ID Q1D591_MYXXD Unreviewed; 1777 AA.
AC Q1D591;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Nonribosomal peptide synthetase {ECO:0000313|EMBL:ABF92114.1};
GN OrderedLocusNames=MXAN_4002 {ECO:0000313|EMBL:ABF92114.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF92114.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF92114.1, 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};
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DR EMBL; CP000113; ABF92114.1; -; Genomic_DNA.
DR RefSeq; WP_011554012.1; NC_008095.1.
DR STRING; 246197.MXAN_4002; -.
DR EnsemblBacteria; ABF92114; ABF92114; MXAN_4002.
DR GeneID; 41361333; -.
DR KEGG; mxa:MXAN_4002; -.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_0_9_7; -.
DR OrthoDB; 8612214at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd05931; FAAL; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR040097; FAAL/FAAC.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002402}.
FT DOMAIN 602..679
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1669..1745
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1744..1777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1767
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1777 AA; 191151 MW; 91A98B331820E477 CRC64;
MHLPTRADPA SEFVCPEDVT LVDMCRARAA AQPDDWIYTF LDEAGEQAVS YAELDASARA
VAALLQRHLA PGERALLLYP PGRDYTLGFL ACLYAGVVAV PAYPPDPMRL GRTLPRLQAL
VADCGARVAL TTSGIADMVE PLTQGAPDLR ALRWLATDSV FQHEAEAWRA PVLRGDSVAF
LQYTSGSTGT PRGVVLRHRH LLHNSWLIAR GFDTRPHPVA ALWLPPYHDM GLIGGLIQAL
YRDIPSVLLP PMSFLHRPLR WLEAMSRFGA TVCGAPNFAF DLCVRKTTPE QRAALDLSRL
EVAFSGAEPV RADTLDRFVD AFAPAGFRRE AFYPCYGLAE GTLIVSGGTR SAVPVVRRFA
RDGLLRGEAR APEVDAPATA LVGCGQALGG QDVRVVDPET GRPCAPGRVG ELWVRGPSVA
DGYWQRPDET ERTFHGRLAG SGEGPYLRTG DLAVIDGGEV FITGRLKDVL VLRGLNYYPQ
DLEHAADRCH PGVRPGCGAA FAVDAGDEER LVIVQEVAAK VATPEAAAEV VASIRAALGE
AHGLAVHAVV LITAGTLPKT SSGKVQRRAT REAFLAGTLD EVHGWKEDAA AASLDIKPDA
APEAADVLAV LRSRLASLLG ANGPALSVDV PLTHQGLDSL RALEVLHAVD EAWGVSPPIT
AVLQGQSLRE LARWVERART EGAEARPEAP AVMPGDPAAF VSDGQLALWF LQRMAPGSKA
YHVSQAVRFV TPVDPGALAR AFSVLVARHP ALSSAFPEVQ GAPARRACVA PPELARVEAS
TWTDEALRER LDADAREAFD MERGPLVRAR LYTGAPRGDV LLLAMHHLVT DFWSLEVIAG
ELGALYTAEV RGTPSGLSPP PPVAPILLSL ARRSTGAQGE ALLAWWREHL GGELPVLELP
TSFPRPRLQS FRGAQVTFRL PRETSTRLKA LARTHGATPF MVLLAGYLAF LRRYSGQEDL
IVGTPTTGRP RADLSRQVGY FVNPVALRAR VPRTLSFSGL VARVRTTVLE VLEHQDLPFT
RLVEQLQSRR DPSRAPIFQT MFALQSPRTE NELLGAFAVG ASGASARLGD DLTVESVPLS
HPGAAFDLAL MMTELEGAFV ARLEYCADLF DAATAERMAR HLGALLDAAV AQPEVPLGDL
PLFAPDERRT LLALGRRTQD TRGALVPGII HRIEDWAAKT PQAPALVAGA SSWSYREVAA
WVARLAARLR RHGVGPEVRV GTLLERGSSE QVVAFLAILK AGGTVVPQEP SYPPARVAWT
LADCGARVLL AQERYAQRLA LPEGVTLLPW EAHGEGDDMP DMSLWEAGEP PPDCAAYITY
TSGSTGKPKG VMVPYRGTAH LCESMVSDLP VGPGSRVLQF ASPAFDMSAW DYFLALASGG
ALHLSPGGPP AGDALYRMLR EQRITSATLP PPVAALLPEG PLPDLSMFMV AAEACPASLV
ARFAEGRAFY NGYGPTEVTV GATWGVIAPD EVGPPNIGRS MPHVDTYVLD EALQPVPVGV
AGELYVGGPS VARGYLDRPD LTAERFIPDP HGGEPGARLY RTGDMARRRA DGRLDFQGRA
DAQLKIRGFR IEPGEVETAL RELAGMRQAH VTSWRPSVDG EPRLVAYVVP PPGDILPPGE
LRARLREQLP EHMIPVDIVP VEALPLLATG KVDVRALPRP SLAVSPAGKP RTPLEETVAR
AWAEALGLPA VDVHAHFFDD LGGSSLSAVR ACSRLGEALG QDVPITHFFE HPTIHELARR
LQAEARPEPT SDVKHQSRAE ARRQALQRRG RNPRGQD
//
