ID   YAFV_STAA4              Reviewed;         261 AA.
AC   P0DP65;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Omega-amidase YafV;
DE            Short=saYafV {ECO:0000303|PubMed:28373563};
DE            EC=3.5.1.3 {ECO:0000269|PubMed:28373563};
GN   Name=yafV {ECO:0000303|PubMed:28373563};
GN   Synonyms=amiE {ECO:0000303|PubMed:20386717}; OrderedLocusNames=SA2981_1975;
OS   Staphylococcus aureus (strain 04-02981).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=703339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=04-02981;
RX   PubMed=20386717; DOI=10.1371/journal.ppat.1000855;
RA   Nubel U., Dordel J., Kurt K., Strommenger B., Westh H., Shukla S.K.,
RA   Zemlickova H., Leblois R., Wirth T., Jombart T., Balloux F., Witte W.;
RT   "A timescale for evolution, population expansion, and spatial spread of an
RT   emerging clone of methicillin-resistant Staphylococcus aureus.";
RL   PLoS Pathog. 6:E1000855-E1000855(2010).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=04-02981;
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 3.87
CC       umol/min/mg), has weak activity on L-glutamine, almost no activity on
CC       deaminated glutathione (dGSH) and none on glutathione. May function as
CC       a 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; CP001844; ADC38186.1; -; Genomic_DNA.
DR   RefSeq; WP_000867951.1; NC_017340.1.
DR   AlphaFoldDB; P0DP65; -.
DR   SMR; P0DP65; -.
DR   KEGG; suy:SA2981_1975; -.
DR   HOGENOM; CLU_030130_3_1_9; -.
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   1: Evidence at protein level;
KW   Hydrolase.
FT   CHAIN           1..261
FT                   /note="Omega-amidase YafV"
FT                   /id="PRO_0000440695"
FT   DOMAIN          1..239
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        41
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        146
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ   SEQUENCE   261 AA;  29840 MW;  99C197D6BB4811EC CRC64;
     MKVQIYQLPI IFGDSSKNET QITQWFEKNM NAEVDVVVLP EMWNNGYDLE HLNEKADNNL
     GQSFSFIKHL AEKYKVDIVA GSVSNIRNYQ IFNTAFSVNK SGQLINEYDK VHLVPMLREH
     EFLTAGENVA EPFQLSDGTY VTQLICYDLR FPELLRYPAR SGAKIAFYVA QWPMSRLQHW
     HSLLKARAIE NNMFVIGTNS TGFDGNTEYA GHSIVINPNG DLVGELNESA DILTVDLNLN
     EVEQQRENIP VFKSIKLDLY K