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Database: UniProt
Entry: A0A1I5YXH9_9RHOB
LinkDB: A0A1I5YXH9_9RHOB
Original site: A0A1I5YXH9_9RHOB 
ID   A0A1I5YXH9_9RHOB        Unreviewed;      1509 AA.
AC   A0A1I5YXH9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Natural product biosynthesis luciferase-like monooxygenase domain-containing protein {ECO:0000313|EMBL:SFQ48948.1};
GN   ORFNames=SAMN05421853_10728 {ECO:0000313|EMBL:SFQ48948.1};
OS   Roseivivax halotolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=93684 {ECO:0000313|EMBL:SFQ48948.1, ECO:0000313|Proteomes:UP000243106};
RN   [1] {ECO:0000313|Proteomes:UP000243106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10271 {ECO:0000313|Proteomes:UP000243106};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOXV01000007; SFQ48948.1; -; Genomic_DNA.
DR   STRING; 93684.SAMN05421853_10728; -.
DR   Proteomes; UP000243106; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase 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: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   Monooxygenase {ECO:0000313|EMBL:SFQ48948.1};
KW   Oxidoreductase {ECO:0000313|EMBL:SFQ48948.1};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243106}.
FT   DOMAIN          1391..1467
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1357..1387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1471..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;  160694 MW;  6CE2553DE35B9C00 CRC64;
     MSFTAILIGN DRLTREAGVK LRAAGHTLTA CVTRDGDVAD WASKEGVRVV APGPGLAERL
     EGCAADWLLS VANLDLLPPE ILRLGRKGGV NFHDGPLPAY AGVNAPVWAI LNGETRHGIT
     WHMLDEGVDR GDILVARSVE IAPEDTALTL NTKCFAAALD SFDTVISELE AGAQNRAPQT
     SDKRSYFGLK DRPAHHGTLD FSQTSAQILR LVRALDHGGY PNPVALPKLW TNGALFAIGQ
     AQTAEGRGQP GEVLSVADET ITIATSDGAV RLSGLQRLDG SGELPNAGTV LPEPPEDDLS
     DLARGEFHWR RALSGYIPAR LPGFGAPTGE TAQMTVSDIP PHALAALAAR LAPEGRADIA
     LVTLESVQRA ASGLALPWMP IAAHVEGPAD AFREQMTAKF NAARNAGPLA RDLGHRLAPA
     MSLATPAFAI SEGAGPLPGA LLTLETGATQ RLHYDAGAMT ASMAELLAAR LNQLAEWSGD
     MADAPLLSEA ERALTLETWN ATETPLADRT MLDRFEAAAQ EHPERVAVVF EDQSLSYADL
     DGLANRIAHL LQGAGAAAGA IVGLHLERGP RLVAAALGVL KAGAAYLPID PAYPAERQAH
     YLSDSGAAIV LTESAIARSL PRHAAKEIRL DIEPKLFSVP ATRPDPGPDA EALAYLIYTS
     GSTGTPKGVM VEHAQVANFF TGMDAVVPDA GNTWLAVTSL NFDISVLELF YALSRGYKVV
     MASENVASGV SSGARRASGM AMSLYYWGND DGTGRDKYRT LLEGAKFADA HGFTAVWTPE
     RHFHAFGGPY PNPSVTGAAV AGVTSRIGVR AGSCVAPLHH PARVAEEWAV IDNLTEGRAG
     LAIASGWQPD DFVLRPENAP PDNKRAMIES IDQIRRLWRG EAVAFPRADG SLHEVVTQPR
     PMSKELPLWI TTAGNPETWK EAGRLGANVL THLLGQSIDE VAEKIALYRQ ARAEAGFDPK
     TGEVALMLHT YLAETRDAAR EIAREPMKDY LRSAAGLIKQ YAWAFPAFKK PAGVTNPMQL
     DLGALEPDEL EAILDHAFER YFNESGLFGT IEDAEVRVAE VQAIGVSEIA CLIDYGIAPD
     TILEGLHPLA EVVSRVTGPD LPAEDDFSVA AQIRRHDATH LQCTPSLMRL MLADDGARAA
     LGSLSHVFLG GEALPGPLVA ALGKATDARV TNMYGPTETT IWSACGPASP GDGVVPVGAA
     IANTRLYVLD DAMEPQPIGA PGELWIGGAG VARGYWKRAA LTEERFRPDP FHGGRMYRTG
     DLVARRADGC LDFLGRADGQ VKLRGMRIEL GEVEARLEAL EGVRQAAAVV RDNRLLAFVT
     GDAGDETQMK ATLEARLPAH MVPARIVTLD ELPLTPNKKV DRARLPEPTE PKTTRPAPIP
     KDARPVRPAQ AGDAATLAEL GEVWSAVLGV SQIGGSDNFF ALGGHSLLAV ELFRAVRDRF
     GVTSFAITDV FRFPTLGGMA GRIGELRGDV PAPAERAAET PASPARNARA EARRAAMARR
     RQMRARQDS
//
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