GenomeNet

Database: UniProt
Entry: A0A136PPX2_9ACTN
LinkDB: A0A136PPX2_9ACTN
Original site: A0A136PPX2_9ACTN 
ID   A0A136PPX2_9ACTN        Unreviewed;      1973 AA.
AC   A0A136PPX2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:KXK60529.1};
GN   ORFNames=AWW66_18400 {ECO:0000313|EMBL:KXK60529.1};
OS   Micromonospora rosaria.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47874 {ECO:0000313|EMBL:KXK60529.1, ECO:0000313|Proteomes:UP000070620};
RN   [1] {ECO:0000313|EMBL:KXK60529.1, ECO:0000313|Proteomes:UP000070620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 803 {ECO:0000313|EMBL:KXK60529.1,
RC   ECO:0000313|Proteomes:UP000070620};
RA   Yang H., He X., Zhu D.;
RT   "Whole genome sequence and analysis of Micromonospora rosaria DSM 803,
RT   which can produce antibacterial substance rosamicin.";
RL   Submitted (JAN-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:KXK60529.1}.
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; LRQV01000068; KXK60529.1; -; Genomic_DNA.
DR   RefSeq; WP_067367776.1; NZ_LRQV01000068.1.
DR   OrthoDB; 3406074at2; -.
DR   Proteomes; UP000070620; Unassembled WGS sequence.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
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; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
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; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070620};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..443
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1350..1424
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          904..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1973 AA;  218467 MW;  E44FB069A1B959D5 CRC64;
     MPESRATKRR ETGLEIAVVG MAGRFPQAED IDQFWANLVE GVDAISRFTD DELLGVGVAK
     AALDDERYVR AKGVFPNIEY FDAEFFNYAP ADATLLDPQV RALHEEVFHA LEDAGYSAEG
     RPEVIGLFLG ATNNLPWETH TLTRHILESG MTFTGMQLND KDFAATRIAY ALDLKGPAFT
     LHTACSTSLV AIDMACRNLW TGSCQIALAG GSGLTLPHKN GYRYQENMIH SPDGHCRPFD
     KDAAGTVEGN GVGVVVLKRL ETALRDGDHV YAVIKGSAVN NDGNRKVGYT APSIEGQAEV
     IRKAYRVANV PTAEVSYVET HGTGTSLGDP IEVEALRKAF GTGEPGATGL GSLKASIGHL
     DTGAGVASLI KVCKILQHRT VPRSLHFKEL NPNVDLDGSP FYVVAEQQEL RPKRSKTDEV
     LPLRAGVSSF GIGGTNAHVV LEEAPEARPA SSTGRTYNTF VVSASSADAV GRIKRNFVDY
     LAAHPDLDGS DLAWTLQNRQ RRLAHRYAVE FGDVAQLRER LQESLDADEP SAQVHKNARR
     DAYFLFSGLG AQHLRMARGL YETEPDFRAH LDECFTISAA QGHEVPREVF FGDSAEAERQ
     LNNIGTTQIL LFMLETSMAR TLIGWGLKPK GMIGHSTGEL AAAYVAGVFS LADGIRLVQA
     RGSLMDTTVE GALTSVRAPE DVVRGMLTDE SAIAAVNGPE DCTVSGTPRA VAEVERQCAE
     REIKFSHIEA DHAYHSQYMD SMLGRFREVL DQVTLHQPKI PYLSNVTGTW ITAAQATDRE
     YYCSHARETV RFAAGVEAIL ERGGTLFVEV GPGKSLSSFV RAIGRDAEVT TVNMLRHRME
     EVSDEEHLAR AVKKLWENGV SLDWKAFHKG RHPRKVTLPL YPFEKVEYPV DIEQFQRLVE
     GQTDAGPRAA TVQPTRQAVT GTEATTGPVP ASRLAWAPSM RPSSTGKEQP KVLIALTDDR
     RGLKRVLDGV AHWRTLYVSF GPQYRFDRLS GAVVRPGHDD DLRRLLDDLE RHALAGDTVV
     VDRTDHPSLV TTLRGLCAAI PDMRERCVKD VVVLDTGDLL GAHGDVVPLL IGLNHEHPTF
     RVRALRCDAS LDDRAGRAAW REHLQTELEA HRPDDVAVSY ERGRRLVPRL VPLDGAVAAA
     GRATRTALLA RRRDVENVVR DLAGANPART VEILPFDLGS DPGGTRVGVV DERITVLPVV
     TGSTWEELAG TLSGGLRALP AVDEVVLWDT PSRDGATDGP DQRRLLGLLT EVGREQRIPC
     YVLSRPGLDR DGWDRHVTTW FADNERAAAE AGITRLYSFA DLREADRSVL DLLPRMRDAG
     IRTAYHGVDL LRAQAAAKLV DVEVESGRAD ERQAIAAVIE REVRTLLGFS EIDGRADIFD
     IGLDSVKLVQ FTNALDRNGY KVLAKEVYNH PTIAGLAAFI ERTVTRGGSE DMSFDSLAVL
     LEQRLGAPCV FREVKSGRDE DTLVVLAVAG LDEALKKRVV REFTELRVPT EFVPHYVVAG
     GPDDIGMGLD FEALRASAGL PSYPGGYAAV FDEIDRRQEE LRRSIGAQPV KWTYPISAMQ
     KQHFATESRL QLYLIQLREL VDLDVLQQAL CDVIGRHGLM RSFLTRSFGR FRWKEFEAPE
     VIALPRLDMS GLEPHEQEEL RAELVKREWS MDFKVVDKPM YQVVLITYND RSHDLLFQFD
     HSIFDAASGQ LFRGDLLKRY EELMAGTGRA MPIAKSYRHL QDQIAKGPVD ITSDELIEKF
     DLVEYVRYAK TIQERSARFA NSPIRDVRYS VELDRLRNAD GTEPDLFYLV VHLYARVVSR
     LLGIDKVALI TLLQSRVFED KDYSEVMGMV LGSLPVLVPA ERDTMRDLDG IITDKVRMMN
     KNNVSFLNLV QNVRSIVKHR KVLSVMGKTL RPTCLLNFVG NVEDEYDAIW DMTLAQLTDD
     QAKLDYADCY CVSKVGNGRL DLLLLSKWVE DPHELIRILD DEVEYLTSRV SAG
//
DBGET integrated database retrieval system