ID A0A150G6X5_GONPE Unreviewed; 1405 AA.
AC A0A150G6X5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Flavin-containing monooxygenase {ECO:0000256|RuleBase:RU361177};
DE EC=1.-.-.- {ECO:0000256|RuleBase:RU361177};
GN ORFNames=GPECTOR_53g109 {ECO:0000313|EMBL:KXZ45523.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ45523.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + indole-3-pyruvate + NADPH + O2 = (indol-3-yl)acetate +
CC CO2 + H2O + NADP(+); Xref=Rhea:RHEA:34331, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17640, ChEBI:CHEBI:30854, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.168;
CC Evidence={ECO:0000256|ARBA:ARBA00035920};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU361177};
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|RuleBase:RU361177}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXZ45523.1}.
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DR EMBL; LSYV01000054; KXZ45523.1; -; Genomic_DNA.
DR STRING; 33097.A0A150G6X5; -.
DR OrthoDB; 5487623at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:RHEA.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR43539:SF78; FAD-DEPENDENT OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR43539; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_4G09220); 1.
DR Pfam; PF00743; FMO-like; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU361177};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361177};
KW Monooxygenase {ECO:0000256|RuleBase:RU361177};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361177};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT REGION 87..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1049..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1405 AA; 141545 MW; 5615F960AFA11C59 CRC64;
MCYVHYVLPQ VVVLEQSEDV GGVWIRNYQG FGLQVPWELY QFPEFPYPRK AELGEYPAGD
AVGEYVRAYA RHFELYRHIL FSCRLPPSQP QAQAQDSRGI TPVQQQRQQQ QQAPGAAATA
HPAPAPSSRL RRLLRPSWGH NPGTGGAHNA GELTGGGGGA GEGGLLKRSH TSTGPGTGPG
TGTGACASPS TCRCTGNTGC PSSCACSSPS ATSSAFRVDG RVGSCCGGQA ASPASAQPRL
SSEASGSGPT RGPGGKAGRQ LPPKLPGLLE ECPEGWDAVY EDSSTGRQYT LHVSFVVLCT
GLYASPFIPT IPGQELYRGL QVHSRDFTDA SVAAGKRVLV VGAGKTAADI VTELTATRTA
AAVTLLYRRP HWPLPRFVGP VSLKLLAYTR LLSIALLPAY YDAGPGGRFA AALLTPLRKA
FWVRFMGRVN SALGVKKTLG VPDRPICQDI WYSGQVVDAA RWPEVIHNPK VHALQGEVDY
FTPVSAVLRD GTELQTDIVL YATGYSAHYG FLEPEAREAL EVQHDGLYLY RHVLAPGLPG
LAFVGAEVST FNNILTAALQ AEWLAAALGG VLALPPRAAM AADVAAQQSW RRATMPPHKL
RGSAVMLYMQ CYHDQLLRDM GAPTHRKRPT WRHPLAECLQ PYTAQDYADL FDTSAAAAAA
TAAAAMAAAA AGCGDAPRAG VVGPEAEAEA EEEPVVVAGR MSSALAPDDA AAAAMVLSNA
AGWSSGAGAA VATATATVLA TAGASGSAAA TATATATGSS PSHRVSHTTT LAAAFSSHSP
SPSNAHVHPE SRLQADGRSP QPRPAPSPSP DPGGHGLAAA AAASADPAPA RGLALRVPGA
DAAVCGLASR SSGAQPLTPV QESANAPRPA SPIAAAGWVQ DNLPAAASQP GPAAALPMSG
LAGGDVVAAA ATAAAADAAA AAAAEDFEAM GEEEGEPDEQ DTLYSLDALP PALQAFRGRT
RALPSAPAAA PSPPTVRSPL PAPAGRSDRR AYSHTASGYA AIPAGGQPGP GVRAGRKSGG
DSLPGSGCSR GNSAVLEAWG SSVVAGGGPA GGSGAGGAGR RDAGGEAARA LGRGSLPAAS
SATGGPMRSM HSAGSDGLVM GRADSGIEGA GSGGVCDGSS GGARRRGPVK RGFSLATLLL
LKRRGVNTDA YDVSSSRIEQ SSPAVAALAY KVLPPRHVEE ALAAAATAAA GGTPSPAQRK
PANAGPGVGV GGRAPRGAAQ QVPPRLGPQN SPAAASAPPS TADTSLFSDD AMLPGLPGCT
VGAPLTAAAA AADRPGAVAF RAAAPSISAS SGISYTPSCS TVAPPQLVLA AADAASAAYD
NRTSYDAGSE TSYTRALRAA ADALTAGAAG GRGAPGGGGR VGRGYGGADS FTSPARSDSS
STSSGVSYVP SCSTVAPPFA QQRYE
//
