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Database: UniProt
Entry: A0A0G0LPF5_9BACT
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Original site: A0A0G0LPF5_9BACT 
ID   A0A0G0LPF5_9BACT        Unreviewed;       521 AA.
AC   A0A0G0LPF5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:KKQ92957.1};
GN   ORFNames=UT16_C0001G0023 {ECO:0000313|EMBL:KKQ92957.1};
OS   Candidatus Azambacteria bacterium GW2011_GWA2_39_10.
OC   Bacteria; Candidatus Azambacteria.
OX   NCBI_TaxID=1618611 {ECO:0000313|EMBL:KKQ92957.1, ECO:0000313|Proteomes:UP000034706};
RN   [1] {ECO:0000313|EMBL:KKQ92957.1, ECO:0000313|Proteomes:UP000034706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKQ92957.1}.
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DR   EMBL; LBVT01000001; KKQ92957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0LPF5; -.
DR   Proteomes; UP000034706; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR023100; D-aminoacylase_insert_dom_sf.
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:KKQ92957.1}.
FT   DOMAIN          417..504
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   521 AA;  56995 MW;  0E30F0D8BA68F860 CRC64;
     MLDILIKNGI VVDGVGTPAY HADVAIKDGK IEKIGFLGEP GAKTVIDAAG QYVAPGFIDI
     NNASDRHWTL FNHPLSESLL YQGITTIIGG NCGSSLAPLT TGNIIAAIQK WADIKQVNVN
     WLTLSEFFNE VKKKKLLLNF GTLVGHATLR RGIVGDQFRE LTEQELAQMK QMLSGALMEG
     ALGFSTGLVY SHAKTATADE ITSLVSLLNP GKIYSSHLRD EEGKLYESVL ETIDTAKKNK
     VSIEISHLKS VGKENWSLFD KVLEAIEKAA EEGTDINFDI YPYTSTATVF YTILPDWIAV
     GGRMKLVENL KNQDLKKRAI EEMKGKENDF SEIVVAGGNI DKTFIGKTIG AISKNQGAGI
     LETIINLLIA AEGKLIVFWP SLSEENFIKA LKNSLSIIAS DGATYNLDDA HDGYLIHPRS
     FGCFPRILSR YVREKNIISL EEAIKKMTAL PALKIGLPYR GVIRQGFFAD IAIFNIDIVK
     DLASLENPFQ YSQGIHSVII NGQIALSGGK IQNHSLGQIL K
//
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