ID   1A1D_BURTA              Reviewed;         338 AA.
AC   Q2T6A1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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}; OrderedLocusNames=BTH_II1101;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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. {ECO:0000255|HAMAP-Rule:MF_00807}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00807};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00807}.
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00807}.
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DR   EMBL; CP000085; ABC34300.1; -; Genomic_DNA.
DR   RefSeq; WP_009907543.1; NZ_CP008786.1.
DR   AlphaFoldDB; Q2T6A1; -.
DR   SMR; Q2T6A1; -.
DR   PRIDE; Q2T6A1; -.
DR   EnsemblBacteria; ABC34300; ABC34300; BTH_II1101.
DR   KEGG; bte:BTH_II1101; -.
DR   HOGENOM; CLU_048897_2_1_4; -.
DR   OMA; IGIRESW; -.
DR   OrthoDB; 1714795at2; -.
DR   Proteomes; UP000001930; Chromosome II.
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   3: Inferred from homology;
KW   Hydrolase; Pyridoxal phosphate.
FT   CHAIN           1..338
FT                   /note="1-aminocyclopropane-1-carboxylate deaminase"
FT                   /id="PRO_0000304376"
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;  36466 MW;  2E72EDCE4A2D6937 CRC64;
     MNLQKFPRYP LTFGPTPIQP LKRLSAHLGG KVELYAKRDD CNSGLAFGGN KTRKLEYLIP
     DALAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYHDAVY DRVGNIQMSR
     MMGADVRLVP DGFDIGFRKS WEDALADVRA RGGKPYAIPA GCSDHPLGGL GFVGFAEEVR
     AQEAELGFKF DYVVVCSVTG STQAGMVVGF AADGRADRVI GIDASAKPAQ TREQILRIAR
     NTADRVELGR DIASGDVVLD ERFGGPEYGL PNEGTLEAIR LCAKLEGVLT DPVYEGKSMH
     GMIEKVRLGE FPAGSKVLYA HLGGVPALNA YSFLFRDG