ID NIT2_PONAB Reviewed; 275 AA.
AC Q5R4L6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 64.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-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; CR861230; CAH93300.1; -; Transcribed_RNA.
DR AlphaFoldDB; Q5R4L6; -.
DR SMR; Q5R4L6; -.
DR STRING; 9601.ENSPPYP00000015207; -.
DR InParanoid; Q5R4L6; -.
DR Proteomes; UP000001595; 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; 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; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR045254; Nit1/2_C-N_Hydrolase.
DR PANTHER; PTHR23088; NITRILASE-RELATED; 1.
DR PANTHER; PTHR23088:SF30; OMEGA-AMIDASE NIT2; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT CHAIN 1..275
FT /note="Omega-amidase NIT2"
FT /id="PRO_0000320255"
FT DOMAIN 4..247
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 152
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 275 AA; 30483 MW; 940793DB9A2F348B CRC64;
MASFRLALIQ LQISSINSDN VTRACSFIRE AATQGAKIVS LPECFNSPYG TKYFPEYAEK
IPGESTQKLS EVAKECSIYL IGGSIPEEDA GKLYNTCAVF GPDGTLLAKY RKIHLFDIDV
PGKITFQESK TLSPGDSFCT FDTYCRVGLG ICYDMRFAEL AQIYAQRGCQ LLVYPGAFNL
TTGPAHWELL QRGRAVDNQV YVATASPARD DKASYVAWGH STVVNPWGEV LAKAGTEEAI
VYSDIDLKKL AEIRQQIPVF RQKRSDLYAV EMKKP
//
