ID   1A1D_PYRFU              Reviewed;         329 AA.
AC   Q8U4R3;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Putative 1-aminocyclopropane-1-carboxylate deaminase;
DE            Short=ACC deaminase;
DE            EC=3.5.99.7;
GN   OrderedLocusNames=PF0010;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL80134.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE009950; AAL80134.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011011122.1; NZ_CP023154.1.
DR   AlphaFoldDB; Q8U4R3; -.
DR   SMR; Q8U4R3; -.
DR   STRING; 186497.PF0010; -.
DR   PRIDE; Q8U4R3; -.
DR   EnsemblBacteria; AAL80134; AAL80134; PF0010.
DR   GeneID; 41713902; -.
DR   KEGG; pfu:PF0010; -.
DR   PATRIC; fig|186497.12.peg.11; -.
DR   eggNOG; arCOG01435; Archaea.
DR   HOGENOM; CLU_048897_1_0_2; -.
DR   OMA; LVQEKWV; -.
DR   OrthoDB; 35277at2157; -.
DR   PhylomeDB; Q8U4R3; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC.
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..329
FT                   /note="Putative 1-aminocyclopropane-1-carboxylate
FT                   deaminase"
FT                   /id="PRO_0000184522"
FT   MOD_RES         54
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   329 AA;  35795 MW;  627852CFD0A450F8 CRC64;
     MHPKVQSLLS KFPRVELIPW ETPIQYLPNI SKLVGADIYV KRDDLTGLGI GGNKIRKLEY
     LLGDAIIRKA DVIITVGAVH SNHAFVTGLA AKKLGFDVVL VLRGKEELRG NYLLDKIMGI
     ETRVYEAKDS FELMKYAEEV AKELEEKGRK PYIIPVGGAS PVGTLGYVRA SGEIAEQGNR
     IGVNFDSIVV ATGSGGTLAG LSVGLAILRK ETRAIGMAVG KFGETMVNKV EELAKATGEF
     IGVKNLKLKI ELYDYSFGEY GKITREVAET IRLVGTKEGV ILDPVYTGKA FYGLLDLAKK
     GELGEKILFI HTGGISGTFH YGDKILSFL