1A1D_RALPJ
ID 1A1D_RALPJ Reviewed; 338 AA.
AC B2UGM5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=Rpic_2004;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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; CP001068; ACD27139.1; -; Genomic_DNA.
DR RefSeq; WP_012435939.1; NC_010682.1.
DR AlphaFoldDB; B2UGM5; -.
DR SMR; B2UGM5; -.
DR STRING; 402626.Rpic_2004; -.
DR EnsemblBacteria; ACD27139; ACD27139; Rpic_2004.
DR KEGG; rpi:Rpic_2004; -.
DR PATRIC; fig|402626.5.peg.3156; -.
DR eggNOG; COG2515; Bacteria.
DR HOGENOM; CLU_048897_2_1_4; -.
DR OMA; LVQEKWV; -.
DR OrthoDB; 1714795at2; -.
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_1000134013"
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; 36780 MW; A703DEE5F6E3EF85 CRC64;
MNLQRFPRYP LTFGPTPIQP LKRLSAHLGG KVELFAKRED CNSGLAFGGN KTRKLEYLIP
EALEGGYDTL VSIGGIQSNQ TRQVAAVAAH LGLKCVLVQE NWVNYSDAVY DRVGNIEMSR
IMGADVRLDS AGFDIGIRPS WEQAMDDVRK RGGKPFPIPA GCSEHPLGGL GFVGFAEEVR
QQEAELGFKF DYIVVCSVTG STQAGMVVGF AADGRADKVI GIDASAKPEQ TRAQILRIAQ
HTAELVDLGR NITERDVVLD TRYGGPEYGL PNEGTLEAIR LCARQEAMLT DPVYEGKSMH
GMIDMVRNGE FPAGSRVLYA HLGGVPALNA YSFIFRNG