ID   1A1D_PSES0              Reviewed;         338 AA.
AC   P30297;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000255|HAMAP-Rule:MF_00807};
DE            Short=ACC deaminase {ECO:0000255|HAMAP-Rule:MF_00807};
DE            Short=ACCD {ECO:0000255|HAMAP-Rule:MF_00807};
DE            EC=3.5.99.7 {ECO:0000255|HAMAP-Rule:MF_00807};
GN   Name=acdS {ECO:0000255|HAMAP-Rule:MF_00807};
OS   Pseudomonas sp. (strain 6G5).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=29439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1821764; DOI=10.2307/3869226;
RA   Klee H.J., Hayford M.B., Kretzmer K.A., Barry G.F., Kishore G.M.;
RT   "Control of ethylene synthesis by expression of a bacterial enzyme in
RT   transgenic tomato plants.";
RL   Plant Cell 3:1187-1193(1991).
CC   -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the
CC       irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to
CC       ammonia and alpha-ketobutyrate. Allows growth on ACC as a nitrogen
CC       source.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate +
CC         NH4(+); Xref=Rhea:RHEA:16933, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58360; EC=3.5.99.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00807};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homotrimer.
CC   -!- BIOTECHNOLOGY: Introduced by genetic manipulation and expressed in
CC       improved ripening tomato by Monsanto. ACC is the immediate precursor of
CC       the phytohormone ethylene which is involved in the control of ripening.
CC       ACC deaminase reduces ethylene biosynthesis and thus extends the shelf
CC       life of fruits and vegetables.
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00807}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M80882; AAA73153.1; -; Genomic_DNA.
DR   PIR; JQ1330; JQ1330.
DR   AlphaFoldDB; P30297; -.
DR   SMR; P30297; -.
DR   GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0018871; P:1-aminocyclopropane-1-carboxylate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00807; ACC_deaminase; 1.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005965; ACP_carboxylate_deaminase.
DR   InterPro; IPR020601; ACP_carboxylate_deaminase_bac.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   PANTHER; PTHR43780; PTHR43780; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01274; ACC_deam; 1.
PE   1: Evidence at protein level;
KW   Genetically modified food; Hydrolase; Pyridoxal phosphate.
FT   CHAIN           1..338
FT                   /note="1-aminocyclopropane-1-carboxylate deaminase"
FT                   /id="PRO_0000184503"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
SQ   SEQUENCE   338 AA;  36873 MW;  F496374E7C12B6AD CRC64;
     MNLNRFERYP LTFGPSPITP LKRLSQHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP
     EAIEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR
     IMGADVRLDA AGFDIGIRPS WEKAMSDVVE QGGKPFPIPA GCSEHPYGGL GFVGFAEEVR
     QQEKELGFKF DYIVVCSVTG STQAGMVVGF AADGRSKNVI GIDASAKPEQ TKAQILRIAR
     HTAELVELGR EITEEDVVLD TRFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH
     GMIEMVRRGE FPEGSKVLYA HLGGAPALNA YSFLFRNG