ID   YAFV_YEREN              Reviewed;         256 AA.
AC   P0DP67;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Omega-amidase YafV;
DE            Short=yeYafV {ECO:0000303|PubMed:28373563};
DE            EC=3.5.1.3 {ECO:0000269|PubMed:28373563};
GN   Name=yafV {ECO:0000303|PubMed:28373563}; ORFNames=CH48_2603;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2516-87;
RA   Davenport K.W., Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O.,
RA   Coyne S.R., Daligault H.E., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RC   STRAIN=2516-87;
RX   PubMed=28373563; DOI=10.1073/pnas.1613736114;
RA   Peracchi A., Veiga-da-Cunha M., Kuhara T., Ellens K.W., Paczia N.,
RA   Stroobant V., Seliga A.K., Marlaire S., Jaisson S., Bommer G.T., Sun J.,
RA   Huebner K., Linster C.L., Cooper A.J.L., Van Schaftingen E.;
RT   "Nit1 is a metabolite repair enzyme that hydrolyzes deaminated
RT   glutathione.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:E3233-E3242(2017).
CC   -!- FUNCTION: Hydrolyzes alpha-ketoglutaramate (a-KGM) to alpha-
CC       ketoglutarate (alpha-KG) and ammonia (specific activity 21
CC       umol/min/mg), has very weak activity on L-glutamine, and no activity on
CC       deaminated glutathione (dGSH) or glutathione. May function as a
CC       metabolite repair enzyme. {ECO:0000269|PubMed:28373563}.
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:28373563};
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       NIT1/NIT2 family. {ECO:0000305}.
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DR   EMBL; CP009838; AJJ26717.1; -; Genomic_DNA.
DR   RefSeq; WP_005164983.1; NZ_UHIX01000001.1.
DR   AlphaFoldDB; P0DP67; -.
DR   SMR; P0DP67; -.
DR   KEGG; yet:CH48_2603; -.
DR   OMA; KIHRFGF; -.
DR   GO; GO:0050152; F:omega-amidase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..256
FT                   /note="Omega-amidase YafV"
FT                   /id="PRO_0000440698"
FT   DOMAIN          4..234
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        141
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   256 AA;  29269 MW;  06614ECA1DF93F56 CRC64;
     MSTLKLTLLQ QPLVWLDAQA NLRHFDMLLE SIQQRDVIVL PEMFTTGFAM NAAENALPET
     EVIDWLRHWS VRTDALIGGS VALNTPDGAV NRFLLVQPDG TILRYDKRHL FRMAGEHHHY
     LAGKERKVVE WRGWRILPQV CYDLRFPVWS RNQQDYDLAL YVANWPAARA KHWQTLLAAR
     AIENQAYVAG CNRVGDDDNG HHYQGNSVIL DALGEIQAQA EPGQAAQLDA ELSLETLQAY
     RERFPAFHDT DKFLLL