ID A0A0A2WYH9_9GAMM Unreviewed; 462 AA.
AC A0A0A2WYH9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KGQ18064.1};
GN ORFNames=LF41_1418 {ECO:0000313|EMBL:KGQ18064.1};
OS Lysobacter dokdonensis DS-58.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1300345 {ECO:0000313|EMBL:KGQ18064.1, ECO:0000313|Proteomes:UP000030518};
RN [1] {ECO:0000313|EMBL:KGQ18064.1, ECO:0000313|Proteomes:UP000030518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-58 {ECO:0000313|EMBL:KGQ18064.1,
RC ECO:0000313|Proteomes:UP000030518};
RA Kim J.F., Kwak M.-J.;
RT "Genome sequences of Lysobacter dokdonensis DS-58.";
RL Submitted (SEP-2014) 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:KGQ18064.1}.
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DR EMBL; JRKJ01000021; KGQ18064.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2WYH9; -.
DR STRING; 1300345.LF41_1418; -.
DR PATRIC; fig|1300345.3.peg.2490; -.
DR eggNOG; COG1228; Bacteria.
DR Proteomes; UP000030518; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01309; Met_dep_hydrolase_C; 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 PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KGQ18064.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030518};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..462
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001996937"
FT DOMAIN 372..437
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 441..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 49067 MW; D397C7D2C8AE1EB0 CRC64;
MSLKPIVAVI ATVLIAGCAS SGATKTTAAP AKPSWTDDPY PTTYQRVQSP PVLITGATVL
TGTGTRLDNA DVLLQDGKIV AVGTGLQAPA GATRVDAQGK WVTPGIIDIH SHLGVYPSPG
MSAHSDGNEM TGPVTPNVWA EHSIWPQDPG FLTALAGGIT SLQVLPGSAN LIGGRGATLK
NVPATTYQAM KFPGAPWGLK MACGENPKRV YGQKGGPATR MANVAGYRAA FIEAADYMKK
QKESKEGPGK RDLKNDTLAG AINGDIRVHI HCYRADEMAT MLDLAKEFGF RISAFHHGVE
AYKIADKLAA AGTCGALWAD WWGFKMEAFD GIQENIALVD RAPGGCAIVH SDSEEGIQRL
NQEAAKVIAN AKRIGIDITP EHAILWLTQN PARAMGIDAM TGTLEPGKMG DVVVWNGNPF
TVYAHAEQVY IDGARLYDRA DPSRQPKSDF MLGQDDKRGG VR
//