1A1D_VARPD
ID 1A1D_VARPD Reviewed; 338 AA.
AC Q6J256;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 25-MAY-2022, entry version 61.
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};
OS Variovorax paradoxus.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=34073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=5C2;
RA Hontzeas N., Belimov A., Safronova V., Glick B.R.;
RT "Rapid molecular screening of soil bacteria for 1-aminocyclopropane-1-
RT carboxylate (ACC) deaminase genes.";
RL Submitted (NOV-2004) 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; AY604531; AAT35829.2; -; Genomic_DNA.
DR AlphaFoldDB; Q6J256; -.
DR SMR; Q6J256; -.
DR eggNOG; COG2515; Bacteria.
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_0000184509"
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; 36592 MW; C0BFF113A31A17AD CRC64;
MNLKKFPRHV LTFGPTPIQP LKRLSAHLGG KVDLYAKRED CNSGLAFGGN KTRKLEYLIP
EALEGGYDTL VSIGGIQSNQ TRQVAAVAAH LGLKCVLVQE NWVNYSDAVY DRVGNIEMSR
IMGADVRLDA AGFDIGIRQS WEQAMADVRA AGGKPFPIPA GCSEHPRGGL GSVGFAEEVR
QQEAELGFKF DYLVVCSVTG STQAGMVVGF AADGRADRVI GIDASAKPQQ TFEQILRIAK
NTAELVELGR DITEKDVVLD RRFGGPEYGL PNEGTLEAIR LSARFEGMLT DPVYEGKSMH
GMIEKVRLGE FPAGSKVLYA HLGGVPALNA YSFLFRNG
