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1A11_ORYSI
ID   1A11_ORYSI              Reviewed;         487 AA.
AC   A2XLL2; Q07215; Q6ATI2;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 1;
DE            Short=ACC synthase 1;
DE            EC=4.4.1.14;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 1;
GN   Name=ACC1; ORFNames=OsI_012955;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INDUCTION.
RC   STRAIN=cv. IR36;
RX   PubMed=8389618; DOI=10.1091/mbc.4.4.363;
RA   Zarembinski T.I., Theologis A.;
RT   "Anaerobiosis and plant growth hormones induce two genes encoding 1-
RT   aminocyclopropane-1-carboxylate synthase in rice (Oryza sativa L.).";
RL   Mol. Biol. Cell 4:363-373(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 53-99.
RX   PubMed=1438312; DOI=10.1073/pnas.89.22.11046;
RA   Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.;
RT   "The 1-aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis
RT   thaliana.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992).
CC   -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate,
CC       a direct precursor of ethylene in higher plants.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate +
CC         H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:21744,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:58360,
CC         ChEBI:CHEBI:59789; EC=4.4.1.14;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC       methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INDUCTION: By anaerobiosis and indoleacetic acid (IAA) + benzyladenine
CC       (BA) + LiCl treatment. {ECO:0000269|PubMed:8389618}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; M96672; AAA33887.1; -; mRNA.
DR   EMBL; M96673; AAA33888.1; -; Genomic_DNA.
DR   EMBL; CM000128; EAY91722.1; -; Genomic_DNA.
DR   PIR; A47729; A47729.
DR   PIR; B46376; B46376.
DR   AlphaFoldDB; A2XLL2; -.
DR   SMR; A2XLL2; -.
DR   STRING; 39946.A2XLL2; -.
DR   HOGENOM; CLU_017584_1_0_1; -.
DR   UniPathway; UPA00384; UER00562.
DR   Proteomes; UP000007015; Chromosome 3.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   2: Evidence at transcript level;
KW   Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..487
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 1"
FT                   /id="PRO_0000291463"
FT   MOD_RES         286
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        129
FT                   /note="T -> N (in Ref. 1; AAA33887)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="L -> F (in Ref. 1; AAA33887)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="D -> G (in Ref. 1; AAA33887)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   487 AA;  53139 MW;  561D262125D7759E CRC64;
     MVSQVVAEEK PQLLSKKAGC NSHGQDSSYF LGWQEYEKNP FDPVSNPSGI IQMGLAENQL
     SFDLLEEWLE KNPHALGLRR EGGGASVFRE LALFQDYHGL PAFKNALARF MSEQRGYKVV
     FDPSNIVLTA GATSANEALM FCLADHGDAF LIPTPYYPGF DRDLKWRTGA EIVPVHCASA
     NGFRVTRPAL DDAYRRAQKR RLRVKGVLIT NPSNPLGTAS PRADLETIVD FVAAKGIHLI
     SDEIYAGTAF AEPPAGFVSA LEVVAGRDGG GADVSDRVHV VYSLSKDLGL PGFRVGAIYS
     ANAAVVSAAT KMSSFGLVSS QTQYLLAALL GDRDFTRSYV AENKRRIKER HDQLVDGLRE
     IGIGCLPSNA GLFCWVDMSH LMRSRSFAGE MELWKKVVFE VGLNISPGSS CHCREPGWFR
     VCFANMSAKT LDVAMQRLRS FVDSATGGGD NAALRRAAVP VRSVSCPLAI KWALRLTPSI
     ADRKAER
 
 
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