FMO1_ARATH
ID FMO1_ARATH Reviewed; 530 AA.
AC Q9LMA1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable flavin-containing monooxygenase 1;
DE EC=1.14.13.-;
GN Name=FMO1; OrderedLocusNames=At1g19250; ORFNames=T29M8.12;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP FUNCTION.
RX PubMed=16856982; DOI=10.1111/j.1365-313x.2006.02813.x;
RA Koch M., Vorwerk S., Masur C., Sharifi-Sirchi G., Olivieri N.,
RA Schlaich N.L.;
RT "A role for a flavin-containing mono-oxygenase in resistance against
RT microbial pathogens in Arabidopsis.";
RL Plant J. 47:629-639(2006).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=16778014; DOI=10.1104/pp.106.081257;
RA Mishina T.E., Zeier J.;
RT "The Arabidopsis flavin-dependent monooxygenase FMO1 is an essential
RT component of biologically induced systemic acquired resistance.";
RL Plant Physiol. 141:1666-1675(2006).
RN [5]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=17461789; DOI=10.1111/j.1365-313x.2007.03101.x;
RA Hansen B.G., Kliebenstein D.J., Halkier B.A.;
RT "Identification of a flavin-monooxygenase as the S-oxygenating enzyme in
RT aliphatic glucosinolate biosynthesis in Arabidopsis.";
RL Plant J. 50:902-910(2007).
CC -!- FUNCTION: Required for the establishment of systemic acquired
CC resistance (SAR). Not involved in local defense mechanisms. Confers a
CC salicylic acid-dependent (SA) resistance to virulent pathogens such as
CC P.syringae pv tomato and H.parasitica. {ECO:0000269|PubMed:16778014,
CC ECO:0000269|PubMed:16856982}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- INDUCTION: Locally and systemically up-regulated by the bacterial
CC pathogen P.syringae. {ECO:0000269|PubMed:16778014}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AC069143; AAF82235.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29823.1; -; Genomic_DNA.
DR PIR; B86326; B86326.
DR RefSeq; NP_173359.3; NM_101783.4.
DR AlphaFoldDB; Q9LMA1; -.
DR SMR; Q9LMA1; -.
DR STRING; 3702.AT1G19250.1; -.
DR PaxDb; Q9LMA1; -.
DR PRIDE; Q9LMA1; -.
DR EnsemblPlants; AT1G19250.1; AT1G19250.1; AT1G19250.
DR GeneID; 838508; -.
DR Gramene; AT1G19250.1; AT1G19250.1; AT1G19250.
DR KEGG; ath:AT1G19250; -.
DR Araport; AT1G19250; -.
DR TAIR; locus:2202155; AT1G19250.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_9_3_1; -.
DR InParanoid; Q9LMA1; -.
DR OMA; ICQEMGW; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q9LMA1; -.
DR BioCyc; ARA:AT1G19250-MON; -.
DR BioCyc; MetaCyc:AT1G19250-MON; -.
DR BRENDA; 1.14.13.8; 399.
DR PRO; PR:Q9LMA1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMA1; baseline and differential.
DR Genevisible; Q9LMA1; AT.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IMP:TAIR.
DR GO; GO:0062047; F:pipecolic acid N-hydroxylase; IMP:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0062034; P:L-pipecolic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IDA:TAIR.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Plant defense;
KW Reference proteome.
FT CHAIN 1..530
FT /note="Probable flavin-containing monooxygenase 1"
FT /id="PRO_0000249421"
FT BINDING 17..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 46..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 58..59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 219..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
SQ SEQUENCE 530 AA; 60396 MW; 83A5840059071816 CRC64;
MASNYDKLTS SRVAIIGAGV SGLAAAKNLV HHNPTVFEAS DSVGGVWRSC TYETTKLQSA
RVDYEFSDFP WPNNRDDTTF PPYLEILDYL ESYAKHFDLL KFMKFGSKVI EVRFIGDGET
PQMVDLGAYG NLLPGKPVWE VAVQIGDSGD IQWHAFEFVV VCTGKYGDVP RIPAFPAKKG
PEMFQGKVMH SMDYCKLEKE EASTLLSGKK VAVIGFKKSA IDLALESALA NQGEGGKACT
MVVRTTHWGI PHYWVWGLPF FLFYSSRASQ FLHDRPNQSF LRTLFCLLFS LLRAVVSKFI
ESYVLWKLPL EKYGLKPNHS FEEDYASCQM AIIPENFFEE ADKGMIRFKK SSKWWFYEEG
IVFEDGTTLE ADVVILATGY DGKKKLKAIV PEPFRTWLEF PSGVMPLYRG TIHPLIPNMG
FVGYVQSSSN LHTSELRSMW LSRLVDEKFR LPSKEKMLDQ FLKEMEVTRN SSRFYKRHCI
STFSIQHADD MCNDMGLNPW RKSNFLLEAF SPYGSQDYRL GQEEKEDMTA
