ACH10_ARATH
ID ACH10_ARATH Reviewed; 362 AA.
AC Q9LSW6; Q94B41;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase homolog 10;
DE EC=1.14.-.-;
GN OrderedLocusNames=At5g43450; ORFNames=MWF20.16;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION BY LOW LIGHT.
RX PubMed=12972669; DOI=10.1104/pp.103.022665;
RA Vandenbussche F., Vriezen W.H., Smalle J., Laarhoven L.J.J., Harren F.J.M.,
RA Van Der Straeten D.;
RT "Ethylene and auxin control the Arabidopsis response to decreased light
RT intensity.";
RL Plant Physiol. 133:517-527(2003).
RN [6]
RP INDUCTION BY ETHYLENE.
RC STRAIN=cv. Columbia;
RX PubMed=15272873; DOI=10.1111/j.1365-313x.2004.02156.x;
RA De Paepe A., Vuylsteke M., Van Hummelen P., Zabeau M., Van Der Straeten D.;
RT "Transcriptional profiling by cDNA-AFLP and microarray analysis reveals
RT novel insights into the early response to ethylene in Arabidopsis.";
RL Plant J. 39:537-559(2004).
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- INDUCTION: By ethylene. Slightly induced in leaf blades in low light
CC intensities. {ECO:0000269|PubMed:12972669,
CC ECO:0000269|PubMed:15272873}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB025638; BAA97424.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94965.1; -; Genomic_DNA.
DR EMBL; AY042870; AAK68810.1; -; mRNA.
DR EMBL; BT015042; AAT70493.1; -; mRNA.
DR RefSeq; NP_199158.1; NM_123711.4.
DR AlphaFoldDB; Q9LSW6; -.
DR SMR; Q9LSW6; -.
DR STRING; 3702.AT5G43450.1; -.
DR PaxDb; Q9LSW6; -.
DR PRIDE; Q9LSW6; -.
DR ProteomicsDB; 244349; -.
DR EnsemblPlants; AT5G43450.1; AT5G43450.1; AT5G43450.
DR GeneID; 834365; -.
DR Gramene; AT5G43450.1; AT5G43450.1; AT5G43450.
DR KEGG; ath:AT5G43450; -.
DR Araport; AT5G43450; -.
DR TAIR; locus:2176466; AT5G43450.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_0_0_1; -.
DR InParanoid; Q9LSW6; -.
DR OMA; PSLACHY; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q9LSW6; -.
DR BioCyc; ARA:AT5G43450-MON; -.
DR PRO; PR:Q9LSW6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSW6; baseline and differential.
DR Genevisible; Q9LSW6; AT.
DR GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..362
FT /note="1-aminocyclopropane-1-carboxylate oxidase homolog
FT 10"
FT /id="PRO_0000408285"
FT DOMAIN 211..310
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 301
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 175
FT /note="V -> A (in Ref. 3; AAK68810)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="T -> A (in Ref. 3; AAK68810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40875 MW; 623E2C9949A9CC86 CRC64;
MTENSEKIDR LNDLTTFIST KTGVKGLVDA EITEVPSMFH VPSSILSNNR PSDISGLNLT
VPIIDLGDRN TSSRNVVISK IKDAAENWGF FQVINHDVPL TVLEEIKESV RRFHEQDPVV
KNQYLPTDNN KRFVYNNDFD LYHSSPLNWR DSFTCYIAPD PPNPEEIPLA CRSAVIEYTK
HVMELGAVLF QLLSEALGLD SETLKRIDCL KGLFMLCHYY PPCPQPDLTL GISKHTDNSF
LTLLLQDQIG GLQVLHEDYW VDVPPVPGAL VVNIGDFMQL ITNDKFLSVE HRVRPNKDRP
RISVACFFSS SLSPNSTVYG PIKDLLSDEN PAKYKDITIP EYTAGFLASI FDEKSYLTNY
MI
