ID Q1D592_MYXXD Unreviewed; 3780 AA.
AC Q1D592;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE SubName: Full=Non-ribosomal peptide synthase/polyketide synthase {ECO:0000313|EMBL:ABF89749.1};
GN OrderedLocusNames=MXAN_4001 {ECO:0000313|EMBL:ABF89749.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF89749.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF89749.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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}.
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DR EMBL; CP000113; ABF89749.1; -; Genomic_DNA.
DR RefSeq; WP_011554011.1; NC_008095.1.
DR STRING; 246197.MXAN_4001; -.
DR EnsemblBacteria; ABF89749; ABF89749; MXAN_4001.
DR GeneID; 41361332; -.
DR KEGG; mxa:MXAN_4001; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_21_2_7; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000002402; 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; 3.40.50.980; -; 2.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..434
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 921..996
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 3227..3301
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 895..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2229..2254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3208..3227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3780 AA; 406185 MW; A3AAFB8058529BD1 CRC64;
MSENNGSAGS DIAIIGIASR FPGSADARAF WRNLREGVES ISRVPVEALE PSPLMSEAVR
HHPDFVPVAA ELEGGDRFDA AFFGMAPREA EWMDPQQRVF LECAWTALED AALDPERFAG
KISLYAGASA SLHGLAMLGQ GNLDPASFYE LMSTSAENLA TRASFKLGLR GESLSLYTAC
STGLVAVHMA CQSLLMRQSD VALAGAVRLA MPQRSGYLFQ EGMILSPDGH CRAFDARAAG
TVPGNGVAVV VLKPLEDARR DGDRVYAVIR GSSINNDGGL KVGYTAPSVE GQADVIGEAL
AFAGLDAGDI GYVEAHGTGT SLGDPIEVAA LTRAYRRHTD RKGYCALGSV KPNVGHLDTA
AGLAGLIKAT LALAHEELPP TLHFERPNPA IDFANSPFFV VDRLRPWPRG PVPRRAGVSS
FGIGGTNAHA VLEEAPLPEP ASPSVRPTQL VTLSGRSAEA LDAAVRDLAS WMEAAPTDVA
LEDVAFTRNV GRRAFEHRRA FVAKDRAELL AKLRGPGKSQ VVEHVVAARE QGVAFLFPGQ
GAQTVGMGRA LHAAEPVYRE ALEACLEGLG ARLGAAVRDV LFPSPGAEAA AEQTLADPGI
ALPALFAVEY ALARQWEAWG VRPRALLGHS FGEYVAACLA EVLPLEDALA LVSARGRLMA
RMPPGSMTAV ACAEEEVRPL LTGALSLAAV NGPDRCVVSG PSGDVEALEH ELSARGVGVL
RLPARHAFHS AAVEPVMAEL RRVVAGLRLS APQRPYISSV TGTWIRPEEA TDPDYWLRQM
RAPVRFGDGL ETLKADGCDV FLEVGPDQAL TALARLGLRG HRGRAVASLP RAGSVLDAHA
ALMEALGTVW AQGLAIDWQR VYAHESRQKV ALPTYPFQRQ TFRTPLPTSV VARPETSAAV
AERPAEAGGT PHLEAPAEQA GAHTDVERKV LAIWRERLGR TDFGIHDDFL ELGGNSLMAA
QLLTRLREAF PVSLPLSDVF DAPTVAGISA RIQARLGTPG TASTEPVLPP LVRIPRGGAL
PLSVVQERIC ALEQALPGNA ALNMYVVLRL HGALDVALLE RGLEAVALRH EALRTSYPRG
EGAPSVCIAP ELKLPLSAEP LDPAAWQPRV HDEVARPFDL EHGPVARARL WRLAPEEHLL
AVTVHHVVCD TWSLVVLAKE LGDHYTAFMQ GRPVALSTLP VQYVDYAAWQ QQALKSGAFA
SQVAAWRGRL AAFPRPLELP VDRPKGDGPA LRGQCLRVGF SRALSASVQA FAQREGVTPF
MVLLASWKAL LSRWTGRDDV VVGTPIGNRS RPELEPLIGY VAHSVPLRTD LSGDPPFKEL
VARVREVMMD AYAHPDVPYE SLVREIEPAK DTGRGRVFDS MFVLHSRFNL NLELPGLRMS
LAELENGPPE FGTVLSDLSV GLGEYEHGFS GTVDYAEERF ERDTVERMVA HWTALLEAAV
AEPGLSLSAL PLEHARASQA LASEPEASAS VVTPIAALLR ARAMADASQV AMTAPDGRGV
TWGELQGAVG RLAAVLSDRG VGPDALVAVC LEPSVERVVA QWAVQETGAA HVLLPVPRLM
ELPDLAPPGA PPPLLLTHAK VRTRVSLDAA RVLHVETVFA QTGDSGRGTS MAPLRASASE
RVCLEPWTGP RGEQLWAIHT HRTVAELFGR LDADATTKEG VWLAAEEPQV PGTGLEVLWA
LTRGLRVVLP AERARFTPVG AGAEPARRRL DFSLSFFAND EDSLGGRKYR LLLDAAKFAD
ANGFSAVWTP ERHFHAFGGL YPRPAVVGAG VATVTQRLGI RAGSVVLPLH DPILVAEEWA
VLDNLSDGRV GVSFASGWHA NDFVFAPDRY ARRKEVMHRG IEEVRTLWRG GTVRRRNGAG
AEVALSLRPR PVQQTLPIWL TAAGNPETFR LAGELGAYVL TNLMGQHLED LEGKVALYRD
AWRQHGHAGR GHVSLMLHAY LGDDPAEVRR RARQPLLDYF RSSVDIAAGF MAGMGLDMDP
RSLTPADMDA LLAHGVERYV ESGGLFGTPD SCGPMVERVQ RLDVDEIACL VDFGVEVEAT
LEGLRHLDAL RGRHSPEPGL AVPMPSLREG PGAAEALLAL VREAGITHLH CTAALARSML
TLPDAAEALR PVRHVWLEGA SEEAAASLVR AMSWRVAHRQ QDLGLGTWAL AAEPGDASRW
DVVDGRGQPV PVGVIGELVV KGAGVPLGLW NAPDSTPVRI LAGSTDAARR MATGRRARRK
RDGSLELLPA LPVPEGRPTP PKVMGARDGV AKKSEAPASI TRVPRGRPLP LSFAQQRLWY
LDRLEPGNVA YNNAVAFTVS GALDAAALER ALNAVVRRHE ALRTTFSMDG TEAVQTIAPS
LEVSISLEAV EGASAADVAR WTREEARRPF DLERGPLLRA TLLRLGSTEH VLLITLHHII
SDGWSAGVMV HEMARLYEAE LTGRPASLPA LPVQYADYAL WQLEQMRGSA LKAEQAWWRD
VLADVPVLQL PVDRPRPPLQ THDGEQLPFA VPKSLTDALV AVGRKEGATP FMVLMAAWQV
LLHAYTGQDD FAVGTPVAGR DRPEVEPLIG CFINSMALRA DLSGDPSFAE VLGRVRRTAL
DAFAHQEVPF EKLLEVLHAP RDLSHTPVFQ TMLILHNTPA AALSLVGLQL RSRPVHAGAT
KLDLALEVTE TPEGLRGSIE YNTGLFDAET IARLSGSLLR LLEAAAGSPE VRLSQLDLLD
RADRNRLLVE WNPAPTEGHL PADTLPSRFL AQVSRTPDRV AVEDGVRTLT YREVEVLSGR
LARHLVSRGV KRGDIVALAV SQPADVVAGL MGVTRAGAAV VVLDVDHPAE RLAGILADTR
AQALVASESC RARVPSREGL TVIPLDSLPE ATEDVCGLPE GTDAACVVYT SGSTGRPRGV
VLEHRHLVAA TQARADVYGE PGVVMSLAPF TFDASLAGLL WSLFGGGTLR YPDAEEHGDP
RRLAERIARS HVTHLVSVPS LYGQILAAAP VGGLRGLRAV SVGGEPCPVE LTRAHHEALP
AVSLFNEYGP TEATIWSTVH RVRVDEEGRV PIGRVVPGAR VYLLDAHRRL VPRGAPGELY
VGGAGVARGY LGQPGLTSER FVMDPFDGRL GARMYRTGDV ARWRADGTLE FIGRVDHQVK
VRGFRIEPGE VEAALLAHPA VKEAVVVARE DGKGPKRLVA YGVLATEGPG EKPDAQALKE
WVRSRLPPYM VPATFVAMDS LPRTRHGKVD RRALPTPDPA SAAAPAAPHS EVEATLVSLW
REVLGVERVG IHDDFFELGG DSILGLQIVT RARAQGIELS PKQLFQNPTV ARLASVAGTR
LAVQAEQGPV VGPVALTPIQ HWFFELGLEA PHHWNMSLLL EARAALDATL LERALAHLLA
HHDALRLGFV GGEDGWHQAI CEPGARVTVA RVDLSAVPEA ERPSALSRHA EAAQRALRLD
GPLVQAVLLE WGAGHSTRLM LAVHHLVVDA VSWRILLEDL ATAYTRLAAG DAVVLPPKTT
SFQAWARGLE ALARSQALTA ERAWWLERPW REASRLPVDF TGGLNTEATA STVQVTLEPE
QTRALLQDVP KAWHTQPQEP LLTALAQALT AWAGGAVALV DVEGHGREEV LPGVDVSRTV
GWFTRVFPAL LDLRGTTGPG EALRAVKEGL RAVPSRGMGW GLLRYVSRDA ALAALSLAEV
GFNHLGQLDG VVGEGAPFVL APEAATLRQR APSARRPYLL DVTGMVRDGR LVVLWTFSEA
VHRRETVTRV AKDFLARLHA LVHASRAPDA GGHSPSDFPL AKVKQAQLDK LAARFGKKTR
//
