ID A0A0M5L1Q3_9MICC Unreviewed; 543 AA.
AC A0A0M5L1Q3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ALE04873.1};
GN ORFNames=AL755_04105 {ECO:0000313|EMBL:ALE04873.1};
OS Arthrobacter sp. ERGS1:01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE04873.1, ECO:0000313|Proteomes:UP000060433};
RN [1] {ECO:0000313|EMBL:ALE04873.1, ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE04873.1,
RC ECO:0000313|Proteomes:UP000060433};
RX PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT bacterium with prospective cold active industrial enzymes, isolated from
RT East Rathong glacier in India.";
RL J. Biotechnol. 214:139-140(2015).
RN [2] {ECO:0000313|Proteomes:UP000060433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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; CP012479; ALE04873.1; -; Genomic_DNA.
DR RefSeq; WP_054009906.1; NZ_CP012479.1.
DR AlphaFoldDB; A0A0M5L1Q3; -.
DR STRING; 1704044.AL755_04105; -.
DR KEGG; are:AL755_04105; -.
DR PATRIC; fig|1704044.3.peg.14; -.
DR OrthoDB; 3238066at2; -.
DR Proteomes; UP000060433; Chromosome.
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:ALE04873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000060433}.
FT DOMAIN 54..539
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 543 AA; 57950 MW; FEAF3DBE6687D2D7 CRC64;
MSNMFADTII VNASVHTLDP ARPGCDTIVM AGGRVVATGD AALLKEHRGS DTSIVDAQGH
TVTPGLIDAH IHPIEGVEAT IGVDFGGVKT LEGFLAALRA EADRVLAHEP SGWVRGWNVD
YGVFEGRPIT AELIEGAVRG LPTFLQLFDL HTVLASRAAL KAADITGPRR FPDSSEIVVT
DEGLPTGELR EASAYALVAA AAPALTRAQA IGRAREIMMN LAKSGITAGS IMDGDIASLD
FLDEIDSTDA GLPVRLVAAL GHKPGMDAQA VRDYLAAKHR SGRRWRGGLI KMFLDGVIDT
GTGWMYEADT SGEGLYSFWP DPSEFPTTVK HYSDEGFQIA THAIGDRAIG VAIDAYIAAG
VASTRSAPHR IEHLECLADQ DLPRLAGAGI TASMQPLHMQ WRNADGSDSW SSRLGPDRAS
LAWRVKDILT SGAPLALGSD WPVAQYDVRI GMAWARLRRT PGQPDAHVFE PAQRLSPTET
LKGFTLWAAR AQGDNDAGSI RPGYRADLTM WADDPLKVSG DQLIDVPITS TWVDGAVVFA
GEE
//