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YUC5_ARATH
ID   YUC5_ARATH              Reviewed;         424 AA.
AC   Q9LKC0;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Probable indole-3-pyruvate monooxygenase YUCCA5;
DE            EC=1.14.13.168;
DE   AltName: Full=Flavin-containing monooxygenase YUCCA5;
DE   AltName: Full=Protein SUPPRESSOR OF ER 1;
GN   Name=YUC5; Synonyms=SUPER1, YUCCA5; OrderedLocusNames=At5g43890;
GN   ORFNames=F6B6.3;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=16126863; DOI=10.1104/pp.105.063495;
RA   Woodward C., Bemis S.M., Hill E.J., Sawa S., Koshiba T., Torii K.U.;
RT   "Interaction of auxin and ERECTA in elaborating Arabidopsis inflorescence
RT   architecture revealed by the activation tagging of a new member of the
RT   YUCCA family putative flavin monooxygenases.";
RL   Plant Physiol. 139:192-203(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16818609; DOI=10.1101/gad.1415106;
RA   Cheng Y., Dai X., Zhao Y.;
RT   "Auxin biosynthesis by the YUCCA flavin monooxygenases controls the
RT   formation of floral organs and vascular tissues in Arabidopsis.";
RL   Genes Dev. 20:1790-1799(2006).
RN   [6]
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   [7]
RP   FUNCTION.
RX   PubMed=22025721; DOI=10.1073/pnas.1108436108;
RA   Won C., Shen X., Mashiguchi K., Zheng Z., Dai X., Cheng Y., Kasahara H.,
RA   Kamiya Y., Chory J., Zhao Y.;
RT   "Conversion of tryptophan to indole-3-acetic acid by TRYPTOPHAN
RT   AMINOTRANSFERASES OF ARABIDOPSIS and YUCCAs in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:18518-18523(2011).
CC   -!- FUNCTION: Involved in auxin biosynthesis. Belongs to the set of
CC       redundant YUCCA genes probably responsible for auxin biosynthesis in
CC       roots. {ECO:0000269|PubMed:16126863, ECO:0000269|PubMed:22025721}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in roots and young
CC       vegetative tissues, while it was under detectable levels in
CC       reproductive tissues, such as inflorescence stems, pedicels, and floral
CC       buds. {ECO:0000269|PubMed:16126863}.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR   EMBL; DQ159070; AAZ93924.1; -; mRNA.
DR   EMBL; AP000368; BAA98069.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95021.1; -; Genomic_DNA.
DR   EMBL; BT029743; ABM06013.1; -; mRNA.
DR   RefSeq; NP_199202.1; NM_123756.2.
DR   AlphaFoldDB; Q9LKC0; -.
DR   SMR; Q9LKC0; -.
DR   BioGRID; 19661; 4.
DR   IntAct; Q9LKC0; 4.
DR   STRING; 3702.AT5G43890.1; -.
DR   PaxDb; Q9LKC0; -.
DR   PRIDE; Q9LKC0; -.
DR   EnsemblPlants; AT5G43890.1; AT5G43890.1; AT5G43890.
DR   GeneID; 834411; -.
DR   Gramene; AT5G43890.1; AT5G43890.1; AT5G43890.
DR   KEGG; ath:AT5G43890; -.
DR   Araport; AT5G43890; -.
DR   TAIR; locus:2149524; AT5G43890.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_006909_2_0_1; -.
DR   InParanoid; Q9LKC0; -.
DR   OMA; NKFEITP; -.
DR   OrthoDB; 405736at2759; -.
DR   PhylomeDB; Q9LKC0; -.
DR   UniPathway; UPA00151; -.
DR   PRO; PR:Q9LKC0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LKC0; baseline and differential.
DR   Genevisible; Q9LKC0; AT.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0103075; F:indole-3-pyruvate monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004497; F:monooxygenase activity; ISS:TAIR.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009851; P:auxin biosynthetic process; IMP:TAIR.
DR   GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   Pfam; PF00743; FMO-like; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   Auxin biosynthesis; FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..424
FT                   /note="Probable indole-3-pyruvate monooxygenase YUCCA5"
FT                   /id="PRO_0000400072"
FT   BINDING         29..34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         199..204
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   424 AA;  47442 MW;  EAD8EA86C7D5260A CRC64;
     MENMFRLMGS EDSSDRRRCI WVNGPVIVGA GPSGLATAAC LREEGVPFVV LERADCIASL
     WQKRTYDRIK LHLPKKVCQL PKMPFPEDYP EYPTKRQFIE YLESYANKFE ITPQFNECVQ
     SARYDETSGL WRIKTTSSSS SGSEMEYICR WLVVATGENA EKVVPEIDGL TTEFEGEVIH
     SCEYKSGEKY RGKSVLVVGC GNSGMEVSLD LANHNANASM VVRSSVHVLP REILGKSSFE
     ISMMLMKWFP LWLVDKILLI LAWLILGNLT KYGLKRPTMG PMELKIVSGK TPVLDIGAME
     KIKSGEVEIV PGIKRFSRSH VELVDGQRLD LDAVVLATGY RSNVPSWLQE NDLFSKNGFP
     KSPFPNAWKG KSGLYAAGFT RKGLAGASAD AVNIAQDIGN VWREETKRQK MRTRVGHRRC
     ISVA
 
 
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