ACCH6_ARATH
ID ACCH6_ARATH Reviewed; 360 AA.
AC P93824;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase homolog 6;
DE EC=1.14.-.-;
GN OrderedLocusNames=At1g04350; ORFNames=F19P19.22;
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 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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
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).
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 -!- TISSUE SPECIFICITY: Constitutively expressed in leaves and blades.
CC {ECO:0000269|PubMed:12972669}.
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; AC000104; AAB70442.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27687.1; -; Genomic_DNA.
DR EMBL; AY050921; AAK93598.1; -; mRNA.
DR EMBL; AY113969; AAM45017.1; -; mRNA.
DR EMBL; BT000698; AAN31842.1; -; mRNA.
DR EMBL; AK226341; BAE98490.1; -; mRNA.
DR PIR; A86175; A86175.
DR RefSeq; NP_171930.1; NM_100315.4.
DR AlphaFoldDB; P93824; -.
DR SMR; P93824; -.
DR STRING; 3702.AT1G04350.1; -.
DR iPTMnet; P93824; -.
DR PaxDb; P93824; -.
DR PRIDE; P93824; -.
DR ProteomicsDB; 243278; -.
DR EnsemblPlants; AT1G04350.1; AT1G04350.1; AT1G04350.
DR GeneID; 839542; -.
DR Gramene; AT1G04350.1; AT1G04350.1; AT1G04350.
DR KEGG; ath:AT1G04350; -.
DR Araport; AT1G04350; -.
DR TAIR; locus:2018349; AT1G04350.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_0_0_1; -.
DR InParanoid; P93824; -.
DR OMA; SSSCVNW; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; P93824; -.
DR BioCyc; ARA:AT1G04350-MON; -.
DR PRO; PR:P93824; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93824; baseline and differential.
DR Genevisible; P93824; AT.
DR GO; GO:0005576; C:extracellular region; 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; 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..360
FT /note="1-aminocyclopropane-1-carboxylate oxidase homolog 6"
FT /id="PRO_0000408281"
FT DOMAIN 208..309
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 299
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 360 AA; 40797 MW; 7F0BB863EAAEB1DA CRC64;
METKEFDSYS ERKAFDETKT GVKGLIDAHI TEIPRIFCLP QGSLSDKKPF VSTTDFAIPI
IDFEGLHVSR EDIVGKIKDA ASNWGFFQVI NHGVPLNVLQ EIQDGVRRFH EEAPEVKKTY
FTRDATKRFV YNSNFDLYSS SSCVNWRDSF ACYMAPDPPN PEDLPVACRV AMFEYSKHMM
RLGDLLFELL SEALGLRSDK LKSMDCMKGL LLLCHYYPPC PQPDLTIGTN NHSDNSFLTI
LLQDQIGGLQ IFHQDCWVDV SPIPGALVIN MGDFLQLITN DKVISVEHRV LANRAATPRI
SVASFFSTSM RPNSTVYGPI KELLSEENPS KYRVIDLKEY TEGYFKKGLD GTSYLSHYKI
