ACCH3_ARATH
ID ACCH3_ARATH Reviewed; 369 AA.
AC Q8H1S4; Q3EDH6; Q94K40; Q9SHK4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase homolog 3;
GN OrderedLocusNames=At1g06650; ORFNames=F12K11.26, 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] (ISOFORM 1).
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).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H1S4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H1S4-2; Sequence=VSP_022947;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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; AEE28018.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28019.1; -; Genomic_DNA.
DR EMBL; AY142493; AAN13044.1; -; mRNA.
DR EMBL; AF370322; AAK44137.1; -; mRNA.
DR PIR; D86201; D86201.
DR RefSeq; NP_172150.1; NM_100542.4. [Q8H1S4-1]
DR RefSeq; NP_849602.1; NM_179271.2. [Q8H1S4-2]
DR AlphaFoldDB; Q8H1S4; -.
DR SMR; Q8H1S4; -.
DR STRING; 3702.AT1G06650.2; -.
DR iPTMnet; Q8H1S4; -.
DR PaxDb; Q8H1S4; -.
DR PRIDE; Q8H1S4; -.
DR ProteomicsDB; 244347; -. [Q8H1S4-1]
DR EnsemblPlants; AT1G06650.1; AT1G06650.1; AT1G06650. [Q8H1S4-2]
DR EnsemblPlants; AT1G06650.2; AT1G06650.2; AT1G06650. [Q8H1S4-1]
DR GeneID; 837175; -.
DR Gramene; AT1G06650.1; AT1G06650.1; AT1G06650. [Q8H1S4-2]
DR Gramene; AT1G06650.2; AT1G06650.2; AT1G06650. [Q8H1S4-1]
DR KEGG; ath:AT1G06650; -.
DR Araport; AT1G06650; -.
DR TAIR; locus:2009175; AT1G06650.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_0_0_1; -.
DR OMA; TTYCSMA; -.
DR PhylomeDB; Q8H1S4; -.
DR BioCyc; ARA:AT1G06650-MON; -.
DR PRO; PR:Q8H1S4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H1S4; baseline and differential.
DR Genevisible; Q8H1S4; 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 Alternative splicing; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..369
FT /note="1-aminocyclopropane-1-carboxylate oxidase homolog 3"
FT /id="PRO_0000274939"
FT DOMAIN 217..318
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 241
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT VAR_SEQ 286..369
FT /note="LITNDKFISLEHRVLANRATRARVSVACFFTTGVRPNPRMYGPIRELVSEEN
FT PPKYRETTIKDYATYFNAKGLDGTSALLHFKI -> FGAQSIGEQSNKSSSVCRMFLYH
FT WSKTES (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_022947"
FT CONFLICT 57
FT /note="D -> G (in Ref. 3; AAK44137)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 42020 MW; B95BCB7EBEC39EB1 CRC64;
MEMMKIDPLF DRASELKAFD ETKTGVKGLV DSGVSQVPRI FHHPTVKLST PKPLPSDLLH
LKTIPTIDLG GRDFQDAIKR NNAIEEIKEA AAKWGFFQVI NHGVSLELLE KMKKGVRDFH
EQSQEVRKEF YSRDFSRRFL YLSNFDLFSS PAANWRDTFS CTMAPDTPKP QDLPEICRDI
MMEYSKQVMN LGKFLFELLS EALGLEPNHL NDMDCSKGLL MLSHYYPPCP EPDLTLGTSQ
HSDNSFLTVL LPDQIEGLQV RREGHWFDVP HVSGALIINI GDLLQLITND KFISLEHRVL
ANRATRARVS VACFFTTGVR PNPRMYGPIR ELVSEENPPK YRETTIKDYA TYFNAKGLDG
TSALLHFKI
