ID A0A0S2DNS2_LYSEN Unreviewed; 482 AA.
AC A0A0S2DNS2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ALN60144.1, ECO:0000313|EMBL:QCW28148.1};
GN ORFNames=FE772_23345 {ECO:0000313|EMBL:QCW28148.1}, GLE_4803
GN {ECO:0000313|EMBL:ALN60144.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN60144.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN60144.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN60144.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCW28148.1, ECO:0000313|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36 {ECO:0000313|EMBL:QCW28148.1,
RC ECO:0000313|Proteomes:UP000308311};
RA Feng T.;
RT "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013140; ALN60144.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW28148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2DNS2; -.
DR STRING; 69.GLE_4803; -.
DR KEGG; lez:GLE_4803; -.
DR PATRIC; fig|69.6.peg.4735; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000308311; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01309; Met_dep_hydrolase_C; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ALN60144.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061569};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033726737"
FT DOMAIN 389..453
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 242..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 51137 MW; 1B8070BEF598098F CRC64;
MFRPFLAGCG LVLLAGAVQA APAPASRYTQ DPYPSTYKPV ASGPVLLQGA TVLTGTGQRL
DGADVLLRDG KIVAVGSRLD APGDATRVDA SGKWITPGII DVHSHLGVYP SPGVGAHSDG
NEMTSPVTPN VWAEHSIWPQ DPGFASALAG GITSLQILPG SANLIGGRGV TLKNVPAGSY
QAMKFPGAPW GLKMACGENP KRVYGSRNVS PGTRMGNVAG YRAAFIDASE YLRKTTPKAA
KPAKKRWWQS SGAPAASDSE KDTGGKRDLK LDTLAGAIKG DILVHIHCYR ADEMTTMLDL
AKEFGFKVSA FHHGVEAYKI ADRLAAENVC GALWADWWGF KMEAFDGIQE NIAIVDRPAN
SCAIVHSDSE EGIQRLNQEA AKVIAHARLA GIEIAPERAI RWLTQNPAKA LGIGERTGTL
EAGKMGDVVV WNGNPFSVYA KTEQVYIDGA RVYDRNDPSR QPKSDFMLGQ PAAQGAAAGD
VR
//
