1A1D_BURM1
ID 1A1D_BURM1 Reviewed; 338 AA.
AC A9AQJ3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Bmul_5215, BMULJ_03304;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000869; ABX18885.1; -; Genomic_DNA.
DR EMBL; AP009386; BAG45178.1; -; Genomic_DNA.
DR RefSeq; WP_012217704.1; NC_010805.1.
DR AlphaFoldDB; A9AQJ3; -.
DR SMR; A9AQJ3; -.
DR STRING; 395019.Bmul_5215; -.
DR EnsemblBacteria; BAG45178; BAG45178; BMULJ_03304.
DR KEGG; bmj:BMULJ_03304; -.
DR KEGG; bmu:Bmul_5215; -.
DR eggNOG; COG2515; Bacteria.
DR HOGENOM; CLU_048897_2_1_4; -.
DR OMA; LVQEKWV; -.
DR Proteomes; UP000008815; 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; Reference proteome.
FT CHAIN 1..338
FT /note="1-aminocyclopropane-1-carboxylate deaminase"
FT /id="PRO_1000134010"
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; 36761 MW; 0CE4A835CA982B2D CRC64;
MNLQRFPRYP LTFGPTPIQP LKRLSEHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP
DALEQRADTL VSIGGVQSNQ TRQVAAVAAH LGMKCVLVQE HWVNYDDPVY DRVGNIQLSR
MMGADVRLVP DGFDIGIRRS WEEALESVKQ AGGRPYPIPA GCSEHPLGGL GFVGFAEEVR
AQEAQFGLRF DYIVVCSVTG STQAGMIVGF AADGRADRVI GIDASATPAR TREQITRIAR
HTAELVDLGR DITDADVVLD TRYAGPEYGL PNEGTLEAIR LCARLEGVLT DPVYEGKSMH
GMIDKVRRGE FEPGSKVLYA HLGGVPALSA YSAIFADG
