1A1D_RHIRD
ID 1A1D_RHIRD Reviewed; 337 AA.
AC Q9AHF0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 71.
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 Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 9674 / d3I;
RX PubMed=11429459; DOI=10.1099/00221287-147-7-1815;
RA Trott S., Bauer R., Knackmuss H.J., Stolz A.;
RT "Genetic and biochemical characterization of an enantioselective amidase
RT from Agrobacterium tumefaciens strain d3.";
RL Microbiology 147:1815-1824(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAK28496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF315580; AAK28496.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q9AHF0; -.
DR SMR; Q9AHF0; -.
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..337
FT /note="1-aminocyclopropane-1-carboxylate deaminase"
FT /id="PRO_0000184496"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
FT MOD_RES 50
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
SQ SEQUENCE 337 AA; 36676 MW; FF5CCED8FE6FB09B CRC64;
MLEKFERYPL TFGATAIEYL PRLTEALGGD VEIWAKREDC NSGLAMGGNK LRKLEYIVPD
AIASNADTLV SIGGVQSNHT RMVAAVAAKL GMKCRLVQES WVPHEDAVYD RVGNILMTRL
MGADSRIVDD GFDIGIRQSW EDAIQSVIDE GGKPYAIPAG ASVHKYGGLG YVAFAEEVAR
QEADLGFKFD YIIVCVVTGS TQAGMIVGFA AQDRADRVIG IDASGTPEQT RSQVRQIVDN
TAELVELGRP VREDEIVILN DYAYPAYGVP SNETNEAIRL AARTEAMITD PVYEGKSMQG
MIDLTRKGFF PKGSKVLYAH LGGAPALNGY SYTYRNG
