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ACCH5_ARATH
ID   ACCH5_ARATH             Reviewed;         398 AA.
AC   Q43383; Q9LR82;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase homolog 5;
DE            EC=1.14.-.-;
GN   Name=2A6; OrderedLocusNames=At1g03410; ORFNames=F21B7.3;
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 [MRNA] OF 35-398, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia; TISSUE=Etiolated seedling;
RX   PubMed=7579161; DOI=10.1007/bf00019127;
RA   Trentmann S.M., Kende H.;
RT   "Analysis of Arabidopsis cDNA that shows homology to the tomato E8 cDNA.";
RL   Plant Mol. Biol. 29:161-166(1995).
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: Expressed in etiolated seedlings, leaves, stems and
CC       flowers. {ECO:0000269|PubMed:7579161}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF86540.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g03410 has been split into 2 genes: At1g03400 and At1g03410.; Evidence={ECO:0000305};
CC       Sequence=BAE98763.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA58151.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC002560; AAF86540.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27569.1; -; Genomic_DNA.
DR   EMBL; AK226654; BAE98763.1; ALT_INIT; mRNA.
DR   EMBL; X83096; CAA58151.1; ALT_INIT; mRNA.
DR   PIR; S59548; S59548.
DR   RefSeq; NP_001323192.1; NM_001331410.1.
DR   RefSeq; NP_171840.2; NM_100223.3.
DR   AlphaFoldDB; Q43383; -.
DR   SMR; Q43383; -.
DR   PaxDb; Q43383; -.
DR   PRIDE; Q43383; -.
DR   ProteomicsDB; 244356; -.
DR   EnsemblPlants; AT1G03410.1; AT1G03410.1; AT1G03410.
DR   GeneID; 838763; -.
DR   Gramene; AT1G03410.1; AT1G03410.1; AT1G03410.
DR   KEGG; ath:AT1G03410; -.
DR   Araport; AT1G03410; -.
DR   TAIR; locus:2020798; AT1G03410.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_0_0_1; -.
DR   InParanoid; Q43383; -.
DR   OrthoDB; 755305at2759; -.
DR   PRO; PR:Q43383; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q43383; baseline and differential.
DR   Genevisible; Q43383; 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..398
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase homolog 5"
FT                   /id="PRO_0000408280"
FT   DOMAIN          247..347
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         271
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         273
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         327
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         338
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   398 AA;  44846 MW;  BFF7C5A6BC08D8CB CRC64;
     MGHDSFCYLI VLRCALRCGI IALMQICALQ KKERRSKMES SDRSSQAKAF DETKTGVKGL
     VASGIKEIPA MFHTPPDTLT SLKQTAPPSQ QLTIPTVDLK GGSMDLISRR SVVEKIGDAA
     ERWGFFQVVN HGISVEVMER MKEGIRRFHE QDPEVKKRFY SRDHTRDVLY YSNIDLHTCN
     KAANWRDTLA CYMAPDPPKL QDLPAVCGEI MMEYSKQLMT LGEFLFELLS EALGLNPNHL
     KDMGCAKSHI MFGQYYPPCP QPDLTLGISK HTDFSFITIL LQDNIGGLQV IHDQCWVDVS
     PVPGALVINI GDLLQLISND KFISAEHRVI ANGSSEPRIS MPCFVSTFMK PNPRIYGPIK
     ELLSEQNPAK YRDLTITEFS NTFRSQTISH PALHHFRI
 
 
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