YAFV_ECOLI
ID YAFV_ECOLI Reviewed; 256 AA.
AC Q47679; Q9R2E1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Omega-amidase YafV;
DE EC=3.5.1.3 {ECO:0000250|UniProtKB:A0A140NDS5};
GN Name=yafV; OrderedLocusNames=b0219, JW5019;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Hydrolyzes alpha-ketoglutaramate (a-KGM) to alpha-
CC ketoglutarate (alpha-KG) and ammonia, has weak activity on L-glutamine,
CC almost no activity on deaminated glutathione (dGSH) and none on
CC glutathione (By similarity). May function as a metabolite repair enzyme
CC (By similarity). {ECO:0000250|UniProtKB:A0A140NDS5}.
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:0000250|UniProtKB:A0A140NDS5};
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC NIT1/NIT2 family. {ECO:0000305}.
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DR EMBL; U70214; AAB08641.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73323.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77889.2; -; Genomic_DNA.
DR PIR; D64746; D64746.
DR RefSeq; NP_414754.1; NC_000913.3.
DR RefSeq; WP_001118036.1; NZ_SSZK01000029.1.
DR AlphaFoldDB; Q47679; -.
DR SMR; Q47679; -.
DR BioGRID; 4261824; 18.
DR DIP; DIP-11225N; -.
DR STRING; 511145.b0219; -.
DR jPOST; Q47679; -.
DR PaxDb; Q47679; -.
DR PRIDE; Q47679; -.
DR EnsemblBacteria; AAC73323; AAC73323; b0219.
DR EnsemblBacteria; BAA77889; BAA77889; BAA77889.
DR GeneID; 946585; -.
DR KEGG; ecj:JW5019; -.
DR KEGG; eco:b0219; -.
DR PATRIC; fig|1411691.4.peg.2064; -.
DR EchoBASE; EB3118; -.
DR eggNOG; COG0388; Bacteria.
DR HOGENOM; CLU_030130_3_7_6; -.
DR InParanoid; Q47679; -.
DR OMA; KIHRFGF; -.
DR PhylomeDB; Q47679; -.
DR BioCyc; EcoCyc:G6103-MON; -.
DR BioCyc; MetaCyc:G6103-MON; -.
DR PRO; PR:Q47679; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0106008; F:2-oxoglutaramate amidase activity; IDA:EcoCyc.
DR GO; GO:0050152; F:omega-amidase activity; IDA:EcoCyc.
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; Reference proteome.
FT CHAIN 1..256
FT /note="Omega-amidase YafV"
FT /id="PRO_0000213257"
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 /note="Proton donor"
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; 28925 MW; 7C2381648065660C CRC64;
MPGLKITLLQ QPLVWMDGPA NLRHFDRQLE GITGRDVIVL PEMFTSGFAM EAAASSLAQD
DVVNWMTAKA QQCNALIAGS VALQTESGSV NRFLLVEPGG TVHFYDKRHL FRMADEHLHY
KAGNARVIVE WRGWRILPLV CYDLRFPVWS RNLNDYDLAL YVANWPAPRS LHWQALLTAR
AIENQAYVAG CNRVGSDGNG CHYRGDSRVI NPQGEIIATA DAHQATRIDA ELSMAALREY
REKFPAWQDA DEFRLW
