ID A0A150WPL2_BDEBC Unreviewed; 592 AA.
AC A0A150WPL2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN ORFNames=AZI86_05065 {ECO:0000313|EMBL:KYG66422.1};
OS Bdellovibrio bacteriovorus.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=959 {ECO:0000313|EMBL:KYG66422.1, ECO:0000313|Proteomes:UP000075320};
RN [1] {ECO:0000313|EMBL:KYG66422.1, ECO:0000313|Proteomes:UP000075320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R0 {ECO:0000313|EMBL:KYG66422.1,
RC ECO:0000313|Proteomes:UP000075320};
RA Ploux O.;
RL Submitted (MAR-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:KYG66422.1}.
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DR EMBL; LUKE01000001; KYG66422.1; -; Genomic_DNA.
DR RefSeq; WP_061833986.1; NZ_LUKE01000001.1.
DR AlphaFoldDB; A0A150WPL2; -.
DR Proteomes; UP000075320; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 3.10.310.70; -; 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; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR PANTHER; PTHR22642:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000075320};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..592
FT /note="Amidohydrolase 3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007573391"
FT DOMAIN 71..559
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 592 AA; 66116 MW; 009791449A493047 CRC64;
MKTIIALSAL LMTACTPLMK SNSEKADLIV KNAKVFTHTS GMKNSFAVKD GKFVAVGDEN
ETTKWQGEKT RIIDAQGKTI IPGLIDTHAH PIRAGLNYTL ELRWDGVKSL KQGLQMIREQ
AQRTPADQWV RVVGGWSPYQ FAEKRFPTLK ELNDASPDRP LFVMYLYSRG FLNQAAVKKL
GYNKDTKFPG GEVQLDKNGK PTGMLLAKPN AFILYKTLVT APKLASLEEE KNSTRLYFQE
LSRFGLTTVI DAGGGGFYFP EDHRVAKDLN DQDQLAVNLP FFLFAPTPGK ELEDFKRWTK
MISPHTQHEL SHIVPYHLVG GGENLTTAAA DFENFLEPRP DLPANMEAEL KPILALLFKS
NWIFRIHATY DESIERVLSV VEELKKEGGP FPERFIIDHA ETIGEKNLQR IKKLGGGISI
QDRMAFQGED FVGRYGAKKA QNAPPIGRIL ELGIPLGSGT DATRVSSYNP WIALYWMTSG
KTVGGLKHLS SENILSREKA LYALTQGAAW FSKEEQVKGD IQPGKVADFA ILNVDYFTVP
EEKIKNIYSV LTVRAGKVRH GDAEFKSLAP QEQFIKALPS WSPVNYFGGY QL
//
