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Database: UniProt
Entry: A0A238JQS1_9RHOB
LinkDB: A0A238JQS1_9RHOB
Original site: A0A238JQS1_9RHOB 
ID   A0A238JQS1_9RHOB        Unreviewed;      1501 AA.
AC   A0A238JQS1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Dimodular nonribosomal peptide synthase {ECO:0000313|EMBL:SMX32905.1};
GN   Name=dhbF {ECO:0000313|EMBL:SMX32905.1};
GN   ORFNames=MAA8898_00355 {ECO:0000313|EMBL:SMX32905.1};
OS   Maliponia aquimaris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Maliponia.
OX   NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX32905.1, ECO:0000313|Proteomes:UP000207598};
RN   [1] {ECO:0000313|EMBL:SMX32905.1, ECO:0000313|Proteomes:UP000207598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX32905.1,
RC   ECO:0000313|Proteomes:UP000207598};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FXYF01000001; SMX32905.1; -; Genomic_DNA.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000207598; 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; cd05930; A_NRPS; 1.
DR   CDD; cd08700; FMT_C_OzmH_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12230; -; 1.
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; 2.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020459; AMP-binding.
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; 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   PRINTS; PR00154; AMPBINDING.
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:UP000207598}.
FT   DOMAIN          1387..1462
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1470..1501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1501 AA;  161679 MW;  21192CB44DA9F378 CRC64;
     MAFSCIVMGN ESLLVHCAEM ALARGNRVAA VVTENADVAR WAEGRGLPVV APGAGLAARL
     PKGVDWLLSI ANLAILPEDV LALPTKGAVN FHDGPLPRHA GLNAPVWALF EGESTHGISW
     HLIEGGVDKG DVLVSAAFYI TAQDTALTLN TRAYEAAMES FPALLDQLES GVLQRQPQDL
     ALRSYHGRVQ RPSGFGLLDF RRPAVELERL VRALDFGGYW NPLCAAKLRA REALWLVGSA
     RLTESFAAPG TVLEVGKDRL TVACGAHALV LGGLRRICGA PVDVDEIART GEVLPLLDAS
     ALAHVDAGMA GVARHEGAMR RRMAELDPVS LSGLREGVAD LQRRDVSLPG DGAQAVARWA
     RQLAGRDGVD LAWADGAWAE MAGLILPWSP LRVSDVGAVT PHPVASDLFA RAPELDWPQV
     PQIGLAVAGA GHIPGTAITV ILGDKPVFSF DAGRLDPAQA ELLAARLEFA AQGGEGLPEA
     ERDIVLSRWN ATGTEHDRAL TMQAAFEAQV AKTPEAVALI FEDTRLSYAE LNARANRAAH
     LLRQMGVERG QVVGLCCRRS VDLMVGALAI LKAGGAYLPM DPTYPVQRLD HFAQDSGARV
     IVTQAGVEPS LPRHDAQLLV LDAEPRLDGM PVENPAPQSG PEDLAYLIYT SGSTGKPKGV
     MVEHRNVCNF YTGMDTHIPQ EGGVWLAVTS LSFDISVLEL FWTTARGLTV VLTGDEDRAL
     ISKGPMPRGG GMEFSLYYWG NDDGAGRDKY RLLLEGAQFA DENGFVAVWT PERHFHAFGG
     PYPNPSVTGA AVAGVTRNIG VRAGSVVAPL HHPARIAEEW AVIDNLTNGR AGMAIASGWQ
     PDDFVLRPEN SPPENKPAML RDIETVRKLW RGEAVAFPRK DGSLHEVVTQ PRPVSKELPV
     WVTTAGNPQT WKEAGQLGCH VLTHLLGQTV EEVGGKIRLY HQALREAGHD PRDFTVTLML
     HSFLSDSREH AREIAREPMK DYLRSAAGLI KQYAWAFPAF KRPEGVSNAF DLQLDGLEPE
     ELDAILDFAF ERYFNDSGLF GTVEDALARV EEVKAIGVTE IACLIDYGID RQTVMDGLKP
     LAEVVARAGG VPELEADDFS IAAQIVRHGV THLQCTPSMA RMIAMNEEAR YALSGVQHVY
     IGGEPLPGAL VAEFAQITGA TVTNMYGPTE TTIWSSCTRA EAGETTVNIG LPLANQQLYV
     LDAEGQPVGL GQEGELWIGG EGVTRGYWNR PELTAERFVP NPFHAGRMYR TGDLVRRRVD
     GRIDFVGRVD HQVKLRGFRI ELGEIEALLA AQGGVTQAVV LAREDVPGDV RLVGYYTGRA
     QDEAALKVAM GRDLPGFMVP GRFVHLAAFP LTPNRKVDRA GLPAPQAAVA KPAERPQPAP
     VAVNGSGEAA QVEAAIAAIW QRTLGVVPSG RDSFFDLGGH SLLAVQAHRA IREELGAAKL
     SITDIFRFPV LADLAARVAG LIDGPVKVPD QTVEPVPASS RAQSRSEAMA RRREMRARRR
     A
//
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