT AMDPQHRLLM ETAWEAMEHA GLTKDTMAEE
     TGVFVGLNYG DYQFVHAATD AFDGPYGNPG TISCMASGRI AYALGLHGPA VTIDTACSSG
     LFAIHQACRS LNDGESNLAF AGGVNVMMEP RRSASASAGG MLSGTGHCYA FDVKADGFVS
     GEGCVVLLLK RLTDAQRDGD RILGVIRATA ANQDGHTMNI AMPSGEAQAA VYRAALAAAG
     VDAGTVGMVE AHGTGTSVGD PIEYGSLAEV YGIGNPCVLG ASKTNFGHTQ AAAGALGMMK
     AVLSVQHGVV PKNLHFESLP DEMARIDTGL FVPQEITPWP LSGDQPRRAA VSAYGISGTN
     VHAIVEEAPE PISRNGAATR PGRDGTLLFP LSATSDDSLR ETAARLADWV EAHATEVAAP
     DLAYTLARKR GHRSVRTTVL ASDTPELLAA LRDVANGDAL FQEVVGQEER GPVWVFSGQG
     SQWATMGTDL LANEPAFAAA IAEIEPLIAH ESGFSVTEAL TAPEKVTGID RVQPTIFAMQ
     VALAATMKSY GVRPGAVIGH SMGESAAAVV AGALSLEDGV RVICRRSRLM TKIAGSGAMA
     SVELPAQQVL SELMARGVND AVVAVVASPQ STVIGGATET VRELVAVWEQ REVMAREVAV
     DVASHSPQVD PILDELYDVL AEIEPLTPEV PYYSATSFDP REEPYCDANY WVDNLRHTVR
     FSAAVQAALE DGYRVFGELS PHPLLTHAVD QTARSLDMTV AALAAMRREQ PLPHGLRGLL
     GDLYATGATV DFSVLYPGGH LVDAPLPAWT HRSLLLSREG HSSRALASSV AVHPLMGQHV
     RLPEEPERHV WQADIGTATL PWLADHQVHG TATLPGAAYC EMALAAARTV FGEASEVRDV
     RFEQMLMLDE ETHISLTATA ETPGTLTFAV ETNEDGVQAR RASAVLHDVD DEDVPTAQDI
     DELLETHPSR LEGSDLRDAM DLCGIQYGPA FTGLAGAHTA EGTGTTVLAE IGLPSVIRTQ
     QTNYGVHPAL LDACFQSVAA HPSVANASLG GLLLPLGVRR LRVHGPVSTA RYCYSRVTSA
     SGGAVEADLD VLDKHGTVLL TVRGLQMGTG ISPSGERAKL MAERLLTVEW QQRQLPEAAA
     ETGAWLLIST SDAADLVATA LTDAMKLHDA EAKTLSWPQQ ADHQAMAGRL RDEVEKGEFA
     GVVVVTEPKN GNPDDESAVR GGDLVHHLVR IARELPELQG ESPRLFVLTR NAQKVLSEDV
     PNLDQGGLRG LLRVIGAEHP HLHTTHIDVD EQTGAEQVVR QLLMTGPGED ETAWRNDEWY
     SARLCPTPLR PEERLSTVID HETAGMRMQI RTPGDLQTME FASFDRVPPG PGQIEVAVTA
     SSINFADVLN AFGRYQSLDN ILPQLGTDFA GVVTAVGPDV TNHKVGDHVG GMSPNGCWAT
     FVTCDARLAT TLPEGLSDAQ AAAVTTAHAT AWYGLNELAR IQAGDKVLIH SGTGGVGQAA
     IAIARAAGAE IFATAGSEQR RQLLRDMGIE HVYDSRTVEF AEAIRRDTDG YGVDIVLNSV
     TGAAQLAGIK LLALGGRFVE IGKRDIYGDT KLGLFPFRRN LAFWGVDLGL MSVSHPSQVS
     QVLSTVYRLT AEGALPMPES THYPLSEAAT AIRVMSAAEH TGKLILDIPR AGRSSVVLPP
     EQAPVFRRDG SYIITGGLGG LGLFLAEKMA AAGAGRIVLT SRSEPSQKAL ETIELVRAIG
     SDVIVECGDI AQADVAARLV ATATATGLPL RGVLHAAAVV EDATLTNITD ELIDRDWAPK
     VYGAWNLHEA TASADLDWFC SFSSAAALLG SPGQGAYAAA NSWLDAFTHW RRAQGLPATA
     IAWGAWGEIG RGADFAEGSG AAIAPDEGAY AFEALLRHDR AYTGYSPLIG TPWIASFAER
     SKFLEMFKSA GEKRSGSSKL RAELSDLPLD EWPTRLRRLL SEQIGLILRR NIDVDHPLSE
     YGLDSLGNLE LRTHIEAQTG VRITSADITT VRGLADHLFS KLAPKEDAAA PA
//

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