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Database: UniProt
Entry: J7RVT6_KAZNA
LinkDB: J7RVT6_KAZNA
Original site: J7RVT6_KAZNA 
ID   J7RVT6_KAZNA            Unreviewed;       581 AA.
AC   J7RVT6;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=amidase {ECO:0000256|ARBA:ARBA00012922};
DE            EC=3.5.1.4 {ECO:0000256|ARBA:ARBA00012922};
GN   Name=KNAG0B06280 {ECO:0000313|EMBL:CCK69057.1};
GN   OrderedLocusNames=KNAG_0B06280 {ECO:0000313|EMBL:CCK69057.1};
OS   Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS   17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS   naganishii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK69057.1, ECO:0000313|Proteomes:UP000006310};
RN   [1] {ECO:0000313|EMBL:CCK69057.1, ECO:0000313|Proteomes:UP000006310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC   / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN   [2] {ECO:0000313|Proteomes:UP000006310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC   / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Genome sequence of Kazachstania naganishii.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; HE978315; CCK69057.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7RVT6; -.
DR   STRING; 1071383.J7RVT6; -.
DR   eggNOG; KOG1212; Eukaryota.
DR   HOGENOM; CLU_009600_9_2_1; -.
DR   OMA; RMTEFAF; -.
DR   OrthoDB; 731186at2759; -.
DR   Proteomes; UP000006310; Chromosome 2.
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:SF4; AMIDASE C550.07-RELATED; 1.
DR   PANTHER; PTHR46072; AMIDASE-RELATED-RELATED; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   PIRSF; PIRSF001221; Amidase_fungi; 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:UP000006310}.
FT   DOMAIN          112..565
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   ACT_SITE        168
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT   ACT_SITE        243
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT   ACT_SITE        267
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-1"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT   BINDING         243
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
FT   BINDING         264..267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001221-2"
SQ   SEQUENCE   581 AA;  64972 MW;  1EABCBB9310C59FE CRC64;
     MATKIIERLY NTDPELTYKP DLVKYETVHL PKITSYREEL ASKFPQETVL KPGLLADKGI
     EIPLDFESSV FKDGPKLAKA SGFFTDRELE ILELKAIEII ERIAAGEQTA LETITAFIKQ
     AAIAQQVTNC AMDFFPEEAF ERARELDKYF AETGKTVGPM HGLPVSVKEH YAFKGKVTSC
     GFVSKLNDVE EIDAYITDLF KKTGAVYYIR TTQPQTIMHL DSFNNIIGLC RNPYNTALSP
     GGSSSGEAAL VGMRGSPLGC GSDIGGSIRC PAAFCNIWGL KPTARRLSCL GSRSQFTKHS
     NEMILPTFGP MANSADDLEL FMKVCSDSKP WLYDNYVLRM PWIKDVKFAI GDLKIAIVLD
     DGVVKPSPPI LRALLLAKKA LESAGVGKII EWESFKTVEA LEICYNAYTK DGNFNARAVL
     GASGEPLAPL TEHYMRFGTG DKKLSNLEIM ECENRRDVLR QEFQLKMNER DIDFILTPAY
     FAPAGIPHKI KYWGYTAVYN ILDLPGVSFP TGIKVNKSID KKDVNYQPRN DMEEYEYPMY
     DEEVYDGMPI GLMLQGRRYH DEETLAAAKL IQEVISKASR T
//
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