ID   NIT_PAENI               Reviewed;         294 AA.
AC   Q93NG1;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=2-oxoglutaramate amidase;
DE            EC=3.5.1.111 {ECO:0000269|PubMed:21288482};
DE   AltName: Full=Omega-amidase;
OS   Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG   Plasmid pAO1.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX   NCBI_TaxID=29320;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11514508; DOI=10.1128/jb.183.18.5262-5267.2001;
RA   Baitsch D., Sandu C., Brandsch R., Igloi G.L.;
RT   "Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in
RT   degradation of the plant alkaloid nicotine: cloning, purification, and
RT   characterization of 2,6-dihydroxypyridine 3-hydroxylase.";
RL   J. Bacteriol. 183:5262-5267(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12618462; DOI=10.1128/jb.185.6.1976-1986.2003;
RA   Igloi G.L., Brandsch R.;
RT   "Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter
RT   nicotinovorans and identification of a pAO1-dependent nicotine uptake
RT   system.";
RL   J. Bacteriol. 185:1976-1986(2003).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21288482; DOI=10.1016/j.resmic.2011.01.001;
RA   Cobzaru C., Ganas P., Mihasan M., Schleberger P., Brandsch R.;
RT   "Homologous gene clusters of nicotine catabolism, including a new omega-
RT   amidase for alpha-ketoglutaramate, in species of three genera of Gram-
RT   positive bacteria.";
RL   Res. Microbiol. 162:285-291(2011).
CC   -!- FUNCTION: Catalyzes the conversion of 2-oxoglutaramate to 2-
CC       oxoglutarate. Together with glutamate dehydrogenase, may form a
CC       physiologically relevant enzyme couple, leading to transformation of
CC       metabolically inert 2-oxoglutaramate derived from trihydroxypyridine
CC       into glutamate, a central compound of nitrogen metabolism.
CC       {ECO:0000269|PubMed:21288482}.
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=3.5.1.111;
CC         Evidence={ECO:0000269|PubMed:21288482};
CC   -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
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DR   EMBL; AF373840; AAK64257.1; -; Genomic_DNA.
DR   EMBL; AJ507836; CAD47935.1; -; Genomic_DNA.
DR   RefSeq; WP_016359446.1; NC_021229.1.
DR   RefSeq; YP_007988761.1; NC_021229.1.
DR   AlphaFoldDB; Q93NG1; -.
DR   SMR; Q93NG1; -.
DR   KEGG; ag:CAD47935; -.
DR   BioCyc; MetaCyc:MON-17151; -.
DR   BRENDA; 3.5.1.111; 449.
DR   UniPathway; UPA00106; -.
DR   GO; GO:0106008; F:2-oxoglutaramate amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   InterPro; IPR001110; UPF0012_CS.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
DR   PROSITE; PS01227; UPF0012; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Plasmid.
FT   CHAIN           1..294
FT                   /note="2-oxoglutaramate amidase"
FT                   /id="PRO_0000424219"
FT   DOMAIN          16..261
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        55
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        168
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   294 AA;  32665 MW;  046E1763D51E8CFA CRC64;
     MNLMEVRELA PSRGQLDVAA VQVKFDSTEL LEDRISRIQD LVSGVGKADL IVLPELWLHG
     GFSYDSWRKN AISLESEVFT FLSEVARDKK AWFHAGSFMV TEPSSAASDM WNTSVLFDPT
     GSLRATYKKI HRFGFSDGEP KLIAAGDEPR VVELQTERAT AITGLSTCYD LRFPELYRHI
     SAEGTALNVI PACWPLTRIQ HWQTLGRARA IENQSFVVQC NMTGVDQEVE LGGHSQIVDG
     NGDILAQADK EEAVLRATLN FDSLNELRSS FPVLNDRRAD IWAAKGKTVI ASHL