ID   1A1D_THEMA              Reviewed;         312 AA.
AC   Q9WY68;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Putative 1-aminocyclopropane-1-carboxylate deaminase;
DE            Short=ACC deaminase;
DE            EC=3.5.99.7;
GN   OrderedLocusNames=TM_0225;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD35317.1; -; Genomic_DNA.
DR   PIR; D72401; D72401.
DR   RefSeq; NP_228040.1; NC_000853.1.
DR   RefSeq; WP_004082912.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WY68; -.
DR   SMR; Q9WY68; -.
DR   STRING; 243274.THEMA_03600; -.
DR   EnsemblBacteria; AAD35317; AAD35317; TM_0225.
DR   KEGG; tma:TM0225; -.
DR   eggNOG; COG2515; Bacteria.
DR   InParanoid; Q9WY68; -.
DR   OMA; YHFGGYA; -.
DR   OrthoDB; 1714795at2; -.
DR   Proteomes; UP000008183; Chromosome.
DR   GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019148; F:D-cysteine desulfhydrase activity; IBA:GO_Central.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005966; D-Cys_desShydrase.
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; TIGR01275; ACC_deam_rel; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..312
FT                   /note="Putative 1-aminocyclopropane-1-carboxylate
FT                   deaminase"
FT                   /id="PRO_0000184520"
FT   MOD_RES         42
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   312 AA;  34756 MW;  6BE2A4A0BFC1E15F CRC64;
     MRIDLSLKPT PVQFLKRLSE KYGFNIYVKR DDLTELVGSG NKIRKLEYLL WEALKKGATT
     VFTCGGLQSN HARATAYVSR RYGLKPVLFL RKGEKVLNGN LLLDILLGAE IVEVSPEEYE
     RIDEIFDVHK KMREKKGEKV YVIPEGGSNS LGAFGYFNAV LEMKDQLNLE SFDAIVCAVG
     SGGTIAGLSA GISFLEYHVP VVGVNVTTKN SDYFVGKVKR IISGMEEYGL RVNETVFEVV
     DDYRGPGYAI PSSEDVEILK EVASIEGIIL DPVYTAKAFR GMIEMFRNSE KNVLFIHTGG
     IFGLFAQSRR LV