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GSXL8_ARATH
ID   GSXL8_ARATH             Reviewed;         461 AA.
AC   Q9FLK4;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Flavin-containing monooxygenase FMO GS-OX-like 8 {ECO:0000303|PubMed:17461789};
DE            EC=1.8.-.- {ECO:0000305};
DE   AltName: Full=Flavin-monooxygenase glucosinolate S-oxygenase-like 8 {ECO:0000303|PubMed:17461789};
GN   OrderedLocusNames=At5g61290 {ECO:0000312|Araport:AT5G61290};
GN   ORFNames=MFB13.9 {ECO:0000312|EMBL:BAB08484.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
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).
RN   [6]
RP   INTERACTION WITH EER5.
RX   PubMed=19843313; DOI=10.1111/j.1365-313x.2009.04048.x;
RA   Lu Q., Tang X., Tian G., Wang F., Liu K., Nguyen V., Kohalmi S.E.,
RA   Keller W.A., Tsang E.W., Harada J.J., Rothstein S.J., Cui Y.;
RT   "Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components
RT   and anchoring nucleoporin.";
RL   Plant J. 61:259-270(2010).
CC   -!- FUNCTION: Catalyzes the conversion of methylthioalkyl glucosinolates of
CC       any chain length into methylsulfinylalkyl glucosinolates.
CC       {ECO:0000250|UniProtKB:Q9SS04}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Interacts with EER5. {ECO:0000269|PubMed:19843313}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR   EMBL; AB010073; BAB08484.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97448.1; -; Genomic_DNA.
DR   EMBL; AK117661; BAC42314.1; -; mRNA.
DR   EMBL; BT006095; AAP04080.1; -; mRNA.
DR   RefSeq; NP_200937.1; NM_125522.4.
DR   AlphaFoldDB; Q9FLK4; -.
DR   SMR; Q9FLK4; -.
DR   BioGRID; 21494; 1.
DR   IntAct; Q9FLK4; 1.
DR   STRING; 3702.AT5G61290.1; -.
DR   PaxDb; Q9FLK4; -.
DR   PRIDE; Q9FLK4; -.
DR   ProteomicsDB; 247229; -.
DR   EnsemblPlants; AT5G61290.1; AT5G61290.1; AT5G61290.
DR   GeneID; 836250; -.
DR   Gramene; AT5G61290.1; AT5G61290.1; AT5G61290.
DR   KEGG; ath:AT5G61290; -.
DR   Araport; AT5G61290; -.
DR   TAIR; locus:2163193; AT5G61290.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_3_3_1; -.
DR   InParanoid; Q9FLK4; -.
DR   OMA; ASCKKVC; -.
DR   OrthoDB; 405736at2759; -.
DR   PhylomeDB; Q9FLK4; -.
DR   BioCyc; ARA:AT5G61290-MON; -.
DR   PRO; PR:Q9FLK4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLK4; baseline and differential.
DR   Genevisible; Q9FLK4; 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   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   Pfam; PF00743; FMO-like; 2.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..461
FT                   /note="Flavin-containing monooxygenase FMO GS-OX-like 8"
FT                   /id="PRO_0000401963"
FT   BINDING         20..25
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         220..225
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   461 AA;  52407 MW;  EFC61B6D7AFB49BC CRC64;
     MVLVITEPIK SQSKTVCVIG AGPSGLVSAR ELKKEGHKVV VMEQNHDVGG QWLYQPNVDE
     EDTLGKTKTL KVHSSVYSSL RLASPREVMG FSDFPFIAKE GRDSRRFPGH EELLLYLKDF
     CQVFGLREMI RFNVRVEFVG MVNEDDDDDD DVKKWMVKSV KKSGEVMEEV FDAVVVASGH
     YSYPRLPTIK GMDLWKRKQL HSHIYRVPEP FCDEVVVVVG CSMSGQDISI ELVEVAKEVH
     LSTKSLDIPP GLSKVIEKHQ NLHLHPQIES LEEDGRVIFE DGSCIVADTI LYCTGYEYKF
     PFLESKGRVE IDDNRVGPLF EHTFSPSLSP FLSFVGIPRK LIGFPFFESQ AKWIAKLLSG
     KTSLPSSDQM MQSISDFYLA READGIPKRN THDIADFNYS DKYADYIGFP HLEEWRKVLC
     LSAILNSIEN LETYRDSWDD DDLLQETLQD PYFTQLSIPS V
 
 
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