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Database: UniProt
Entry: A0A0Q5E7I0_9BURK
LinkDB: A0A0Q5E7I0_9BURK
Original site: A0A0Q5E7I0_9BURK 
ID   A0A0Q5E7I0_9BURK        Unreviewed;       592 AA.
AC   A0A0Q5E7I0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Hydrolase {ECO:0000313|EMBL:KQQ47783.1};
GN   ORFNames=ASF61_02490 {ECO:0000313|EMBL:KQQ47783.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ47783.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ47783.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47783.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ47783.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ47783.1};
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:KQQ47783.1}.
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DR   EMBL; LMNW01000001; KQQ47783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5E7I0; -.
DR   STRING; 1736266.ASF61_02490; -.
DR   Proteomes; UP000051032; 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; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 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:KQQ47783.1}.
FT   DOMAIN          68..586
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   592 AA;  63350 MW;  A94553A63896C601 CRC64;
     MAAAKPVATP LVSPISTLVA DTIYRNGYIY TVDANDSVQQ ALAVRGGRIV YVGDDAGAAR
     LQGRRTTVID LGGKMLMPGL VDGHLHPQSG GSRLLNCSLD YLPLTVAQFQ QRIQACLDSD
     VRLGKGDPQR WLVVVNWFQQ GMLPDGVTTS AATLDALKTD RPILVRSSFG HSLQLNSKGI
     AVAGITVATP DPAGGKIARD AGGQATGLLE DAAQDLAMNL LPPLTVAENL AASAKALEAM
     RRQGITSFLD AYTDPETMTA FTTLQRQGKL TARAHFAVLI DLDKGNTPQR AVAELLKQKK
     QFDQGPTRVA PSLQVRHAKL FMDGVISAPA FTGAMLAPYW VNKGTEQQPD WQPGSSNGPA
     TYFSQAALRS TLDVLARAGI DPHLHVDGDR AVREALDAVA WLRGTPAGKQ VRPALAHDEI
     VDPADYPRFA QLDVTPVLSF QWAKPAPDTL GALKPYMGPQ RYRLVQPQSA LLDAGARIAY
     GSDWPVDPLD QWFALKVGVT RTAAPDAGAE YAGRLGDTPG LPRAAVLRAI TLNAAYTLRQ
     ERLTGSLEAG KLADLIVLDR NFFTIPAEDI ANIKVLQTVV GGKVVYQSPA MR
//
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