ID A0A1B7URB8_9GAMM Unreviewed; 483 AA.
AC A0A1B7URB8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=D-aminoacylase {ECO:0000313|EMBL:OBP17041.1};
GN ORFNames=A5320_05840 {ECO:0000313|EMBL:OBP17041.1};
OS Rheinheimera sp. SA_1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1827365 {ECO:0000313|EMBL:OBP17041.1, ECO:0000313|Proteomes:UP000092258};
RN [1] {ECO:0000313|EMBL:OBP17041.1, ECO:0000313|Proteomes:UP000092258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA_1 {ECO:0000313|EMBL:OBP17041.1,
RC ECO:0000313|Proteomes:UP000092258};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OBP17041.1}.
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DR EMBL; LXWK01000011; OBP17041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7URB8; -.
DR STRING; 1827365.A5320_05840; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000092258; 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; 2.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000092258}.
FT DOMAIN 49..213
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 333..459
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 483 AA; 51513 MW; 1D76D143CDCE613C CRC64;
MNPVLYDRIF FGASVIDGTG AAAIVADVAL LADRIAAIGT LTPGTGRVEI AAQGLVLAPG
FIDVHTHDDL ELIRNPAMLA KLSQGVTTVI TGNCGISAAP ADLNAPPPDP MNLLGQQAEF
AYRSFAEYAK ALQQAKPGVN TAALVGHTTL RHAVMTDLSK AATPKQQLKM QQQLRQSLEQ
GALGLSSGLA YHNAIAAPSA ELAVVGAPLA EFDAIYTSHL RSEFAAIIPA LAEAADLGLH
LKVPVVISHL KCAGMANWGR AGEVLEFIGK RAAKQHFCCD CYPYSASSST LDLKQVTADF
EIFITWSEPY PAMAGQTLAQ IAASWQLPLL ETAARLMPAG AVYHGMSETD VQQFLSYPPT
MIGSDGLPCD PHPHPRLWGA FPRVLGHYSR DLQLFSLSQA IHKMTGLSAQ NFKLAQRGSI
KVGNFADLVL FDAEKIKDNA DFVQPFAQAE GIVQVYVNGG LAFDGGMACP DRHGRFLAHQ
PQR
//