ID A0A0Q8FAM3_9GAMM Unreviewed; 445 AA.
AC A0A0Q8FAM3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=N-ethylammeline chlorohydrolase {ECO:0000313|EMBL:KRA52558.1};
GN ORFNames=ASD77_13010 {ECO:0000313|EMBL:KRA52558.1};
OS Pseudoxanthomonas sp. Root65.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1736576 {ECO:0000313|EMBL:KRA52558.1, ECO:0000313|Proteomes:UP000051430};
RN [1] {ECO:0000313|EMBL:KRA52558.1, ECO:0000313|Proteomes:UP000051430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root65 {ECO:0000313|EMBL:KRA52558.1,
RC ECO:0000313|Proteomes:UP000051430};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA52558.1, ECO:0000313|Proteomes:UP000051430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root65 {ECO:0000313|EMBL:KRA52558.1,
RC ECO:0000313|Proteomes:UP000051430};
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 -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000256|ARBA:ARBA00006745}.
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:KRA52558.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMHA01000002; KRA52558.1; -; Genomic_DNA.
DR RefSeq; WP_055942367.1; NZ_LMHA01000002.1.
DR AlphaFoldDB; A0A0Q8FAM3; -.
DR STRING; 1736576.ASD77_13010; -.
DR OrthoDB; 9807210at2; -.
DR Proteomes; UP000051430; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01298; ATZ_TRZ_like; 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; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43794:SF11; AMIDOHYDRO-REL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43794; AMINOHYDROLASE SSNA-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KRA52558.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051430}.
FT DOMAIN 66..414
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 445 AA; 48377 MW; BF0C5230670F2F45 CRC64;
MTDTAPDPCD LLIEAGYVVP VIPHGVVLEQ HAVAVTGGRI VAILPVAEAR TRFAPRETVS
RPEAALIPGM VNAHTHNPMT LLRGVADDLP LKVWLQEHIW PIEAAVIGPD FVADGITLAI
AEMLRGGTTC VNENYFFPDV QAATYKRHGF RARVGLPVID FPTAWASSDD EYFEKAGEVH
DQWRDDALIA TAFAPHAPYT VNDANFERVR MLSDQLDVPV HLHLHETAQE VEQSLEKHGQ
RPIARLDRLG LFNDRLIAIH MTQLTEAEIH LCAERGVSVV HCPESNLKLA SGFCPACALE
RAGVTLAVGT DGCASNNDLD MFSETRTAAL LAKAVAQDAA ALDAFSALRA ATLGGAKAIG
FDDRVGSIEP GKDADLVCVD LSALETQPLH YVVSQLIYAT GRQQVSDVWI AGKAKLRQRV
LVDIDIDGVI ANARQWRERI ARLGR
//
