1A1C_MALDO
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 03-AUG-2022, entry version 119.
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 S-
CC 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 STRING; 3750.XP_008342238.1; -.
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 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 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
