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ACCH7_ARATH
ID   ACCH7_ARATH             Reviewed;         345 AA.
AC   P93821; Q0WR06;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase homolog 7;
DE            EC=1.14.-.-;
GN   OrderedLocusNames=At1g04380; ORFNames=F19P19.18;
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   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-16, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AC000104; AAB70438.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27690.1; -; Genomic_DNA.
DR   EMBL; AK228520; BAF00443.1; -; mRNA.
DR   PIR; E86175; E86175.
DR   RefSeq; NP_171933.1; NM_100318.5.
DR   AlphaFoldDB; P93821; -.
DR   SMR; P93821; -.
DR   STRING; 3702.AT1G04380.1; -.
DR   iPTMnet; P93821; -.
DR   PaxDb; P93821; -.
DR   PRIDE; P93821; -.
DR   ProteomicsDB; 244399; -.
DR   EnsemblPlants; AT1G04380.1; AT1G04380.1; AT1G04380.
DR   GeneID; 839535; -.
DR   Gramene; AT1G04380.1; AT1G04380.1; AT1G04380.
DR   KEGG; ath:AT1G04380; -.
DR   Araport; AT1G04380; -.
DR   TAIR; locus:2018274; AT1G04380.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_0_0_1; -.
DR   InParanoid; P93821; -.
DR   OMA; KSLDCMK; -.
DR   OrthoDB; 755305at2759; -.
DR   PhylomeDB; P93821; -.
DR   BioCyc; ARA:AT1G04380-MON; -.
DR   PRO; PR:P93821; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P93821; baseline and differential.
DR   Genevisible; P93821; 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   1: Evidence at protein level;
KW   Iron; Isopeptide bond; Metal-binding; Oxidoreductase; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..345
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase homolog 7"
FT                   /id="PRO_0000408282"
FT   DOMAIN          194..293
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         274
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         284
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   CROSSLNK        16
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:17272265"
FT   CONFLICT        315
FT                   /note="P -> T (in Ref. 3; BAF00443)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   345 AA;  38618 MW;  EA5597EE9FD13371 CRC64;
     MVVKNSIKFN SQSERKSLEE TKVPPIFGLP PDALDDKKPT SDFAVPIIDF AGVHKSREAV
     VEKIKAAAEN WGIFQVINHG VPLSVLEEIQ NGVVRFHEED PEVKKSYFSL DLTKTFIYHN
     NFELYSSSAG NWRDSFVCYM DPDPSNPEDL PVACRDAMIG YSKHVMSLGG LLFELLSEAL
     GLNSDTLKSM GCMKGLHMIC HYYPPCPQPD QTLGTSKHSD NTFITILLQD NIGGLQILHQ
     DCWVDVSPLP GALIINIGDF LQLMTNDKFI SVDHRVLTNR VGPRISIACF FSSSMNPNST
     VYGPIKELLS EENPPKYRDF TIPEYSKGYI EKGLDGTSHL SHYRI
 
 
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