ID   1A1C_MALDO              Reviewed;         473 AA.
AC   P37821; O04993; Q40278;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase {ECO:0000303|PubMed:7716231};
DE            Short=ACC synthase;
DE            EC=1.4.-.- {ECO:0000269|PubMed:10704193};
DE            EC=4.4.1.14 {ECO:0000269|PubMed:11591146, ECO:0000269|PubMed:7809054};
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase;
GN   Name=ACS-1 {ECO:0000303|PubMed:7716231};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Golden Delicious; TISSUE=Fruit cortical tissue;
RX   PubMed=7716231; DOI=10.1104/pp.107.3.1017;
RA   Lay-Yee M., Knighton M.L.;
RT   "A full-length cDNA encoding 1-aminocyclopropane-1-carboxylate synthase
RT   from apple.";
RL   Plant Physiol. 107:1017-1018(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Golden Delicious;
RA   Harada T., Sunako T., Sakuraba W., Goto S., Akada S., Senda M.,
RA   Ishikawa R., Niizeki M.;
RT   "Genomic nucleotide sequence of a ripening-related 1-aminocyclopropane-1-
RT   carboxylate synthase gene (MdACS-1) in apple (Accession No. U89156) (PGR97-
RT   066).";
RL   Plant Physiol. 113:1465-1465(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-473, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Golden Delicious; TISSUE=Fruit;
RX   PubMed=24186277; DOI=10.1007/bf00194512;
RA   Dong J.G., Kim W.T., Yip W.K., Thompson G.A., Li L., Bennett A.B.,
RA   Yang S.F.;
RT   "Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate synthase and
RT   expression of its mRNA in ripening apple fruit.";
RL   Planta 185:38-45(1991).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF TYR-233;
RP   LYS-273 AND ARG-407, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=7809054; DOI=10.1073/pnas.91.26.12428;
RA   White M.F., Vasquez J., Yang S.F., Kirsch J.F.;
RT   "Expression of apple 1-aminocyclopropane-1-carboxylate synthase in
RT   Escherichia coli: kinetic characterization of wild-type and active-site
RT   mutant forms.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:12428-12432(1994).
RN   [5]
RP   COFACTOR, AND MUTAGENESIS OF TYR-85 AND LYS-273.
RX   PubMed=9398277; DOI=10.1021/bi971625l;
RA   Li Y., Feng L., Kirsch J.F.;
RT   "Kinetic and spectroscopic investigations of wild-type and mutant forms of
RT   apple 1-aminocyclopropane-1-carboxylate synthase.";
RL   Biochemistry 36:15477-15488(1997).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=10704193; DOI=10.1021/bi9922704;
RA   Feng L., Kirsch J.F.;
RT   "L-Vinylglycine is an alternative substrate as well as a mechanism-based
RT   inhibitor of 1-aminocyclopropane-1-carboxylate synthase.";
RL   Biochemistry 39:2436-2444(2000).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-47.
RX   PubMed=11591146; DOI=10.1021/bi011050z;
RA   McCarthy D.L., Capitani G., Feng L., Gruetter M.G., Kirsch J.F.;
RT   "Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major
RT   specificity determinant.";
RL   Biochemistry 40:12276-12284(2001).
RN   [8]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=14678788; DOI=10.1016/j.abb.2003.10.017;
RA   Ko S., Eliot A.C., Kirsch J.F.;
RT   "S-methylmethionine is both a substrate and an inactivator of 1-
RT   aminocyclopropane-1-carboxylate synthase.";
RL   Arch. Biochem. Biophys. 421:85-90(2004).
RN   [9] {ECO:0007744|PDB:1B8G}
RP   X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 3-431 IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE, AND MUTAGENESIS OF ASP-230.
RX   PubMed=10610793; DOI=10.1006/jmbi.1999.3255;
RA   Capitani G., Hohenester E., Feng L., Storici P., Kirsch J.F.,
RA   Jansonius J.N.;
RT   "Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in
RT   the biosynthesis of the plant hormone ethylene.";
RL   J. Mol. Biol. 294:745-756(1999).
RN   [10] {ECO:0007744|PDB:1M7Y}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-435 IN COMPLEX WITH AN
RP   INHIBITOR, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=12228256; DOI=10.1074/jbc.m208427200;
RA   Capitani G., McCarthy D.L., Gut H., Grutter M.G., Kirsch J.F.;
RT   "Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the
RT   inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine
RT   intermediate.";
RL   J. Biol. Chem. 277:49735-49742(2002).
RN   [11] {ECO:0007744|PDB:1M4N}
RP   X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-435 IN COMPLEX WITH SUBSTRATE
RP   ANALOG.
RX   PubMed=12686108; DOI=10.1016/s1570-9639(03)00049-9;
RA   Capitani G., Eliot A.C., Gut H., Khomutov R.M., Kirsch J.F., Gruetter M.G.;
RT   "Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an
RT   amino-oxy analogue of the substrate: implications for substrate binding.";
RL   Biochim. Biophys. Acta 1647:55-60(2003).
RN   [12] {ECO:0007744|PDB:1YNU}
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH AN INHIBITOR.
RX   PubMed=15848188; DOI=10.1016/j.febslet.2005.03.048;
RA   Capitani G., Tschopp M., Eliot A.C., Kirsch J.F., Gruetter M.G.;
RT   "Structure of ACC synthase inactivated by the mechanism-based inhibitor L-
RT   vinylglycine.";
RL   FEBS Lett. 579:2458-2462(2005).
RN   [13] {ECO:0007744|PDB:3PIU}
RP   X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1-435 IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE, AND MUTAGENESIS OF ALA-46.
RX   PubMed=21075107; DOI=10.1016/j.febslet.2010.11.013;
RA   Schaerer M.A., Eliot A.C., Gruetter M.G., Capitani G.;
RT   "Structural basis for reduced activity of 1-aminocyclopropane-1-carboxylate
RT   synthase affected by a mutation linked to andromonoecy.";
RL   FEBS Lett. 585:111-114(2011).
CC   -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate,
CC       a direct precursor of ethylene in higher plants (PubMed:7809054,
CC       PubMed:11591146). Catalyzes also the conversion of L-vinylglycine (L-
CC       VG) to alpha-ketobutyrate and ammonia (PubMed:10704193). Can use S-
CC       methylmethionine as substrate (PubMed:14678788).
CC       {ECO:0000269|PubMed:10704193, ECO:0000269|PubMed:11591146,
CC       ECO:0000269|PubMed:14678788, ECO:0000269|PubMed:7809054}.
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:0000269|PubMed:11591146, ECO:0000269|PubMed:7809054};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-amino-3-butenoate + H2O = 2-oxobutanoate + NH4(+);
CC         Xref=Rhea:RHEA:51916, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:134467;
CC         Evidence={ECO:0000269|PubMed:10704193};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:7809054, ECO:0000269|PubMed:9398277};
CC   -!- ACTIVITY REGULATION: Inhibited by L-aminoethoxyvinylglycine (AVG)
CC       (PubMed:12228256). Inhibited by L-vinylglycine (L-VG)
CC       (PubMed:10704193). Inhibited by S-methylmethionine through a L-VG
CC       ketimine intermediate (PubMed:14678788). {ECO:0000269|PubMed:10704193,
CC       ECO:0000269|PubMed:12228256, ECO:0000269|PubMed:14678788}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:7809054};
CC         KM=1.4 mM for L-vinylglycine {ECO:0000269|PubMed:10704193};
CC         KM=4 mM for S-methylmethionine {ECO:0000269|PubMed:14678788};
CC         Note=kcat is 9 sec(-1) per monomer with S-adenosyl-L-methionine as
CC         substrate (PubMed:7809054). kcat is 1.8 sec(-1) with L-vinylglycine
CC         as substrate (PubMed:10704193). kcat is 2.7 min(-1) with
CC         S-methylmethionine as substrate (PubMed:14678788).
CC         {ECO:0000269|PubMed:10704193, ECO:0000269|PubMed:14678788,
CC         ECO:0000269|PubMed:7809054};
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:0000269|PubMed:12228256,
CC       ECO:0000269|PubMed:7809054}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during ripening.
CC       {ECO:0000269|PubMed:24186277}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; L31347; AAA73941.1; -; mRNA.
DR   EMBL; U89156; AAB68617.1; -; Genomic_DNA.
DR   EMBL; U03294; AAA03472.1; -; mRNA.
DR   PIR; T16999; T16999.
DR   PDB; 1B8G; X-ray; 2.37 A; A/B=3-431.
DR   PDB; 1M4N; X-ray; 2.01 A; A=1-435.
DR   PDB; 1M7Y; X-ray; 1.60 A; A=1-435.
DR   PDB; 1YNU; X-ray; 2.25 A; A=1-473.
DR   PDB; 3PIU; X-ray; 1.35 A; A=1-435.
DR   PDBsum; 1B8G; -.
DR   PDBsum; 1M4N; -.
DR   PDBsum; 1M7Y; -.
DR   PDBsum; 1YNU; -.
DR   PDBsum; 3PIU; -.
DR   AlphaFoldDB; P37821; -.
DR   SMR; P37821; -.
DR   BRENDA; 4.4.1.14; 3164.
DR   SABIO-RK; P37821; -.
DR   UniPathway; UPA00384; UER00562.
DR   EvolutionaryTrace; P37821; -.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; NAS:UniProtKB.
DR   GO; GO:0009693; P:ethylene biosynthetic process; IC:UniProtKB.
DR   GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   PANTHER; PTHR43795:SF10; AMINOTRAN_1_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ethylene biosynthesis; Fruit ripening; Lyase; Oxidoreductase;
KW   Pyridoxal phosphate; S-adenosyl-L-methionine.
FT   CHAIN           1..473
FT                   /note="1-aminocyclopropane-1-carboxylate synthase"
FT                   /id="PRO_0000123915"
FT   BINDING         84..85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:12686108,
FT                   ECO:0007744|PDB:1M4N"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:12686108,
FT                   ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:12686108,
FT                   ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:10610793,
FT                   ECO:0000269|PubMed:9398277, ECO:0007744|PDB:1B8G,
FT                   ECO:0007744|PDB:3PIU"
FT   MUTAGEN         46
FT                   /note="A->V: Reduced activity."
FT                   /evidence="ECO:0000305|PubMed:21075107"
FT   MUTAGEN         47
FT                   /note="E->D,Q: Decreased catalytic activity and reaction
FT                   specificity."
FT                   /evidence="ECO:0000269|PubMed:11591146"
FT   MUTAGEN         85
FT                   /note="Y->A: Strongly reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:9398277"
FT   MUTAGEN         230
FT                   /note="D->N: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:10610793"
FT   MUTAGEN         233
FT                   /note="Y->A: Decreased affinity for the substrate."
FT                   /evidence="ECO:0000269|PubMed:7809054"
FT   MUTAGEN         273
FT                   /note="K->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:7809054,
FT                   ECO:0000269|PubMed:9398277"
FT   MUTAGEN         407
FT                   /note="R->K: Strongly decreased catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:7809054"
FT   CONFLICT        15
FT                   /note="Q -> E (in Ref. 3; AAA03472)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        101
FT                   /note="E -> K (in Ref. 3; AAA03472)"
FT                   /evidence="ECO:0000305"
FT   TURN            6..8
FT                   /evidence="ECO:0007829|PDB:1YNU"
FT   HELIX           18..28
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          39..42
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           52..61
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           76..81
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           89..102
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           119..131
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          137..143
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           148..151
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   TURN            152..156
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          159..164
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           175..187
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          192..200
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   TURN            202..204
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           210..223
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          226..230
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           234..236
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          239..241
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           246..249
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   TURN            250..254
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           261..264
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          265..275
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           278..280
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          282..288
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           290..299
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           300..302
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           307..318
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           320..346
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          357..364
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           366..368
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          369..373
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           374..386
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           395..398
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          405..409
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   STRAND          411..413
FT                   /evidence="ECO:0007829|PDB:1M7Y"
FT   HELIX           415..432
FT                   /evidence="ECO:0007829|PDB:1M7Y"
SQ   SEQUENCE   473 AA;  53251 MW;  6ACA20759615E75D CRC64;
     MRMLSRNATF NSHGQDSSYF LGWQEYEKNP YHEVHNTNGI IQMGLAENQL CFDLLESWLA
     KNPEAAAFKK NGESIFAELA LFQDYHGLPA FKKAMVDFMA EIRGNKVTFD PNHLVLTAGA
     TSANETFIFC LADPGEAVLI PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITETALEE
     AYQEAEKRNL RVKGVLVTNP SNPLGTTMTR NELYLLLSFV EDKGIHLISD EIYSGTAFSS
     PSFISVMEVL KDRNCDENSE VWQRVHVVYS LSKDLGLPGF RVGAIYSNDD MVVAAATKMS
     SFGLVSSQTQ HLLSAMLSDK KLTKNYIAEN HKRLKQRQKK LVSGLQKSGI SCLNGNAGLF
     CWVDMRHLLR SNTFEAEMEL WKKIVYEVHL NISPGSSCHC TEPGWFRVCF ANLPERTLDL
     AMQRLKAFVG EYYNVPEVNG GSQSSHLSHS RRQSLTKWVS RLSFDDRGPI PGR
//