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Database: UniProt
Entry: A0A0Q5ZJ68_9BRAD
LinkDB: A0A0Q5ZJ68_9BRAD
Original site: A0A0Q5ZJ68_9BRAD 
ID   A0A0Q5ZJ68_9BRAD        Unreviewed;       572 AA.
AC   A0A0Q5ZJ68;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQT12783.1};
GN   ORFNames=ASG57_07410 {ECO:0000313|EMBL:KQT12783.1};
OS   Bradyrhizobium sp. Leaf396.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT12783.1, ECO:0000313|Proteomes:UP000051536};
RN   [1] {ECO:0000313|EMBL:KQT12783.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT12783.1,
RC   ECO:0000313|Proteomes:UP000051536};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT12783.1, ECO:0000313|Proteomes:UP000051536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf396 {ECO:0000313|EMBL:KQT12783.1,
RC   ECO:0000313|Proteomes:UP000051536};
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:KQT12783.1}.
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DR   EMBL; LMQJ01000034; KQT12783.1; -; Genomic_DNA.
DR   RefSeq; WP_057198044.1; NZ_LMQJ01000034.1.
DR   AlphaFoldDB; A0A0Q5ZJ68; -.
DR   OrthoDB; 9815027at2; -.
DR   Proteomes; UP000051536; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01297; D-aminoacylase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR013108; Amidohydro_3.
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:KQT12783.1}.
FT   DOMAIN          46..550
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          553..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  62461 MW;  143B8A37539BFD48 CRC64;
     MSTTPDLVIR GGNVADGSGG ELFEADVAIT GGKISEVGKV SARGREEIDA RGKLVTPGFV
     DVHTHYDGQV TWSQDITPSS QNGVTTAIMG NCGVGFAPCK PDDHTRLIQL MEGVEDIPEP
     VLSAGIPWAW ESFPDYMDWL AKRDFDIDVG AQLPHAALRV YVMGERGARR DPSTAEDNAT
     MAKLAGEAVR SGALGFSTSR TLNHRTSTGD FTPTLKAGED ELTAIAGAMH REGRSVLQFV
     LDLSTIHEDL PMMLRVADST NCPISFSITQ NDKAPQRWRQ TLDEINAASR RGLSVTAQIA
     ARPVGLLLGL ELSRNPFQTH PSYRAIAHLP LQERLALLRQ SDVRKAILSE TATATDDPLF
     FRPNYDKMFL LGDPPDYEQP PENALGPQAR RQGRQPEELA YDAMLSDEGR GMLYVPFLNY
     SDGNLDATRE MLLDPRSVPG LSDGGAHCGI ICDASFPTYL LTHWTRDRKR GEKLTIPFVV
     AAQSRKTALS VGLRDRGLIA PGYKADVNVI DYDRLHLHPP KVHYDLPVGG RRLLQDVDGY
     EATIVSGVVT RRHGEATGRR PGKLIRGAQG VN
//
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