ID   A0A3B0MQT2_9RHOB        Unreviewed;      1509 AA.
AC   A0A3B0MQT2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Dimodular nonribosomal peptide synthase {ECO:0000313|EMBL:SUZ31274.1};
GN   Name=dhbF {ECO:0000313|EMBL:SUZ31274.1};
GN   ORFNames=ROE7235_01010 {ECO:0000313|EMBL:SUZ31274.1};
OS   Roseibaca ekhonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Roseibaca.
OX   NCBI_TaxID=254356 {ECO:0000313|EMBL:SUZ31274.1, ECO:0000313|Proteomes:UP000272908};
RN   [1] {ECO:0000313|Proteomes:UP000272908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7235 {ECO:0000313|Proteomes:UP000272908};
RA   Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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; UIHC01000007; SUZ31274.1; -; Genomic_DNA.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000272908; Unassembled WGS sequence.
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:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd08700; FMT_C_OzmH_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12230; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.20.20.30; Luciferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR024011; Biosynth_lucif-like_mOase_dom.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR036477; Formyl_transf_N_sf.
DR   InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   NCBIfam; TIGR04020; seco_metab_LLM; 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; PF00296; Bac_luciferase; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51679; Bacterial luciferase-like; 1.
DR   SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000272908}.
FT   DOMAIN          1391..1467
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1373..1394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1467..1509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1492..1509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1509 AA;  160822 MW;  709824998C62CB5D CRC64;
     MTQFNSILIG DETLTAECGA QLLARGHRIG AVVTDNPRVA DWAAGAGLNV LAPGAGLAAR
     LAGLQADWLF NIAGLRMLPR NVLDLPALGA INFHDGPLPR HAGLNAPVWA LLEGEARHGI
     AWHVIEDGVD TGDVLVSAEF DISPEDTALT LNTKCFSAGL DSFAQVLDML AAGQLARQPQ
     DMTARSVHTR ADRPGLGGQI DPRQTTTDIL RLVRAMDHGP YWNPLTTPKL RLGQTVVCVG
     QADMADGHAP AGTILDVSED SVTVACADGA LRLFGLICQQ GKPVMPAALV AAGDKLGAPD
     TRLHDVLVQI ANAEPAYRDA LRGAGDPGLG QGTESEMLPL DLGGATTDAS IAAFAAALGA
     AFGRTALRMA HVTRAGAELA AQAPDFLLGW APLLVSMDDT GPLSSLQNQM KRAAHAPALA
     RDLPARDPSL GPIAPPELAV TDGSPSDAAL VLDLSGPALR YDPACLSAEL AATLKTTIEA
     LAPKLADMPL AAQVTAPDIK ADDTARPYDR ACIHHAFEHQ VAKTPDAEAL SFENQSLTYA
     ELNARANRVA HVLLGMGLRP DTPVALCAKR GPNLLVGALG ILKAGGAYVP LDPAYPADRL
     AHYLSDSGAP FIVTEHALLD MLPDHSAEML QLDTDTRLDA APDTNPDSAV TPDNLAYLIY
     TSGSTGTPKG VMVEHGNVAN FFAGMDDCIR HDPPGVWLAV TSLSFDISVL ELFWTLARGF
     KVVLMGDEDR AMVAKGPVRV SEGHMDFSLM YWGNDDGQGP QKYHLLLEGA KFADSHGFCA
     VWTPERHFHA FGGPFANPSV SGAAVAAVTQ NIAVRAGSCV APLHSPIRIA EEWAMIDNLT
     NGRTGIGIAS GWHPVDFVLR PENRPPNNKA AMFETLETLR KLWRGETVEF DKGDGMVPIQ
     TLPRPVSSEL NIWLTTAGNP ETWREAGRLG AHVLTHLLGQ SVAEVEGKIK IYHEALRETG
     RDPADYTVTL MLHTFVARDR EHAREVARGP MKSYLKAAAA LVKQYAWAFP AFKKPEGAKN
     PMDIDLSTLS DDEVEGILDY AFNRYFEDSG LFGTVEDCLE RVEQLKAIGV NEVACLIDYG
     IATEQVLEGL YPLAEVVKRS NAGLHLPDDD FSLSAQILRH KVTHLQCTPS MARMLCMSDE
     ARAALATVPN VLVGGEALPG ALAQEISGLT GQPLRNMYGP TETTIWSSST TTRGNAGVVG
     IGAPIANTSL HVLDETQRPV PLGTEGELYI GGDGVTRGYW NRAEMTADRF IPNPFGAGRL
     YRTGDLVRRN PAGGIDFLGR VDNQVKLRGH RIELGEIESA LDAVAGITQS VVIAREDQPG
     DLRLVAYYTG TPAGDLRSSL ADRLPAHMLP SHFVPMAALP LTPNKKIDRK ALPAPTQAPA
     ATTQPASDAA PAAEGTQATI AQVWQDVLGI AQVAGSDNFF NLGGHSLLAV QAHRELRARL
     NMPGLSITDI FRFPVLGDLA RHLDAKQRPA PAATVQPLHP TADTPAAPTD RMDAMARRRA
     MRDRRAGTK
//