Y3136_ARATH
ID Y3136_ARATH Reviewed; 330 AA.
AC Q9LIG0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Clavaminate synthase-like protein At3g21360;
DE EC=1.-.-.-;
GN OrderedLocusNames=At3g21360; ORFNames=MHC9_4;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-330, AND IRON-BINDING.
RX PubMed=16511070; DOI=10.1107/s1744309105011565;
RA Bitto E., Bingman C.A., Allard S.T.M., Wesenberg G.E., Aceti D.J.,
RA Wrobel R.L., Frederick R.O., Sreenath H., Vojtik F.C., Jeon W.B.,
RA Newman C.S., Primm J., Sussman M.R., Fox B.G., Markley J.L.,
RA Phillips G.N. Jr.;
RT "The structure at 2.4 A resolution of the protein from gene locus
RT At3g21360, a putative FeII/2-oxoglutarate-dependent enzyme from Arabidopsis
RT thaliana.";
RL Acta Crystallogr. F 61:469-472(2005).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 1 Fe cation per subunit.;
CC -!- MISCELLANEOUS: May use 2-oxoglutarate as a cosubstrate. {ECO:0000250}.
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DR EMBL; AP001305; BAB03049.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76500.1; -; Genomic_DNA.
DR EMBL; AK117772; BAC42419.1; -; mRNA.
DR RefSeq; NP_188773.1; NM_113031.2.
DR PDB; 1Y0Z; X-ray; 2.40 A; A/B=1-330.
DR PDB; 2Q4A; X-ray; 2.39 A; A/B=1-330.
DR PDBsum; 1Y0Z; -.
DR PDBsum; 2Q4A; -.
DR AlphaFoldDB; Q9LIG0; -.
DR SMR; Q9LIG0; -.
DR STRING; 3702.AT3G21360.1; -.
DR iPTMnet; Q9LIG0; -.
DR PaxDb; Q9LIG0; -.
DR PRIDE; Q9LIG0; -.
DR ProteomicsDB; 242541; -.
DR DNASU; 821690; -.
DR EnsemblPlants; AT3G21360.1; AT3G21360.1; AT3G21360.
DR GeneID; 821690; -.
DR Gramene; AT3G21360.1; AT3G21360.1; AT3G21360.
DR KEGG; ath:AT3G21360; -.
DR Araport; AT3G21360; -.
DR TAIR; locus:2089423; AT3G21360.
DR eggNOG; ENOG502QRUR; Eukaryota.
DR HOGENOM; CLU_044153_3_0_1; -.
DR InParanoid; Q9LIG0; -.
DR OMA; HNEQAYT; -.
DR OrthoDB; 868657at2759; -.
DR PhylomeDB; Q9LIG0; -.
DR EvolutionaryTrace; Q9LIG0; -.
DR PRO; PR:Q9LIG0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIG0; baseline and differential.
DR Genevisible; Q9LIG0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..330
FT /note="Clavaminate synthase-like protein At3g21360"
FT /id="PRO_0000220604"
FT BINDING 120
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 122
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 313
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1Y0Z"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2Q4A"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1Y0Z"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1Y0Z"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2Q4A"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2Q4A"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:2Q4A"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2Q4A"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:2Q4A"
SQ SEQUENCE 330 AA; 37212 MW; DE838BFFB70ADF2B CRC64;
MAELLLVETP IPQQKHYESK PFPAVISPPS ASIPIPALSL PLFTQTIKTQ KHYLDSLLHE
SGAVLFRGFP VNSADDFNDV VEAFGFDELP YVGGAAPRTS VVGRVFTANE SPPDQKIPFH
HEMAQVREFP SKLFFYCEIE PKCGGETPIV LSHVVYERMK DKHPEFVQRL EEHGLLYVRV
LGEDDDPSSP IGRGWKSTFL THDKNLAEQR AVDLGMKLEW TEDGGAKTVM GPIPAIKYDE
SRNRKVWFNS MVAAYTGWED KRNDPRKAVT FGDGKPLPAD IVHDCLRILE EECVAVPWQR
GDVLLIDNWA VLHSRRPFDP PRRVLASLCK
