ID   NIT2_BOVIN              Reviewed;         276 AA.
AC   Q2T9R6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Omega-amidase NIT2;
DE            EC=3.5.1.3 {ECO:0000250|UniProtKB:Q9NQR4};
DE   AltName: Full=Nitrilase homolog 2;
GN   Name=NIT2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has omega-amidase activity. The role of omega-amidase is to
CC       remove potentially toxic intermediates by converting 2-oxoglutaramate
CC       and 2-oxosuccinamate to biologically useful 2-oxoglutarate and
CC       oxaloacetate, respectively. {ECO:0000250|UniProtKB:Q9NQR4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutaramate + H2O = 2-oxoglutarate + NH4(+);
CC         Xref=Rhea:RHEA:32963, ChEBI:CHEBI:15377, ChEBI:CHEBI:16769,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:28938; EC=3.5.1.3;
CC         Evidence={ECO:0000250|UniProtKB:Q9NQR4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32964;
CC         Evidence={ECO:0000250|UniProtKB:Q9NQR4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxosuccinamate + H2O = NH4(+) + oxaloacetate;
CC         Xref=Rhea:RHEA:59412, ChEBI:CHEBI:15377, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57735; EC=3.5.1.3;
CC         Evidence={ECO:0000250|UniProtKB:Q9NQR4};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59413;
CC         Evidence={ECO:0000250|UniProtKB:Q9NQR4};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9NQR4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NQR4}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
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DR   EMBL; BC111301; AAI11302.1; -; mRNA.
DR   RefSeq; NP_001033222.1; NM_001038133.1.
DR   AlphaFoldDB; Q2T9R6; -.
DR   SMR; Q2T9R6; -.
DR   STRING; 9913.ENSBTAP00000006347; -.
DR   PaxDb; Q2T9R6; -.
DR   PeptideAtlas; Q2T9R6; -.
DR   PRIDE; Q2T9R6; -.
DR   GeneID; 520620; -.
DR   KEGG; bta:520620; -.
DR   CTD; 56954; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   InParanoid; Q2T9R6; -.
DR   OrthoDB; 1154369at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106008; F:2-oxoglutaramate amidase activity; IEA:RHEA.
DR   GO; GO:0050152; F:omega-amidase activity; IBA:GO_Central.
DR   GO; GO:0006528; P:asparagine metabolic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IBA:GO_Central.
DR   CDD; cd07572; nit; 1.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Omega-amidase NIT2"
FT                   /id="PRO_0000320253"
FT   DOMAIN          4..248
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        43
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        112
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   MOD_RES         68
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHW2"
FT   MOD_RES         68
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHW2"
FT   MOD_RES         123
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHW2"
SQ   SEQUENCE   276 AA;  30518 MW;  8744F496C6F54F32 CRC64;
     MATFRLALIQ LQVSSIKSEN LTRACGLIRE ASKQGAQIVS LPECFNSPYG TKYFPDYAEK
     IPGDSTQKLS EVAKECSMYV IGGSIPEKDA GKLYNTCAVF GPDGTLLVKH RKLHLFDIDV
     PGKITFQESE TLSPGDSFSL FDTPYCRVGL GICYDIRFAE LAQIYAQRGC QLLVYPGAFN
     LTTGPAHWEL LQRGRAVDNQ VYVATASPAR DEKASYVAWG HSTVVNPWGE VLAKAGTEET
     IVYADIDLKK LAEIRQQIPI FSQKRSDLYE VEAKKS