ID A0A0E9NLP5_SAICN Unreviewed; 661 AA.
AC A0A0E9NLP5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN ORFNames=G7K_4725-t1 {ECO:0000313|EMBL:GAO50601.1};
OS Saitoella complicata (strain BCRC 22490 / CBS 7301 / JCM 7358 / NBRC 10748
OS / NRRL Y-17804).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Taphrinomycotina incertae sedis; Saitoella.
OX NCBI_TaxID=698492 {ECO:0000313|EMBL:GAO50601.1, ECO:0000313|Proteomes:UP000033140};
RN [1] {ECO:0000313|EMBL:GAO50601.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO50601.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=21914972; DOI=10.2323/jgam.57.243;
RA Nishida H., Hamamoto M., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic yeast Saitoella complicata.";
RL J. Gen. Appl. Microbiol. 57:243-246(2011).
RN [2] {ECO:0000313|EMBL:GAO50601.1, ECO:0000313|Proteomes:UP000033140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-17804 {ECO:0000313|EMBL:GAO50601.1,
RC ECO:0000313|Proteomes:UP000033140};
RX PubMed=24646756; DOI=10.2323/jgam.60.7;
RA Nishida H., Matsumoto T., Kondo S., Hamamoto M., Yoshikawa H.;
RT "The early diverging ascomycetous budding yeast Saitoella complicata has
RT three histone deacetylases belonging to the Clr6, Hos2, and Rpd3
RT lineages.";
RL J. Gen. Appl. Microbiol. 60:7-12(2014).
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 Evidence={ECO:0000256|ARBA:ARBA00001311};
CC -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO50601.1}.
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DR EMBL; BACD03000034; GAO50601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9NLP5; -.
DR STRING; 698492.A0A0E9NLP5; -.
DR OMA; QFKYYGY; -.
DR Proteomes; UP000033140; 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 Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR PANTHER; PTHR46072:SF9; ACETAMIDASE; 1.
DR PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000033140}.
FT DOMAIN 196..647
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 74..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 73201 MW; 7AE6C23CB8DD0D14 CRC64;
MSCGRRRRND SAGSCLPDLN FYFADHFDEQ RKVWSFPGIE GLGSEVTRMK HGDGIRASGG
ARAGVLALRG QWPRKTGTGR AERSRWHKKT HSSQGLGSSA TRRPYLVGLI SPLKTRHTIS
RMAKWEELVK AKREALANQI PSEWKLQSPP SEDEKRVIDF PEKSGLFTKE ELEITGLDAA
TLVKKLQARE LKAYDVAKAF CHRAAVAQQL VNCCAEIFFE KALAQAKELD DYYEKNGKPI
GPLHGLPVSL KDQFRVKGEQ CAMGYVGWIG KKDEKDSVLT ECLRSAGAVF YVKTTVPQSL
MVGETLNNIT GRTVNPYNRG LSCGGSSGGE GALVGFHGSP IGVGTDIGGS IRMPAAFNGL
FGIRPSHGRM PYAGAANSME GQETVHSVCG PMAHTAESLT EFLKGVLSQH PWDFDPKVIE
LPWRQEIYEE ARVAKKLRIG ILTTDGVVDP QPPIKRGLEQ TRKALEAAGH EVVEFAPMDH
ARGVDIINRI YVVDAGKDIQ NALEASGEPM IDNLKVLVDL DNMSTPLTIN QGWDLNLEKY
KYQSEYLEYL KKNPVDAFIM PVAPHAAVRH DHYFYYGYTS IINLLDYTSV VFPVGFQDPS
IDKKDESYKP RSDLDKQVYE DYVPELYDGA PISLQIVGRR LTEEKVLGFA EVVAKALKAQ
A
//
