ID A0A061LVT1_9MICO Unreviewed; 537 AA.
AC A0A061LVT1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:EYT54736.1};
GN ORFNames=H490_0107530 {ECO:0000313|EMBL:EYT54736.1};
OS Leucobacter sp. UCD-THU.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT54736.1, ECO:0000313|Proteomes:UP000026917};
RN [1] {ECO:0000313|EMBL:EYT54736.1, ECO:0000313|Proteomes:UP000026917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT54736.1,
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:EYT54736.1}.
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DR EMBL; APJM01000011; EYT54736.1; -; Genomic_DNA.
DR RefSeq; WP_017884158.1; NZ_KB714602.1.
DR AlphaFoldDB; A0A061LVT1; -.
DR HOGENOM; CLU_009942_2_0_11; -.
DR OrthoDB; 3173428at2; -.
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:EYT54736.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000026917}.
FT DOMAIN 54..536
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 537 AA; 57461 MW; 03883EB6B86F0FB0 CRC64;
MLRITGRFVR TDLDCIGETA GPASAPEAML VEHGRIVAVG SQDEVPAPAA ARRIDLGEGW
AIPGLIEPHG HPSEAAQLLG GDVIDIRPVT LESADAVWGA VKRALAAEPR PERVLANGWD
PLLQRGLVPP SIVDLDAIAG DIPLVIVHNS LHSAYFNTAA AREAGVDRGT PDPAGASYGR
DASGELTGVA YEAAAVMRIA GPVMAAVRQQ LPQRMAEHLA EVRRRGITTV ADLTWTGELG
PLFDGLRDAG RLPVRVRGYE MSRPGARATR PLDNGDARVR QTGVKVWSDG SPWVGNIATS
FPYLDTEATR GIGLEPGHIG RANYTTEQLI DIGSQYAGDG WQLACHSHGD VAVDSTLDAY
EHLIRDFALR DHRFRIEHCG LMTPAQFRRA ADLGVTVSLF VDHITYWGDV LVDDLFGERG
ASWADAGAAF AAGHRATFHN DGTVTPYEPL RNMAVAETRT SRTGRRLDGG TAVTRLDALR
AHTANAAWQL RSEHEVGALT PGLRADFAVL DVDPRTAQPE ALAEARVLAS AVDGEIE
//
