ID   1A1D_BURMA              Reviewed;         338 AA.
AC   Q62CE3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=BMAA0952;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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}.
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; CP000011; AAU46138.1; -; Genomic_DNA.
DR   RefSeq; WP_004184549.1; NC_006349.2.
DR   RefSeq; YP_105635.1; NC_006349.2.
DR   AlphaFoldDB; Q62CE3; -.
DR   SMR; Q62CE3; -.
DR   STRING; 243160.BMAA0952; -.
DR   EnsemblBacteria; AAU46138; AAU46138; BMAA0952.
DR   GeneID; 56597527; -.
DR   KEGG; bma:BMAA0952; -.
DR   PATRIC; fig|243160.12.peg.4473; -.
DR   eggNOG; COG2515; Bacteria.
DR   HOGENOM; CLU_048897_2_1_4; -.
DR   OMA; IGIRESW; -.
DR   Proteomes; UP000006693; Chromosome 2.
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_0000184498"
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;  36481 MW;  64927D39E112B86F CRC64;
     MNLQKFSRYP 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