ID A0A0Q3T7S2_BRECH Unreviewed; 534 AA.
AC A0A0Q3T7S2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aminoacylase {ECO:0000313|EMBL:KQL49968.1};
GN ORFNames=AN963_09900 {ECO:0000313|EMBL:KQL49968.1};
OS Brevibacillus choshinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL49968.1, ECO:0000313|Proteomes:UP000051063};
RN [1] {ECO:0000313|EMBL:KQL49968.1, ECO:0000313|Proteomes:UP000051063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL49968.1,
RC ECO:0000313|Proteomes:UP000051063};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KQL49968.1}.
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DR EMBL; LJJB01000007; KQL49968.1; -; Genomic_DNA.
DR RefSeq; WP_055744301.1; NZ_LJJB01000007.1.
DR AlphaFoldDB; A0A0Q3T7S2; -.
DR STRING; 54911.AN963_09900; -.
DR PATRIC; fig|54911.3.peg.6202; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000051063; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
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;
FT DOMAIN 45..508
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 534 AA; 58599 MW; C0448D39278AEF04 CRC64;
MFDVLIRNGM VCDGTGNPWT KLDIGIRNGK IAVMADLSQS TGQVEIDATD LVVSPGFIDP
HVHSDLLCIK PDVHKIKVLQ GVTTELFGQD GISVAPVSEE TKPLWQQQLK GLNGDVGEWS
WNSIDEYLQF LEGNQLAGNA TYLVPHGNVR TLVLGFEGRE ATSEEIERMA GLVELGMQQG
AFGVSTGIQY PPCVFANKAE LVAICKAAAK YDGCFVVHIR NESNLSLEAL AEVIDVARQS
GVRLNVSHFK VCGSINRDKL APALALLDAG RAEGIEITFD QYPYTAASTV FSAILPPWMH
DGGTAVMLER LKDAESREKV KHEMLNNSEY DNTVRNNGWK NIVIASVASE QNRDLEGKSV
AEIGEMRGID PSDAALDLLL EENAAVTMVI HWGVDADVMQ VMRHPLQMVG SDGVFGGKPH
PRLYGSFPRV LGRYSREKEA FPIWEAVRKM TSAPAQLLRL QKRGLLCEGY WADIAIFDPK
MVLDRATYEE PAQLPLGIHH VLVNGQIAVR DGHYTGVTAG QVIRRANKQH VLSR
//