ID   AMDS_EMENI              Reviewed;         548 AA.
AC   P08158; C8V9R2; Q5ASF3;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Acetamidase;
DE            EC=3.5.1.4;
GN   Name=amdS; ORFNames=AN8777;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3036667; DOI=10.1016/0378-1119(87)90093-x;
RA   Corrick C.M., Twomey A.P., Hynes M.J.;
RT   "The nucleotide sequence of the amdS gene of Aspergillus nidulans and the
RT   molecular characterization of 5' mutations.";
RL   Gene 53:63-71(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Allows acetamide to be used as a sole carbon or nitrogen
CC       source.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetamide + H2O = acetate + NH4(+); Xref=Rhea:RHEA:45048,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:27856, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30089; EC=3.5.1.4;
CC   -!- INDUCTION: Acetate induction mediated by facB regulatory gene and
CC       probably by amdA regulatory gene. Omega amino acid induction is
CC       dependent on amdR regulatory gene.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; M16371; AAA33295.1; -; Genomic_DNA.
DR   EMBL; AACD01000161; EAA60570.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF78041.1; -; Genomic_DNA.
DR   PIR; A26511; A26511.
DR   RefSeq; XP_682046.1; XM_676954.1.
DR   AlphaFoldDB; P08158; -.
DR   SMR; P08158; -.
DR   STRING; 162425.CADANIAP00006284; -.
DR   PRIDE; P08158; -.
DR   EnsemblFungi; CBF78041; CBF78041; ANIA_08777.
DR   EnsemblFungi; EAA60570; EAA60570; AN8777.2.
DR   GeneID; 2868318; -.
DR   KEGG; ani:AN8777.2; -.
DR   VEuPathDB; FungiDB:AN8777; -.
DR   eggNOG; KOG1212; Eukaryota.
DR   HOGENOM; CLU_009600_9_2_1; -.
DR   InParanoid; P08158; -.
DR   OMA; HQLVNCA; -.
DR   OrthoDB; 852596at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0004040; F:amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043864; F:indoleacetamide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034251; P:regulation of cellular amide catabolic process; IMP:AspGD.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..548
FT                   /note="Acetamidase"
FT                   /id="PRO_0000105129"
FT   ACT_SITE        129
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        204
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        228
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   548 AA;  60229 MW;  1EC6368CB867C630 CRC64;
     MPQSWEELAA DKRARLAKTI PDEWKVQTLP AEDSVIDFPK KSGILSEAEL KITEASAADL
     VSKLAAGELT SVEVTLAFCK RAAIAQQLTN CAHEFFPDAA LAQARELDEY YAKHKRPVGP
     LHGLPISLKD QLRVKGYETS MGYISWLNKY DEGDSVLTTM LRKAGAVFYV KTSVPQTLMV
     CETVNNIIGR TVNPRNKNWS CGGSSGGEGA IVGIRGGVIG VGTDIGGSIR VPAAFNFLYG
     LRPSHGRLPY AKMANSMEGQ ETVHSVVGPI THSVEDLRLF TKSVLGQEPW KYDSKVIPMP
     WRQSESDIIA SKIKNGGLNI GYYNFDGNVL PHPPILRGVE TTVAALAKAG HTVTPWTPYK
     HDFGHDLISH IYAADGSADV MRDISASGEP AIPNIKDLLN PNIKAVNMNE LWDTHLQKWN
     YQMEYLEKWR EAEEKAGKEL DAIIAPITPT AAVRHDQFRY YGYASVINLL DFTSVVVPVT
     FADKNIDKKN ESFKAVSELD ALVQEEYDPE AYHGAPVAVQ VIGRRLSEER TLAIAEEVGK
     LLGNVVTP