ID   NIT2_XENTR              Reviewed;         276 AA.
AC   Q28IE5; Q5BKE8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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; ORFNames=TNeu073c04.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-276.
RC   STRAIN=F6;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-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; CR760444; CAJ82781.1; -; mRNA.
DR   EMBL; BC091101; AAH91101.1; -; mRNA.
DR   RefSeq; NP_001016633.1; NM_001016633.1.
DR   AlphaFoldDB; Q28IE5; -.
DR   SMR; Q28IE5; -.
DR   STRING; 8364.ENSXETP00000025924; -.
DR   PaxDb; Q28IE5; -.
DR   GeneID; 549387; -.
DR   KEGG; xtr:549387; -.
DR   CTD; 56954; -.
DR   Xenbase; XB-GENE-946902; nit2.
DR   eggNOG; KOG0806; Eukaryota.
DR   HOGENOM; CLU_030130_1_0_1; -.
DR   InParanoid; Q28IE5; -.
DR   OrthoDB; 1154369at2759; -.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; 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   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Omega-amidase NIT2"
FT                   /id="PRO_0000320260"
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"
SQ   SEQUENCE   276 AA;  30805 MW;  98ADA0FB5674631A CRC64;
     MAKFRLSLVQ FLVSPVKSEN LNRACKLIKE AAQKGAQIVA LPECFNSPYG TKYFPEYAEK
     IPGESTERLS QVAKECGIYL IGGSIPEEDS GKLYNTCAVF GPDGTLLVKH RKIHLFDIDV
     PGKIRFQESE TLSPGDSFSV FETPYCKVGV GICYDIRFAE LAQLYSKKGC QLLVYPGAFN
     MTTGPAHWEL LQRARALDNQ VYVATASPAR DEKASYVAWG HSTIVSPWGE VIAKAGSEET
     VISADIDLEY LAEIREQIPI RRQRRHDLYS VEEKKN