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ACCH9_ARATH
ID   ACCH9_ARATH             Reviewed;         365 AA.
AC   Q9LSW7; Q0WVA2;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase homolog 9;
DE            EC=1.14.-.-;
GN   OrderedLocusNames=At5g43440; ORFNames=MWF20.15;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 (NOV-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=Q9LSW7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LSW7-2; Sequence=VSP_041040, VSP_041041;
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB025638; BAA97423.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94963.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94964.1; -; Genomic_DNA.
DR   EMBL; AY056810; AAL10501.1; -; mRNA.
DR   EMBL; AY143873; AAN28812.1; -; mRNA.
DR   EMBL; AK226856; BAE98946.1; -; mRNA.
DR   RefSeq; NP_001078700.1; NM_001085231.2. [Q9LSW7-2]
DR   RefSeq; NP_199157.1; NM_123710.2. [Q9LSW7-1]
DR   AlphaFoldDB; Q9LSW7; -.
DR   SMR; Q9LSW7; -.
DR   STRING; 3702.AT5G43440.1; -.
DR   PaxDb; Q9LSW7; -.
DR   PRIDE; Q9LSW7; -.
DR   ProteomicsDB; 244515; -. [Q9LSW7-1]
DR   EnsemblPlants; AT5G43440.1; AT5G43440.1; AT5G43440. [Q9LSW7-1]
DR   EnsemblPlants; AT5G43440.2; AT5G43440.2; AT5G43440. [Q9LSW7-2]
DR   GeneID; 834364; -.
DR   Gramene; AT5G43440.1; AT5G43440.1; AT5G43440. [Q9LSW7-1]
DR   Gramene; AT5G43440.2; AT5G43440.2; AT5G43440. [Q9LSW7-2]
DR   KEGG; ath:AT5G43440; -.
DR   Araport; AT5G43440; -.
DR   TAIR; locus:2176456; AT5G43440.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_0_0_1; -.
DR   InParanoid; Q9LSW7; -.
DR   OMA; ACYIAPA; -.
DR   OrthoDB; 755305at2759; -.
DR   PhylomeDB; Q9LSW7; -.
DR   BioCyc; ARA:AT5G43440-MON; -.
DR   PRO; PR:Q9LSW7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LSW7; baseline and differential.
DR   Genevisible; Q9LSW7; AT.
DR   GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; ISS:TAIR.
DR   GO; GO:0046872; F:metal ion binding; 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..365
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase homolog 9"
FT                   /id="PRO_0000408284"
FT   DOMAIN          214..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"
FT   BINDING         304
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   VAR_SEQ         283..290
FT                   /note="LITNDKFL -> ASSIDASF (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_041040"
FT   VAR_SEQ         291..365
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_041041"
SQ   SEQUENCE   365 AA;  40860 MW;  0A8EDA3D4CC69389 CRC64;
     MTEKSAELVR LNELKAFVST KAGVKGLVDT KITEVPRIFH IPSSSTLSNN KPSDIFGLNL
     TVPIIDLGDG NTSAARNVLV SKIKEAAENW GFFQVINHGI PLTVLKDIKQ GVRRFHEEDP
     EVKKQYFATD FNTRFAYNTN FDIHYSSPMN WKDSFTCYTC PQDPLKPEEI PLACRDVVIE
     YSKHVMELGG LLFQLLSEAL GLDSEILKNM DCLKGLLMLC HYYPPCPQPD LTLGISKHTD
     NSFITILLQD QIGGLQVLHQ DSWVDVTPVP GALVISIGDF MQLITNDKFL SMEHRVRANR
     DGPRISVACF VSSGVFPNST VYGPIKELLS DENPAKYRDI TIPEYTVGYL ASIFDGKSHL
     SKFRI
 
 
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