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
//