ID   1A12_ORYSJ              Reviewed;         483 AA.
AC   Q7XQ85; Q0JAT6;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 2 {ECO:0000303|PubMed:17012402};
DE            Short=ACC synthase 2 {ECO:0000303|PubMed:17012402};
DE            Short=OsACS2 {ECO:0000303|PubMed:17012402};
DE            EC=4.4.1.14 {ECO:0000250|UniProtKB:P37821};
GN   Name=ACS2 {ECO:0000303|PubMed:17012402}; Synonyms=ACC2 {ECO:0000305};
GN   OrderedLocusNames=Os04g0578000 {ECO:0000312|EMBL:BAS90624.1},
GN   LOC_Os04g48850 {ECO:0000305};
GN   ORFNames=OSJNBa0011J08.4 {ECO:0000312|EMBL:CAE03249.1};
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=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
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.
RX   PubMed=23031077; DOI=10.1111/pbi.12004;
RA   Helliwell E.E., Wang Q., Yang Y.;
RT   "Transgenic rice with inducible ethylene production exhibits broad-spectrum
RT   disease resistance to the fungal pathogens Magnaporthe oryzae and
RT   Rhizoctonia solani.";
RL   Plant Biotechnol. J. 11:33-42(2013).
RN   [9]
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 (Probable). Involved in
CC       defense response by producing ethylene after pathogen infection
CC       (PubMed:17012402, PubMed:23031077). Involved in several phospate
CC       deficiency-induced adaptive responses, such as lateral root elongation
CC       (PubMed:30810167). {ECO:0000269|PubMed:17012402,
CC       ECO:0000269|PubMed:23031077, ECO:0000269|PubMed:30810167,
CC       ECO:0000305|PubMed:23031077}.
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   -!- INDUCTION: Down-regulated by partial submergence (PubMed:9037160).
CC       Induced in leaves by infection with the fungal pathogen Magnaporthe
CC       oryzae (PubMed:17012402). Induced by phosphate deficency
CC       (PubMed:30810167). {ECO:0000269|PubMed:17012402,
CC       ECO:0000269|PubMed:30810167, ECO:0000269|PubMed:9037160}.
CC   -!- MISCELLANEOUS: Lines with ACS2 transgene under the control of a strong
CC       pathogen-inducible promoter show significantly increased levels of
CC       endogenous ethylene and defense gene expression in response to pathogen
CC       infection, and exhibit increased resistance to Magnaporthe oryzae and
CC       Ralstonia solanacearum. {ECO:0000269|PubMed:23031077}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AL606624; CAE03249.1; -; Genomic_DNA.
DR   EMBL; AP008210; BAF15551.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS90624.1; -; Genomic_DNA.
DR   EMBL; AK064250; BAG89048.1; -; mRNA.
DR   RefSeq; XP_015634087.1; XM_015778601.1.
DR   AlphaFoldDB; Q7XQ85; -.
DR   SMR; Q7XQ85; -.
DR   STRING; 4530.OS04T0578000-01; -.
DR   PaxDb; Q7XQ85; -.
DR   PRIDE; Q7XQ85; -.
DR   EnsemblPlants; Os04t0578000-01; Os04t0578000-01; Os04g0578000.
DR   GeneID; 4336750; -.
DR   Gramene; Os04t0578000-01; Os04t0578000-01; Os04g0578000.
DR   KEGG; osa:4336750; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   HOGENOM; CLU_017584_1_0_1; -.
DR   InParanoid; Q7XQ85; -.
DR   OMA; VLIVNPH; -.
DR   OrthoDB; 1156861at2759; -.
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 4.
DR   Proteomes; UP000059680; Chromosome 4.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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; Plant defense; Pyridoxal phosphate;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..483
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 2"
FT                   /id="PRO_0000455669"
FT   MOD_RES         275
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P37821"
SQ   SEQUENCE   483 AA;  54340 MW;  30D003099C83AFDA CRC64;
     MAYQGIDLLS TKAAGDDHGE NSSYFDGWKA YDTNPFDLRH NRGGVIQMGL AENQLSLDLI
     EEWSKNHPEA SICTPEGVSQ FKRIANFQDY HGLPEFRKAM AQFMGQVRGG KATFDPDRVV
     MSGGATGAQE TLAFCLANPG EAFLVPTPYY PAFDRDCCWR SGIKLLPIEC HSFNDFRLTK
     EALVSAYDGA RRQGISVKGI LITNPSNPLG TITDRDTLAM LATFATEHRV HLVCDEIYAG
     SVFATPEYVS IAEVIERDVP WCNRDLIHVV YSLSKDFGLP GFRVGIIYSY NDAVVAAARR
     MSSFGLVSSQ TQYFLARMLS DEEFIGRFLQ ESKCRLVARH ERFTSGLREV GIGCLRGNAG
     LFSWMDLRRM LREKTAEAEL ELWRVIVHQV KLNVSPGTSF HCREPGWFRV CHANMDDETM
     EVALGRIHDF VRQHQQRRVK AERWAANRQL RLSLPHHHHL SPAHLSSPLA LLSPQSPMVR
     ATS