ID   NIT2B_XENLA             Reviewed;         276 AA.
AC   Q6INI7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Omega-amidase NIT2-B;
DE            EC=3.5.1.3 {ECO:0000250|UniProtKB:Q9NQR4};
DE   AltName: Full=Nitrilase homolog 2;
GN   Name=nit2b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) 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; BC072293; AAH72293.1; -; mRNA.
DR   RefSeq; NP_001085409.1; NM_001091940.1.
DR   AlphaFoldDB; Q6INI7; -.
DR   SMR; Q6INI7; -.
DR   PRIDE; Q6INI7; -.
DR   DNASU; 443835; -.
DR   GeneID; 443835; -.
DR   KEGG; xla:443835; -.
DR   OrthoDB; 1154369at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 443835; Expressed in testis and 19 other tissues.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
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-B"
FT                   /id="PRO_0000320259"
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;  30764 MW;  79FEC1A99847A97A CRC64;
     MAKFRLSLVQ FLVSPVKSDN LNKACKLIKE AAQKGAQIVA LPECFNSPYG TKYFPEYAEK
     IPGESTELLS QVAKECGIYL IGGSIPEEDS GKFYNTCAVF GPDGTLLVKH RKIHLFDIDV
     PGKIRFQESE TLSPGDSFSV FDTPYCKVGV GICYDMRFAE LAQIYANKGC QLLVYPGAFN
     MTTGPAHWEL LQRARALDNQ VYVATASPAR DEKASYVAWG HSTVVSPWGE VIAKAGFEET
     VISADIDLQY LAEIREQIPI RRQRRDNLYT VEEKKN