ID   1A1D_RHILO              Reviewed;         337 AA.
AC   Q98AM7;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=mlr5932;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB52295.1; -; Genomic_DNA.
DR   RefSeq; WP_010913628.1; NC_002678.2.
DR   AlphaFoldDB; Q98AM7; -.
DR   SMR; Q98AM7; -.
DR   STRING; 266835.14025695; -.
DR   EnsemblBacteria; BAB52295; BAB52295; BAB52295.
DR   KEGG; mlo:mlr5932; -.
DR   PATRIC; fig|266835.9.peg.4718; -.
DR   eggNOG; COG2515; Bacteria.
DR   HOGENOM; CLU_048897_2_1_5; -.
DR   OMA; LVQEKWV; -.
DR   OrthoDB; 1714795at2; -.
DR   Proteomes; UP000000552; Chromosome.
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_0000184508"
FT   MOD_RES         50
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00807"
SQ   SEQUENCE   337 AA;  36602 MW;  3C5C52F995C49646 CRC64;
     MLEKFERYPL TFGLTPIEKL DRLGKHLGGK VEIYAKREDC NSGLAFGGNK LRKLEYVIPD
     AIASDADTLV TVGGVQSNHT RMVAAVAAKI GMKCLLVHES WVPHEDVVYD RVGNILLSRI
     LGAEVRLVDD GFDIGIRRSW EKALYEVKAR GGRPYAIPAG ASVHPNGGLG YVGFAEEVRA
     QEEQLGFAFD YMVVCTVTGS THAGMLVGFA KDGRQRNVIG IDASATPAKT KAQVLSIARH
     TATLVELGSE LAEDDVVLLE DYAHPRYGIP SEETKEAIRL CARLEGMITD PVYEGKSMQG
     MIDLVQKGFF PAGSRILYAH LGGAPAINGY GYTFRNG