ID   1A1D_CRYNJ              Reviewed;         345 AA.
AC   Q5KMX3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Probable 1-aminocyclopropane-1-carboxylate deaminase;
DE            Short=ACC deaminase;
DE            Short=ACCD;
DE            EC=3.5.99.7;
GN   OrderedLocusNames=CNB00190;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Catalyzes a cyclopropane ring-opening reaction, the
CC       irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to
CC       ammonia and alpha-ketobutyrate. {ECO:0000250}.
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; AE017342; AAW41453.1; -; Genomic_DNA.
DR   RefSeq; XP_568760.1; XM_568760.1.
DR   AlphaFoldDB; Q5KMX3; -.
DR   SMR; Q5KMX3; -.
DR   STRING; 5207.AAW41453; -.
DR   PaxDb; Q5KMX3; -.
DR   EnsemblFungi; AAW41453; AAW41453; CNB00190.
DR   GeneID; 3255867; -.
DR   KEGG; cne:CNB00190; -.
DR   VEuPathDB; FungiDB:CNB00190; -.
DR   eggNOG; ENOG502QPS1; Eukaryota.
DR   HOGENOM; CLU_048897_2_1_1; -.
DR   InParanoid; Q5KMX3; -.
DR   OMA; LVQEKWV; -.
DR   OrthoDB; 817780at2759; -.
DR   Proteomes; UP000002149; Chromosome 2.
DR   GO; GO:0008660; F:1-aminocyclopropane-1-carboxylate deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009310; P:amine catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005965; ACP_carboxylate_deaminase.
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; Reference proteome.
FT   CHAIN           1..345
FT                   /note="Probable 1-aminocyclopropane-1-carboxylate
FT                   deaminase"
FT                   /id="PRO_0000184510"
FT   ACT_SITE        85
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   345 AA;  37050 MW;  82A7CAC10E8F3D39 CRC64;
     MSTPAYLTKL ESIPKEKFLF GPSPISYLPN LTAVLGGKVK LYAKREDCNS GLAYGGNKVR
     KLEYLVADAK AKGCNTLVSV GGVQSNHTRA VTAVAVASGL KAVTVQEKWV PIDPPLYSET
     GNILLSRLMG GDVRLNQETF DIRHKKATED AFKDVEAKGG KPYYIPAGAS DHPLGGLGFT
     NWVVELAKQE KELGVFFDVV IVCSVTGSSH AGTVVGAVAE GRKRKIIGID ASGKPEATRN
     QVLKIARNTA ALLDERLEIK EEDVILDDRF HAGIYGIPDD ETIAAMKLAA QTDAFITDPV
     YEGKSMAGMI RLVKEGAIKE GSNVLYIHLG GQPALNAYSS YFPHA