ID F8CHL5_MYXFH Unreviewed; 3782 AA.
AC F8CHL5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Non-ribosomal peptide synthase/polyketide synthase {ECO:0000313|EMBL:AEI67516.1};
GN OrderedLocusNames=LILAB_28145 {ECO:0000313|EMBL:AEI67516.1};
OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI67516.1, ECO:0000313|Proteomes:UP000000488};
RN [1] {ECO:0000313|EMBL:AEI67516.1, ECO:0000313|Proteomes:UP000000488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX PubMed=21868801; DOI=10.1128/JB.05516-11;
RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT 1.";
RL J. Bacteriol. 193:5015-5016(2011).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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; CP002830; AEI67516.1; -; Genomic_DNA.
DR STRING; 483219.LILAB_28145; -.
DR KEGG; mfu:LILAB_28145; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_21_2_7; -.
DR Proteomes; UP000000488; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19534; E_NRPS; 1.
DR CDD; cd19531; LCL_NRPS-like; 2.
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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
DR Gene3D; 3.20.20.30; Luciferase-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; 3.40.50.12780; N-terminal domain of ligase-like; 3.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR024011; Biosynth_lucif-like_mOase_dom.
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; IPR011251; Luciferase-like_dom.
DR InterPro; IPR036661; Luciferase-like_sf.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR010060; NRPS_synth.
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; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR01720; NRPS-para261; 1.
DR NCBIfam; TIGR04020; seco_metab_LLM; 1.
DR PANTHER; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00296; Bac_luciferase; 1.
DR Pfam; PF00668; Condensation; 3.
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; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 3.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 6.
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; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..440
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 923..998
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3229..3303
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2204..2265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3782 AA; 405121 MW; 45FBCB64A1BCDC64 CRC64;
MAEHDTLSEN SGGTGNDIAI IGMAGRFPGS ADVQSFWRNL REGVESIVRL APEALEWSPL
MAEASRHHPD FVPVAAEMEG GDGFDAAFFG MAPREAEWMD PQQRVFLECA WTALEDAALD
PERFEGKIAL YAGASASMHG LGRVGQGNLD PASLYELMSN TAENLATRAS FKLGLRGESL
SLYTACSTGL VAVHMACQSL VMRQSDVALA GAVRLAMPQR TGYLFQEGMI LSPDGHCRAF
DARAAGTVPG NGVAVVVLKP LEDARRDGDR VYAVIRGSSI NNDGGQKVGY TAPSVEGQAD
VIGEALAFAG LEAGDIGYVE AHGTGTALGD PIEVAALTRA YRRQTEQKGY CALGSVKTNV
GHLDTAAGLA GLIKTALALT HEELPPTLHF ERPNPAIDFA NSPFFVVDRL RPWPRGPVPR
RAGVSSFGIG GTNAHAVLEE APLPEPTTPS VRPTQVVTLS GRSPEALDAA ARELAGWLDA
APADVALADV AFTRNVGRRA FEHRRSFVAP DVAALREKLR APGKAQAVEN VVAAREQGVA
FLFPGQGAQS VGMGHELHAA EPVYREALES CLDGLGATLG AAVRGVLSPA PGAEDAAKQA
LADPGIALPA LFAVEYALAR QWEAWGVRPR AYLGHSFGEY VAACLAEVLP LEDALALVAA
RGRLMARMPP GSMTAVGCAE ETVRPLLTEA LSLAAVNGPD RCVVSGPTPD VEALERDLAV
RGIGVLRLPA AHAFHSAAVE PLMAELRRVV AGLRLAAPQR PYVSSVTGTW IRAEEATDPD
YWLRQMRAPV RFGDGLEALR ADGCTVFLEV GPDQALTALA RGGPGRAVAS QPRTGSKRGM
HATLMEALGA LWEQGLVLDW HQVYAHEARR KLSLPTYPFQ RQTFRVAAPA PVKALQAPAE
VVAVSPVVAD GGGAAEAASD LAGARTEVER KVLAIWRERL GRSDFGIHDD FLELGGNSLM
AAQLLTRLRE AFPVPLPLSD VFDSPTVAGI SARIQERLGA SGANGAEPVL PPLVRIPRDG
DLPLSVVQGR VCALEQALPG NPALNMYVVL RFQGALDVAV LERSLEAAAQ RHEALRTSYP
LQDGVPVLRI APRLTFPLTP EPLAGATWQQ RVYDEVSRPF DLERGPVARA RLWRLDADDF
MLAVTIHHVV CDTWSLVVFA KELGEHYAAL KQGHPARLPA LPVQYVDFAA WQRKALKEGA
FASQIAAWRE RLAAFPSPLE LPVDRARGDG PALRGQVLKV GFSATLSAAV QALAQREGVT
PFMVLLASWK ALLSRWTGRD DIVVGTPIGN RSRPELEPMI GYVAHAVPLR TDMAGAPSFR
ELVMRVRDVI MEAYAHPDVP YEELGREIEP TKDTGRSRVF DTLFVLHSRF DRTVDLPGVR
MSLAELDDVP PEFGSVLSDL TVGLGEHAHG FSGTIDYADE RFERDTVERL VAHWTTLLEA
AVAAPETPLL ALPLEQPRPG PVAVEAGRSA SAPVPVAAAL QARAAADAAS VAMTAPDGRA
VTWGELRASA DRLAAELAGH EVGPEVLVAV CVEPSVERVV AQWAVQALGA AYVLLSVPQL
RELASLSPPG APSPLLLTHT NVRTGVPLDA ARVIRVDEVL SRTDSRLSVP AREAPRASDG
DMVCLEPLVG SRGEQLRAIH THHTVAALFA RLDAEAPSKD GIWLAAEEAQ APGSGLELLW
ALTRGLRVVL PAERARFTSW GTGAAAERRR TDFSLSFFAN DEDSLGGRKY RLLLEAAKFA
DAHGFSAVWT PERHFHSFGG LYPRPAVVGA GVATVTERLG IRAGSVVLPL HDPILVAEEW
AVLDNLSDGR VGVSFASGWH ANDFVFAPDR YARRKDVLHR GIEEVRTLWR GGTVLRRNGA
GEEVAISLRP KPVQKVLPIW LTAAGSPETF RLAGELGAYV LTNLMGQHLD DLASKVALYR
DAWRQHGHAG RGHVSLMMHA FLGDDPAEVQ KKARPPLLDY FRSSVDISSG FLASLGLDVD
PRSLSRSDID ALLAHGVERY VQDGGLIGTP ESCAPMVERV QRLDVDEIAC LVDFGVEVEA
TLEGLRHLDA LRGRHSPAPS PAIPSAALRE GPGAAEALLS LVREAGITHL HCTAALARSM
LALPDAAEVL RPVRHVLLEG ASEEAAASLA RAMPWRVAHR QPGLGLGAWA VAMGPVDASR
WDVVDGRGQP VPVGVVGELV VTGAGVPRGF WNAPETTSMR VLAGDSDGAR RLGTGRRARR
KRDGSVELLA AAPVTERRPA PPKSAARMGS GAASRPEGSG TIPLVPRGRP LPLSFAQQRL
WYLDRLEPGN VAYNNAVAFT LSGKLDAAAL ERALNGVVRR HEALRTTFAV EGDAAVQLIA
PALEVSILVR DAEDASEEEL ARQAREEARR TFDLEQGPLL RATLLRVGST EHVLLLTLHH
IISDGWSAAV MVHEMIQLYE SEMSGQPPTL PALSVQYADY ALWQLEWMRG PSLKAEQDWW
GEVLAEVPVL QLPVDRPRPP VQTHDGAQLP FSVPRSLMDA VVAAGRKEGA TPFMVLLAAW
QVLLHAYTGQ EDFAVGSPVA GRNRPEVEPL IGCFINSIAL RADLSGDPTF TQVLGRVRRT
ALAAFSHQEM PFEKVLEVLN TPRDLSHNPV FQTMLVLHNT PTPVLSLAGL QMRGRYVHTG
ATKMDLTLEV TETAEGLRGG IDFNTRLFDE ATIARLAGSL LRVLEAAASR PDARLSQLDL
LDAAERARLL VEWNPAPVAE LPASDTVPAR FLAQAARTPD AVAVADGART FTYRELEALS
LRVAGHLVSR GVGRGAVVAL AVAQPSEVVA GLLGVMRAGA AVVVLDVDHP PERLSSILAD
TQARMLLTSE SLRARVPSRA GPEVITLDSL PEATGGLRVR PEGTDAACIV YTSGSTGRPR
GVVLEHRHLV AATRARAEVY GAPGVVMSLA PFTFDAALAG LLWSLFEGGA LRYPDAEERE
DPRRLAERIA QSRVTHLISV PSLYGQLLAA AAVGGLKSLT AVSVGGEACP VELTRAHHEA
LPSVALFNEY GPTEATIWST VHRVRVGEEH RVPIGRAVPG ARVYLLDARR KLVPQGAPGE
VYLGGAGVAR GYLGQPGLTA ERFVTDPFDG RSGARMYRTG DVARWRGDGT LEFLGRVDEQ
VKVRGFRIEP GEVEATLLAN PSVREAVVVA RDDGKGPKRL VAYVVPVATD SGAAPDAAAL
KGWVRSRLPP YMVPAAVVAL DALPRTRHGK VDRRALPAPE TGPAVAPVAP RSEVEATLVS
LWREVLGVER VGIHDDFFEL GGDSILGLQI ITRARAQGIE LSPKQLFQNP TVARLATVAG
TRLAVQAEQG AVVGPVALTP IQHWFFELAQ EAPHHWNMSL LLEVKTPLDG ALLGQALTHL
LAHHDALRAR FARGDAGWRQ VVPEPEAGVL VEQVDLSTVP EVEQAAVLQH RAEEAQQALR
LDGGLLHATL LTLGRGRSAR LLLTVHHLVV DAVSWRILLE DLAGVYAQLA AGNAARLPPK
TTSFQAWARG LETLARSEKL AAERKWWLER PWQEAARVPV DFPEGVNTEA TAHSVRVTLD
VEETRALLQD VPKAWHTQAQ DPLLTALGQA LTAWAGGGVA LVDVEGHGRE EVLPGVDVSR
TVGWFTRVFP ALLDLRGAPT PGDALRAVKE GLRAVPSQGM GWGLLRYVSK DAALAALPAA
EVGFNHLGQV DGVVGADGPF ALAAESESLR QRAPVARRPY LIDVMSAVRN GRLEVLWTFS
GAVHRRETVA RVAEDFVTRL RALVAASKAP DAGGHSPSDF PLAKVKQAQL DKLSARFGKK
TR
//
