ID   1A11_ORYSJ              Reviewed;         487 AA.
AC   Q10DK7; B7EIR0; Q07215; Q6ATI2;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 1 {ECO:0000303|PubMed:17012402};
DE            Short=ACC synthase 1 {ECO:0000303|PubMed:17012402};
DE            Short=OsACS1 {ECO:0000303|PubMed:17012402};
DE            EC=4.4.1.14 {ECO:0000250|UniProtKB:P37821};
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 1 {ECO:0000305};
GN   Name=ACS1 {ECO:0000303|PubMed:17012402}; Synonyms=ACC1 {ECO:0000305};
GN   OrderedLocusNames=Os03g0727600 {ECO:0000312|EMBL:BAS86187.1},
GN   LOC_Os03g51740 {ECO:0000312|EMBL:ABF98659.1};
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=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA   Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA   Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA   Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA   Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA   Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA   Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA   Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA   Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA   Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA   Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT   and diverged grass species.";
RL   Genome Res. 15:1284-1291(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=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   INDUCTION.
RX   PubMed=9037160; DOI=10.1023/b:plan.0000009693.26740.c3;
RA   Zarembinski T.I., Theologis A.;
RT   "Expression characteristics of OS-ACS1 and OS-ACS2, two members of the 1-
RT   aminocyclopropane-1-carboxylate synthase gene family in rice (Oryza sativa
RT   L. cv. Habiganj Aman II) during partial submergence.";
RL   Plant Mol. Biol. 33:71-77(1997).
RN   [7]
RP   FUNCTION, AND INDUCTION BY INFECTION WITH MAGNAPORTHE ORYZAE.
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   [8]
RP   FUNCTION, AND INDUCTION.
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 (PubMed:17012402).
CC       Involved in defense response by producing ethylene at early stage after
CC       fungal pathogen infection (PubMed:17012402). Involved in several
CC       phospate deficiency-induced adaptive responses, such as lateral root
CC       elongation (PubMed:30810167). {ECO:0000269|PubMed:17012402,
CC       ECO:0000269|PubMed:30810167, ECO:0000305|PubMed:17012402}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P37821}.
CC   -!- INDUCTION: Induced by partial submergence (PubMed:9037160). Induced in
CC       leaves by infection with the fungal pathogen Magnaporthe oryzae
CC       (PubMed:17012402). Induced by phosphate deficency (PubMed:30810167).
CC       {ECO:0000269|PubMed:17012402, ECO:0000269|PubMed:30810167,
CC       ECO:0000269|PubMed:9037160}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AC135956; AAT77071.1; -; Genomic_DNA.
DR   EMBL; DP000009; ABF98659.1; -; Genomic_DNA.
DR   EMBL; AP008209; BAF13056.1; -; Genomic_DNA.
DR   EMBL; AP014959; BAS86187.1; -; Genomic_DNA.
DR   EMBL; AK071011; BAG92257.1; -; mRNA.
DR   RefSeq; XP_015629245.1; XM_015773759.1.
DR   AlphaFoldDB; Q10DK7; -.
DR   SMR; Q10DK7; -.
DR   STRING; 4530.OS03T0727600-01; -.
DR   PaxDb; Q10DK7; -.
DR   PRIDE; Q10DK7; -.
DR   EnsemblPlants; Os03t0727600-01; Os03t0727600-01; Os03g0727600.
DR   GeneID; 4333976; -.
DR   Gramene; Os03t0727600-01; Os03t0727600-01; Os03g0727600.
DR   KEGG; osa:4333976; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   HOGENOM; CLU_017584_1_0_1; -.
DR   OMA; RRHTQAI; -.
DR   OrthoDB; 1156861at2759; -.
DR   BRENDA; 4.4.1.14; 4460.
DR   PlantReactome; R-OSA-1119334; Ethylene biosynthesis from methionine.
DR   PlantReactome; R-OSA-1119624; Methionine salvage pathway.
DR   UniPathway; UPA00384; UER00562.
DR   Proteomes; UP000000763; Chromosome 3.
DR   Proteomes; UP000059680; Chromosome 3.
DR   Genevisible; Q10DK7; OS.
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:0008483; F:transaminase activity; IBA:GO_Central.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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; Plant defense;
KW   Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..487
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 1"
FT                   /id="PRO_0000123916"
FT   MOD_RES         286
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P37821"
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