ID   1A1D_BURP1              Reviewed;         338 AA.
AC   Q3JLQ0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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};
GN   OrderedLocusNames=BURPS1710b_A0344;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000125; ABA51522.1; -; Genomic_DNA.
DR   RefSeq; WP_004524261.1; NC_007435.1.
DR   AlphaFoldDB; Q3JLQ0; -.
DR   SMR; Q3JLQ0; -.
DR   EnsemblBacteria; ABA51522; ABA51522; BURPS1710b_A0344.
DR   KEGG; bpm:BURPS1710b_A0344; -.
DR   HOGENOM; CLU_048897_2_1_4; -.
DR   OMA; IGIRESW; -.
DR   OrthoDB; 1714795at2; -.
DR   Proteomes; UP000002700; 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_0000304374"
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;  36491 MW;  37030F65E07D8B91 CRC64;
     MNLQKFPRYP LTFGPTPIQP LKRLSAHLGG KVELYAKRDD CNSGLAFGGN KTRKLEYLIP
     DALAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYHDAVY DRVGNIQMSR
     MMGADVRLVP DGFDIGFRKS WEDALADVRA RGGKPYAIPA GCSDHPLGGL GFVGFAEEVR
     AQEAELGFQF DYVVVCSVTG STQAGMVVGF AADGRADRVI GVDASAKPAQ TREQILRIAK
     HTADRVELGR DITSADVVLD ERFGGPEYGL PNEGTLEAIR LCAKLEGVLT DPVYEGKSMH
     GMIEKVRLGE FPAGSKVLYA HLGGVPALNA YSFLFRDG