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