ID   NIT2_RAT                Reviewed;         276 AA.
AC   Q497B0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Omega-amidase NIT2;
DE            EC=3.5.1.3 {ECO:0000269|PubMed:19595734};
DE   AltName: Full=Nitrilase homolog 2;
GN   Name=Nit2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION.
RX   PubMed=19464248; DOI=10.1016/j.ab.2009.05.025;
RA   Krasnikov B.F., Nostramo R., Pinto J.T., Cooper A.J.L.;
RT   "Assay and purification of omega-amidase/Nit2, a ubiquitously expressed
RT   putative tumor suppressor, that catalyzes the deamidation of the alpha-keto
RT   acid analogues of glutamine and asparagine.";
RL   Anal. Biochem. 391:144-150(2009).
RN   [3]
RP   FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=19595734; DOI=10.1016/j.biochi.2009.07.003;
RA   Krasnikov B.F., Chien C.-H., Nostramo R., Pinto J.T., Nieves E.,
RA   Callaway M., Sun J., Huebner K., Cooper A.J.L.;
RT   "Identification of the putative tumor suppressor Nit2 as omega-amidase, an
RT   enzyme metabolically linked to glutamine and asparagine transamination.";
RL   Biochimie 91:1072-1080(2009).
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:0000269|PubMed:19464248,
CC       ECO:0000269|PubMed:19595734}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a monoamide of a dicarboxylate + H2O = a dicarboxylate +
CC         NH4(+); Xref=Rhea:RHEA:11716, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:77450; EC=3.5.1.3;
CC         Evidence={ECO:0000269|PubMed:19595734};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11717;
CC         Evidence={ECO:0000269|PubMed:19595734};
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:0000269|PubMed:19595734};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32964;
CC         Evidence={ECO:0000269|PubMed:19595734};
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:0000269|PubMed:19464248};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59413;
CC         Evidence={ECO:0000269|PubMed:19464248};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.0054 mM for 2-oxoglutaramate (open-chain form)
CC         {ECO:0000269|PubMed:19595734};
CC         Vmax=20.6 umol/min/mg enzyme with 2-oxoglutaramate as substrate
CC         {ECO:0000269|PubMed:19595734};
CC         Note=In solution, 2-oxoglutaramate is in equilibrium with a cyclic
CC         form (2-hydroxy-5-oxoproline), and at pH 8.0 or above, the rate of
CC         ring opening is no longer limiting for the omega-amidase reaction.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19595734}.
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; BC100637; AAI00638.1; -; mRNA.
DR   RefSeq; NP_001029298.1; NM_001034126.1.
DR   AlphaFoldDB; Q497B0; -.
DR   SMR; Q497B0; -.
DR   BioGRID; 252479; 1.
DR   STRING; 10116.ENSRNOP00000034144; -.
DR   iPTMnet; Q497B0; -.
DR   PhosphoSitePlus; Q497B0; -.
DR   jPOST; Q497B0; -.
DR   PaxDb; Q497B0; -.
DR   PRIDE; Q497B0; -.
DR   GeneID; 288174; -.
DR   KEGG; rno:288174; -.
DR   UCSC; RGD:1310494; rat.
DR   CTD; 56954; -.
DR   RGD; 1310494; Nit2.
DR   VEuPathDB; HostDB:ENSRNOG00000027797; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   HOGENOM; CLU_030130_1_0_1; -.
DR   InParanoid; Q497B0; -.
DR   OMA; GNTYRES; -.
DR   OrthoDB; 1154369at2759; -.
DR   PhylomeDB; Q497B0; -.
DR   TreeFam; TF300747; -.
DR   Reactome; R-RNO-6798695; Neutrophil degranulation.
DR   PRO; PR:Q497B0; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000027797; Expressed in kidney and 19 other tissues.
DR   Genevisible; Q497B0; RN.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0106008; F:2-oxoglutaramate amidase activity; IEA:RHEA.
DR   GO; GO:0050152; F:omega-amidase activity; ISO:RGD.
DR   GO; GO:0006528; P:asparagine metabolic process; ISO:RGD.
DR   GO; GO:0006541; P:glutamine metabolic process; ISO:RGD.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; ISO:RGD.
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   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..276
FT                   /note="Omega-amidase NIT2"
FT                   /id="PRO_0000320256"
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         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQR4"
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"
FT   MOD_RES         130
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHW2"
SQ   SEQUENCE   276 AA;  30701 MW;  38C64D674B171EF3 CRC64;
     MSTFRLALIQ LQVSSIKSDN ITRACSLVRE AAKQGANIVS LPECFNSPYG TNYFPEYAEK
     IPGESTKKLS EVAKENSIYL IGGSIPEEDD GKLYNTCAVF GPDGNLLVKH RKIHLFDIDV
     PGKITFQESK TLSPGDSFST FDTPYCRVGL GICYDMRFAE LAQIYARRGC QLLVYPGAFN
     MTTGPAHWEL LQRARAVDNQ VYVATASPAR DEKASYVAWG HSTVVDPWGQ VLTKAGTEET
     ILYSDIDLKK LSEIRQQIPI LKQKRADLYS VESKKP