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ACH12_ARATH
ID   ACH12_ARATH             Reviewed;         366 AA.
AC   Q9LTH7; Q2V2X0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase homolog 12;
DE            EC=1.14.-.-;
GN   OrderedLocusNames=At5g59540; ORFNames=F2O15.6;
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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(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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LTH7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LTH7-2; Sequence=VSP_041042, VSP_041043;
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB025604; BAA97488.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97202.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97203.1; -; Genomic_DNA.
DR   EMBL; AF424616; AAL11609.1; -; mRNA.
DR   EMBL; BT024895; ABD85166.1; -; mRNA.
DR   EMBL; AK226221; BAE98386.1; -; mRNA.
DR   RefSeq; NP_001032104.1; NM_001037027.1. [Q9LTH7-2]
DR   RefSeq; NP_200762.1; NM_125346.3. [Q9LTH7-1]
DR   AlphaFoldDB; Q9LTH7; -.
DR   SMR; Q9LTH7; -.
DR   iPTMnet; Q9LTH7; -.
DR   PaxDb; Q9LTH7; -.
DR   PRIDE; Q9LTH7; -.
DR   ProteomicsDB; 243281; -. [Q9LTH7-1]
DR   EnsemblPlants; AT5G59540.1; AT5G59540.1; AT5G59540. [Q9LTH7-1]
DR   EnsemblPlants; AT5G59540.2; AT5G59540.2; AT5G59540. [Q9LTH7-2]
DR   GeneID; 836073; -.
DR   Gramene; AT5G59540.1; AT5G59540.1; AT5G59540. [Q9LTH7-1]
DR   Gramene; AT5G59540.2; AT5G59540.2; AT5G59540. [Q9LTH7-2]
DR   KEGG; ath:AT5G59540; -.
DR   Araport; AT5G59540; -.
DR   TAIR; locus:2148303; AT5G59540.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_0_0_1; -.
DR   InParanoid; Q9LTH7; -.
DR   OMA; TAISHYQ; -.
DR   OrthoDB; 755305at2759; -.
DR   PhylomeDB; Q9LTH7; -.
DR   BioCyc; ARA:AT5G59540-MON; -.
DR   PRO; PR:Q9LTH7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LTH7; baseline and differential.
DR   Genevisible; Q9LTH7; 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   Alternative splicing; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..366
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase homolog
FT                   12"
FT                   /id="PRO_0000408287"
FT   DOMAIN          215..314
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         239
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
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         295
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         305
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   VAR_SEQ         284..285
FT                   /note="LI -> VK (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041042"
FT   VAR_SEQ         286..366
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041043"
SQ   SEQUENCE   366 AA;  41539 MW;  8C80B52FE06DD4A5 CRC64;
     MMTKNSIEFD PYIERKAFDE TKQGVKGLVD AKITEVPRIF HHRQDILTNK KPSASVSDLE
     IPIIDFASVH ADTASREAIV EKVKYAVENW GFFQVINHSI PLNVLEEIKD GVRRFHEEDP
     EVKKSFFSRD AGNKKFVYNS NFDLYSSSPS VNWRDSFSCY IAPDPPAPEE IPETCRDAMF
     EYSKHVLSFG GLLFELLSEA LGLKSQTLES MDCVKTLLMI CHYYPPCPQP DLTLGITKHS
     DNSFLTLLLQ DNIGGLQILH QDSWVDVSPI HGALVVNIGD FLQLITNDKF VSVEHRVLAN
     RQGPRISVAS FFSSSMRPNS RVYGPMKELV SEENPPKYRD ITIKEYSKIF FEKGLDGTSH
     LSNIRI
 
 
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