1A13_ORYSJ
ID 1A13_ORYSJ Reviewed; 452 AA.
AC A0A0P0WIY3; Q53WJ0; Q688L9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 3 {ECO:0000303|PubMed:17012402};
DE Short=ACC synthase 3 {ECO:0000303|PubMed:17012402};
DE Short=OsACS3 {ECO:0000303|PubMed:17012402};
DE EC=4.4.1.14 {ECO:0000250|UniProtKB:P37821};
GN Name=ACS3 {ECO:0000303|PubMed:17012402}; Synonyms=ACC3 {ECO:0000305};
GN OrderedLocusNames=Os05g0196600 {ECO:0000312|EMBL:BAS92679.1},
GN LOC_Os05g10780 {ECO:0000305};
GN ORFNames=OsJ_17447 {ECO:0000312|EMBL:EEE62644.1},
GN P0617H07.9 {ECO:0000312|EMBL:AAV59454.1},
GN P0636E04.1 {ECO:0000312|EMBL:AAU10812.1};
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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 [5]
RP TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=17012402; DOI=10.1104/pp.106.085258;
RA Iwai T., Miyasaka A., Seo S., Ohashi Y.;
RT "Contribution of ethylene biosynthesis for resistance to blast fungus
RT infection in young rice plants.";
RL Plant Physiol. 142:1202-1215(2006).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=30810167; DOI=10.1093/jxb/erz074;
RA Lee H.Y., Chen Z., Zhang C., Yoon G.M.;
RT "Editing of the OsACS locus alters phosphate deficiency-induced adaptive
RT responses in rice seedlings.";
RL J. Exp. Bot. 70:1927-1940(2019).
CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate,
CC a direct precursor of ethylene in higher plants.
CC {ECO:0000250|UniProtKB:P37821}.
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 Evidence={ECO:0000250|UniProtKB:P37821};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P37821};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (PubMed:17012402). Expressed in
CC roots and leaf blades (PubMed:30810167). Expressed at low levels in
CC leaf sheaths and shoot bases (PubMed:30810167).
CC {ECO:0000269|PubMed:17012402, ECO:0000269|PubMed:30810167}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU10812.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV59454.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EEE62644.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC132493; AAU10812.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC135427; AAV59454.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP014961; BAS92679.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE62644.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_015639403.1; XM_015783917.1.
DR AlphaFoldDB; A0A0P0WIY3; -.
DR SMR; A0A0P0WIY3; -.
DR STRING; 4530.OS05T0196600-00; -.
DR PaxDb; A0A0P0WIY3; -.
DR EnsemblPlants; Os05t0196600-00; Os05t0196600-00; Os05g0196600.
DR GeneID; 107275928; -.
DR Gramene; Os05t0196600-00; Os05t0196600-00; Os05g0196600.
DR KEGG; osa:107275928; -.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; A0A0P0WIY3; -.
DR OMA; STKECEL; -.
DR OrthoDB; 1156861at2759; -.
DR UniPathway; UPA00384; UER00562.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
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; Lyase; Pyridoxal phosphate; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..452
FT /note="1-aminocyclopropane-1-carboxylate synthase 3"
FT /id="PRO_0000455670"
FT MOD_RES 283
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P37821"
SQ SEQUENCE 452 AA; 49322 MW; C35563DB0777914E CRC64;
MVGRMLSSPE PTLSTMAMSA AHGEDSPYFA GWRAYDEDPY DPITNPQGVI QMGLAENQVS
FDLLEEYMRE HPEASDCGAG VRENALFQDY HGLKSFRKAM ASFMETIRGG KARFDPDRVV
LTAGATAANE LLTFILADPG DALLVPTPYY PGFDRDLRWR TGVNIVPVSC DSAAGFQVTA
GALRAAYDEA VAAGTRVRGV LITNPSNPLG TTAARGVLEG ILDFVARHDM HLISDEIYSG
SVFAAPDLVS VAELVDERRR ARGGAADAED IARRVHVVYS LSKDLGLPGF RVGVVYSYND
AVVAAARRMS SFTLVSSQTQ RTLAAMLSDA AFAAAYVRSN RDRLRERHAR AVAGLRRAGV
ACLRGANAGL FVWVDMRRLL GDGEATVAGE LRLWRRVVAE AKLNISPGSS CHCREPGWFR
VCFANMSLET LDVALHRLGC FIKKWEQEQH EN
