ID   YAFV_ECOBD              Reviewed;         256 AA.
AC   A0A140NDS5;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Omega-amidase YafV;
DE            Short=ecYafV {ECO:0000303|PubMed:28373563};
DE            EC=3.5.1.3 {ECO:0000269|PubMed:28373563};
GN   Name=yafV; OrderedLocusNames=ECBD_3403;
OS   Escherichia coli (strain B / BL21-DE3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=469008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / BL21-DE3;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.;
RT   "Complete sequence of Escherichia coli BL21(DE3).";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=B / BL21;
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 6.65
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; CP001665; ACT30403.1; -; Genomic_DNA.
DR   RefSeq; WP_001118052.1; NZ_CP053602.1.
DR   AlphaFoldDB; A0A140NDS5; -.
DR   SMR; A0A140NDS5; -.
DR   STRING; 469008.B21_00218; -.
DR   KEGG; ebd:ECBD_3403; -.
DR   PATRIC; fig|469008.15.peg.218; -.
DR   eggNOG; COG0388; Bacteria.
DR   HOGENOM; CLU_030130_3_7_6; -.
DR   OMA; KIHRFGF; -.
DR   Proteomes; UP000002032; Chromosome.
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..256
FT                   /note="Omega-amidase YafV"
FT                   /id="PRO_0000440692"
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;  28953 MW;  1394D16498D23C30 CRC64;
     MPGLKITLLQ QPLVWMDGPA NLRHFDRQLE GITGRDVIVL PEMFTSGFAM EAAASSLAQD
     DVVNWMTAKA QQCNALIAGS VALQTESGSV NRFLLVEPGG TVHFYDKRHL FRMVDEHLHY
     KAGNARVIVE WRGWRILPLV CYDLRFPVWS RNLNDYDLAL YVANWPAPRS LHWQALLTAR
     AIENQAYVAG CNRVGSDGNG CHYRGDSRVI NPQGEIIATA DAHQATRIDA ELSMAALREY
     REKFPAWQDA DEFRLW