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Database: UniProt
Entry: A0A061LW94_9MICO
LinkDB: A0A061LW94_9MICO
Original site: A0A061LW94_9MICO 
ID   A0A061LW94_9MICO        Unreviewed;       575 AA.
AC   A0A061LW94;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:EYT51784.1};
GN   ORFNames=H490_0114605 {ECO:0000313|EMBL:EYT51784.1};
OS   Leucobacter sp. UCD-THU.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leucobacter.
OX   NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT51784.1, ECO:0000313|Proteomes:UP000026917};
RN   [1] {ECO:0000313|EMBL:EYT51784.1, ECO:0000313|Proteomes:UP000026917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-THU {ECO:0000313|EMBL:EYT51784.1,
RC   ECO:0000313|Proteomes:UP000026917};
RX   PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA   Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA   Coil D.A.;
RT   "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:S69-S82(2013).
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:EYT51784.1}.
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DR   EMBL; APJM01000028; EYT51784.1; -; Genomic_DNA.
DR   RefSeq; WP_017882598.1; NZ_APJM01000028.1.
DR   AlphaFoldDB; A0A061LW94; -.
DR   STRING; 1292023.H490_0114605; -.
DR   HOGENOM; CLU_009942_6_1_11; -.
DR   OrthoDB; 3238066at2; -.
DR   Proteomes; UP000026917; 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:SF25; EXOENZYMES REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 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:EYT51784.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026917}.
FT   DOMAIN          55..550
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          555..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  61697 MW;  9968F441785A0579 CRC64;
     MTHTPQADVV FENGWIYTGT EARPRRGALA IADGRILSTD PDEVARLAET AAERIDLAGR
     LLIPGFQDAH VHPVSAGIEL LSCNLTECDT ADDALATIAA YAEAHPELDW ILGAGWSMDS
     FPGGTPTRRM LDAVVPGRPV FLENRDHHGA WFNTRAAELA GIDANTPDPA DGRFERETDG
     TPAGTAHEGA MGLFDRVRPR ATQQKAYAGL LAAQEHLVSF GITAWQDAAV GEFMGSPDTV
     PVYRRAAADG TLKVRVRGAQ WWNREDGDAQ LEPILARRDE AAAECDPDRL SLGSVKVMVD
     GVAENFTAAM HDCYLDHHGR ATDNRGISFF DARQMADFVT ALDREGVQVH FHALGDRAVT
     DALDALDQAL STNGPTDNRH HLAHLQVVRS EDVARFTPLG ATANMQALWA CHEDQLDELT
     LPFLAGDAEA HHYPFGELAA TGAALAAGSD WPVSSPDPIA AIHVAVNRVA PGAQRPPLGP
     EHQKLTLAQA LDAYTQGTAR INHLDHATGR LVPGYYADLA IVDRNLFELP AEQIGGAVVD
     ETWIGGERVY SRAEGSDPIA AAQRAPQLDA TGAEA
//
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