ID   1A1D_SCHPO              Reviewed;         338 AA.
AC   Q9URX3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Probable 1-aminocyclopropane-1-carboxylate deaminase;
DE            Short=ACC deaminase;
DE            Short=ACCD;
DE            EC=3.5.99.7;
GN   ORFNames=SPAC922.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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; CU329670; CAB63550.1; -; Genomic_DNA.
DR   PIR; T50268; T50268.
DR   RefSeq; NP_595003.1; NM_001020434.2.
DR   AlphaFoldDB; Q9URX3; -.
DR   SMR; Q9URX3; -.
DR   BioGRID; 279980; 1.
DR   STRING; 4896.SPAC922.03.1; -.
DR   MaxQB; Q9URX3; -.
DR   PaxDb; Q9URX3; -.
DR   EnsemblFungi; SPAC922.03.1; SPAC922.03.1:pep; SPAC922.03.
DR   GeneID; 2543564; -.
DR   KEGG; spo:SPAC922.03; -.
DR   PomBase; SPAC922.03; -.
DR   VEuPathDB; FungiDB:SPAC922.03; -.
DR   eggNOG; ENOG502QPS1; Eukaryota.
DR   HOGENOM; CLU_048897_2_1_1; -.
DR   InParanoid; Q9URX3; -.
DR   OMA; LVQEKWV; -.
DR   PhylomeDB; Q9URX3; -.
DR   PRO; PR:Q9URX3; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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   GO; GO:1990748; P:cellular detoxification; NAS:PomBase.
DR   GO; GO:0071941; P:nitrogen cycle metabolic process; IC:PomBase.
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..338
FT                   /note="Probable 1-aminocyclopropane-1-carboxylate
FT                   deaminase"
FT                   /id="PRO_0000184511"
FT   ACT_SITE        78
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   338 AA;  36687 MW;  AE480741BD708BF3 CRC64;
     MGLEQFKKYP LTFGPTPITS MKRLSKTLGG KVEIFAKRED CNSGLAFGGN KIRKLEYLIP
     EAIDGGYDTL VSIGGIQSNQ TRQVAAVAAH LGLDCVLIQE DWVDYKDTMY DRVGNIELSR
     IVNADVRLDS SKFDIGIRPS FKNALEELTK KGKKPFPIPA GCSEHPYGGL GFVGCVEEIY
     EQEKQLGFKF DKIVVCTVTG SSFAGIIVGM ALTGRQKDVI GIDASATPEK TKAQVLRIAQ
     NTAKLIGLEK ELTESDVNID TRFAHPAYGI PNEGTIEAIK LCGATEGVLT DPVYEGKSMQ
     GLIHLVRNNE IAEGSKVLYI HLGGAPALSA YSAYFKNT