ID   A0A0Q8BJ19_9BURK        Unreviewed;       635 AA.
AC   A0A0Q8BJ19;
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=Amidohydrolase {ECO:0000313|EMBL:KRA01875.1};
GN   ORFNames=ASD71_07395 {ECO:0000313|EMBL:KRA01875.1};
OS   Achromobacter sp. Root565.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1736564 {ECO:0000313|EMBL:KRA01875.1, ECO:0000313|Proteomes:UP000052040};
RN   [1] {ECO:0000313|EMBL:KRA01875.1, ECO:0000313|Proteomes:UP000052040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root565 {ECO:0000313|EMBL:KRA01875.1,
RC   ECO:0000313|Proteomes:UP000052040};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA01875.1, ECO:0000313|Proteomes:UP000052040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root565 {ECO:0000313|EMBL:KRA01875.1,
RC   ECO:0000313|Proteomes:UP000052040};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRA01875.1}.
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DR   EMBL; LMGO01000001; KRA01875.1; -; Genomic_DNA.
DR   RefSeq; WP_056561577.1; NZ_LMGO01000001.1.
DR   AlphaFoldDB; A0A0Q8BJ19; -.
DR   Proteomes; UP000052040; 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.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KRA01875.1}.
FT   DOMAIN          60..543
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   635 AA;  69226 MW;  2ACB5368115D8E58 CRC64;
     MADTLGPARQ GAPDLILHQG RFTTLDPANP IADAVAIKDG RFTRVGAASD ILPLAGPATR
     VIALGGRGVL PGLIDNHLHI IRGGLNYNME LRWDGVTSLA DAMAMLRRQV AITPAPQWVR
     VVGGFTEHQF AEKRLPTIEE LNAVAPDTPV FILHLYDRAL LNAAALRAVG YDKNTPAPPG
     GEIVRDSAGN PTGLLLAKPN ASILYATLAK GPKLPFEYQV NSTRHFMRDL NRLGVTGAID
     AGGGNQNYPE DYQVIQQLAD ADQLTIRLAY NLFTQKPKQE KEDFLNWTAT SQYKQGTDYF
     RHNGAGEMLV FSAADFEDFR QPRPEMGPEM EGDLEEVVRI LAQNRWPWRM HATYDETISR
     SLDVFERVNK DVPLAGLNWF FDHAETISER SIDRIAALGG GVAVQHRMAY QGEYFVERYG
     PGAAEATPPV KRMLEKGVNV SAGTDATRVA SYNPWVSLSW LITGKTVGGL RLTPQRNCLD
     RDAALRMWTE NVTWFSNEQG KKGRIAAGQL ADLIVPDRDF FSCPESEIAD TSSLLTVVGG
     KVVWGAGDFA AHDESAPPPA MPDWSPTRLF GGYGAWGDSE GKPLQATLRE AAAACACAND
     CNVHGHQHAG AWTSKLPVSD LKGFWGALGC ACWAV
//