ID   YI01_SCHPO              Reviewed;         583 AA.
AC   Q9URY4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative amidase C869.01;
DE            EC=3.5.1.4;
DE   Flags: Precursor;
GN   ORFNames=SPAC869.01;
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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monocarboxylic acid amide + H2O = a monocarboxylate +
CC         NH4(+); Xref=Rhea:RHEA:12020, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:35757, ChEBI:CHEBI:83628; EC=3.5.1.4;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB60011.1; -; Genomic_DNA.
DR   PIR; T39112; T39112.
DR   RefSeq; NP_595018.1; NM_001020449.2.
DR   AlphaFoldDB; Q9URY4; -.
DR   SMR; Q9URY4; -.
DR   STRING; 4896.SPAC869.01.1; -.
DR   iPTMnet; Q9URY4; -.
DR   SwissPalm; Q9URY4; -.
DR   PaxDb; Q9URY4; -.
DR   PRIDE; Q9URY4; -.
DR   EnsemblFungi; SPAC869.01.1; SPAC869.01.1:pep; SPAC869.01.
DR   GeneID; 2543104; -.
DR   KEGG; spo:SPAC869.01; -.
DR   PomBase; SPAC869.01; -.
DR   VEuPathDB; FungiDB:SPAC869.01; -.
DR   eggNOG; KOG1211; Eukaryota.
DR   HOGENOM; CLU_009600_14_4_1; -.
DR   InParanoid; Q9URY4; -.
DR   OMA; DMRSNNY; -.
DR   PhylomeDB; Q9URY4; -.
DR   PRO; PR:Q9URY4; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..583
FT                   /note="Putative amidase C869.01"
FT                   /id="PRO_0000316204"
FT   ACT_SITE        141
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        246
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   583 AA;  64589 MW;  5EA98820C6120CB2 CRC64;
     MKLQLLFLTL AQLAKHGLAI PLLQSSKTTT NSTLVASQEV NFTTYVYPDT NSTNIFPMPK
     CQNITLEDAT IDQLQNYMEN GILTSTDIVH CYLDRYLQVN PYVNGILQLN PDVLTIASEL
     DDERANGIIR GPLHGIPFIV KDNFATKDKM DTTAGSYALL GSIVPRDAYV VKQLREAGAV
     LFGHATLSEW ADMRSNDYSE GYSARGGQSR CPFNLTVNPG GSSSGSAISV ASNMIAFALG
     TETDGSIIDP AMRNGVVGLK PTVGLTSRYG VIPESEHQDT TGPIARTVRD AVYVFQSMWG
     IDENDIYTLN QTGKTPEDGD YMKFLSNKTS LEGARFGLPW KRLWQNAKAD EIDRLLEVVK
     QIEEAGAIVY NNTNFYNLDV ISNDGWNWEL GSVNESEYTV VKVDFYNNIK SYLSEVKNTE
     IHSLEDIVEY NNKYMGTEGG KPNIVPAFSS GQDGFLASLE WGGVKNETYW QAVEYVRRTS
     QDEGIDYALN YTDPKTNDSF ILNGLLVPSG TSITYQQAAK AGYPMITLPI GVKTNGRPFG
     LGIMHSAWQE PQLIKYGSAI EDLLQYKAKP KFYEYVAKNV PVW