ID   NIT2_DANRE              Reviewed;         277 AA.
AC   Q4VBV9; Q6TGW8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=zgc:109720;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney marrow;
RX   PubMed=15520368; DOI=10.1073/pnas.0407241101;
RA   Song H.-D., Sun X.-J., Deng M., Zhang G.-W., Zhou Y., Wu X.-Y., Sheng Y.,
RA   Chen Y., Ruan Z., Jiang C.-L., Fan H.-Y., Zon L.I., Kanki J.P., Liu T.X.,
RA   Look A.T., Chen Z.;
RT   "Hematopoietic gene expression profile in zebrafish kidney marrow.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-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; AY398388; AAQ97821.1; -; mRNA.
DR   EMBL; BC094964; AAH94964.1; -; mRNA.
DR   AlphaFoldDB; Q4VBV9; -.
DR   SMR; Q4VBV9; -.
DR   STRING; 7955.ENSDARP00000121828; -.
DR   PaxDb; Q4VBV9; -.
DR   PeptideAtlas; Q4VBV9; -.
DR   ZFIN; ZDB-GENE-050522-65; nit2.
DR   eggNOG; KOG0806; Eukaryota.
DR   InParanoid; Q4VBV9; -.
DR   PhylomeDB; Q4VBV9; -.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   PRO; PR:Q4VBV9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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..277
FT                   /note="Omega-amidase NIT2"
FT                   /id="PRO_0000320257"
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   CONFLICT        29
FT                   /note="K -> T (in Ref. 1; AAQ97821)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   277 AA;  30366 MW;  366BE00B4214A687 CRC64;
     MSKFRLAVVQ LHVSKIKADN LGRAQTLVKE AAGQGAKVVV LPECFNSPYG TGFFKEYAEK
     IPGESTQVLS ETAKKCGIYL VGGSIPEEDG GKLYNTCSVF GPDGTLLVTH RKIHLFDIDV
     PGKIRFQESE TLSPGKSLSM FETPYCKVGV GICYDIRFAE LAQIYAKKGC QLLVYPGAFN
     MTTGPAHWEL LQRGRAVDNQ VYVATASPAR DETASYVAWG HSSVINPWGE VISKAGSEES
     VVYADIDLQY LADVRQQIPI TKQRRNDLYS VNSVQEG