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
//