ACCO5_ARATH
ID ACCO5_ARATH Reviewed; 307 AA.
AC Q0WPW4; Q8LCA2; Q9FVX5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 5;
DE Short=ACC oxidase 5;
DE Short=AtACO5;
DE EC=1.14.17.4;
GN OrderedLocusNames=At1g77330; ORFNames=F2P24.4;
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=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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Enzyme involved in the ethylene biosynthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-aminocyclopropane-1-carboxylate + L-ascorbate + O2 = CO2 +
CC ethene + 2 H2O + hydrogen cyanide + L-dehydroascorbate;
CC Xref=Rhea:RHEA:23640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18153, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58360, ChEBI:CHEBI:58539;
CC EC=1.14.17.4;
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 -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG29196.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC078898; AAG29196.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35965.1; -; Genomic_DNA.
DR EMBL; BT026444; ABH04551.1; -; mRNA.
DR EMBL; AK228946; BAF00835.1; -; mRNA.
DR EMBL; AY086710; AAM63764.1; -; mRNA.
DR PIR; C96802; C96802.
DR RefSeq; NP_565154.1; NM_106382.3.
DR AlphaFoldDB; Q0WPW4; -.
DR SMR; Q0WPW4; -.
DR STRING; 3702.AT1G77330.1; -.
DR PaxDb; Q0WPW4; -.
DR PRIDE; Q0WPW4; -.
DR ProteomicsDB; 244367; -.
DR EnsemblPlants; AT1G77330.1; AT1G77330.1; AT1G77330.
DR GeneID; 844069; -.
DR Gramene; AT1G77330.1; AT1G77330.1; AT1G77330.
DR KEGG; ath:AT1G77330; -.
DR Araport; AT1G77330; -.
DR TAIR; locus:2031422; AT1G77330.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR InParanoid; Q0WPW4; -.
DR OMA; MGEYREE; -.
DR OrthoDB; 755305at2759; -.
DR PhylomeDB; Q0WPW4; -.
DR BioCyc; ARA:AT1G77330-MON; -.
DR UniPathway; UPA00384; UER00563.
DR PRO; PR:Q0WPW4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WPW4; baseline and differential.
DR Genevisible; Q0WPW4; AT.
DR GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; ISS:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009693; P:ethylene biosynthetic process; TAS:TAIR.
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 Coiled coil; Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Plant defense; Reference proteome; Vitamin C.
FT CHAIN 1..307
FT /note="1-aminocyclopropane-1-carboxylate oxidase 5"
FT /id="PRO_0000408300"
FT DOMAIN 152..256
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT COILED 106..134
FT /evidence="ECO:0000255"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 182
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 247
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 107
FT /note="N -> K (in Ref. 5; AAM63764)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="L -> V (in Ref. 5; AAM63764)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> T (in Ref. 5; AAM63764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 34947 MW; F1B751D7F35E612A CRC64;
MAIPVIDFSK LNGEEREKTL SEIARACEEW GFFQLVNHGI PLELLNKVKK LSSDCYKTER
EEAFKTSNPV KLLNELVQKN SGEKLENVDW EDVFTLLDHN QNEWPSNIKE TMGEYREEVR
KLASKMMEVM DENLGLPKGY IKKAFNEGME DGEETAFFGT KVSHYPPCPH PELVNGLRAH
TDAGGVVLLF QDDEYDGLQV LKDGEWIDVQ PLPNAIVINT GDQIEVLSNG RYKSAWHRVL
AREEGNRRSI ASFYNPSYKA AIGPAAVAEE EGSEKKYPKF VFGDYMDVYA NQKFMPKEPR
FLAVKSL
