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ACCH1_ARATH
ID   ACCH1_ARATH             Reviewed;         365 AA.
AC   Q84MB3; Q9SHK4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase homolog 1;
GN   OrderedLocusNames=At1g06620; ORFNames=F12K11.24, F12K11.6;
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.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF24827.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g06630 has been split into 4 genes: At1g06620, At1g06630, At1g06640 and At1g06650.; Evidence={ECO:0000305};
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DR   EMBL; AC007592; AAF24827.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28010.1; -; Genomic_DNA.
DR   EMBL; BT006430; AAP21238.1; -; mRNA.
DR   EMBL; AK227676; BAE99663.1; -; mRNA.
DR   PIR; D86201; D86201.
DR   RefSeq; NP_172147.2; NM_100539.3.
DR   AlphaFoldDB; Q84MB3; -.
DR   SMR; Q84MB3; -.
DR   BioGRID; 22412; 1.
DR   STRING; 3702.AT1G06620.1; -.
DR   PaxDb; Q84MB3; -.
DR   PRIDE; Q84MB3; -.
DR   ProteomicsDB; 244540; -.
DR   EnsemblPlants; AT1G06620.1; AT1G06620.1; AT1G06620.
DR   GeneID; 837171; -.
DR   Gramene; AT1G06620.1; AT1G06620.1; AT1G06620.
DR   KEGG; ath:AT1G06620; -.
DR   Araport; AT1G06620; -.
DR   TAIR; locus:2009130; AT1G06620.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_0_0_1; -.
DR   OMA; VKRELYT; -.
DR   OrthoDB; 755305at2759; -.
DR   PhylomeDB; Q84MB3; -.
DR   BioCyc; ARA:AT1G06620-MON; -.
DR   PRO; PR:Q84MB3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q84MB3; baseline and differential.
DR   Genevisible; Q84MB3; AT.
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..365
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase homolog 1"
FT                   /id="PRO_0000274937"
FT   DOMAIN          212..313
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         240
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         294
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   365 AA;  40351 MW;  77AFD66C6EF1BBC6 CRC64;
     MESSLPQVAA LDRSTLLKAF DETKTGVKGL IDAGITEIPS IFRAPPATLT SPKPPSSSDF
     SIPTIDLKGG GTDSITRRSL VEKIGDAAEK WGFFQVINHG IPMDVLEKMI DGIREFHEQD
     TEVKKGFYSR DPASKMVYSS NFDLFSSPAA NWRDTLGCYT APDPPRPEDL PATCGEMMIE
     YSKEVMKLGK LLFELLSEAL GLNTNHLKDM DCTNSLLLLG HYYPPCPQPD LTLGLTKHSD
     NSFLTILLQD HIGGLQVLHD QYWVDVPPVP GALVVNVGDL LQLITNDKFI SVEHRVLANV
     AGPRISVACF FSSYLMANPR VYGPIKEILS EENPPNYRDT TITEYAKFYR SKGFDGTSGL
     LYLKI
 
 
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