ID A0A1Q5K5E3_9ACTN Unreviewed; 537 AA.
AC A0A1Q5K5E3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:OKJ76749.1};
GN ORFNames=AMK32_31965 {ECO:0000313|EMBL:OKJ76749.1};
OS Streptomyces sp. CB01883.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ76749.1, ECO:0000313|Proteomes:UP000186398};
RN [1] {ECO:0000313|EMBL:OKJ76749.1, ECO:0000313|Proteomes:UP000186398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01883 {ECO:0000313|EMBL:OKJ76749.1,
RC ECO:0000313|Proteomes:UP000186398};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ76749.1}.
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DR EMBL; LIWA01000008; OKJ76749.1; -; Genomic_DNA.
DR RefSeq; WP_073899292.1; NZ_LIWA01000008.1.
DR AlphaFoldDB; A0A1Q5K5E3; -.
DR OrthoDB; 3238066at2; -.
DR Proteomes; UP000186398; 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:SF23; AMIDOHYDROLASE YTCJ-RELATED; 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:OKJ76749.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186398}.
FT DOMAIN 54..532
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 537 AA; 55657 MW; FF3188F3956731DF CRC64;
MSEQSAEPKT VLLRRGEVHS PADPFATAMV VERGQVSWVG SEGAADAFAD GVDEVVDLDG
ALVTPAFTDA HVHTTATGLA LTGLDLSTAP SLDAALALVR EFAAARPGDR VLLGHGWDAA
RWPGGRPPTR AELDEATGGR PLYLSRIDVH SAVVTTALLD LVSADVPRED APLTADAHHT
VREAALAAIT PAQRAEAQRT ALAHAASLGI GSVHECGGPQ ISSADDFTAL LRLAGEIPGP
RVVGYWAEQG DEGVTRAREL GATGAAGDLF ADGALGSHTA CLHEPYADAG HSGTAYLDAD
AVAAHVVACT EAGLQAGFHA IGDAAVTAVV EGLRAAADKV GLARVRAARH RVEHAEMLTP
GTVAAFAELG LIASVQPAFD ALWGGEDGMY AQRLGAERAR TLNPYAALLR AGVPLAFGSD
SPVTPLDPWG TVRAAAFHHT PEHRISVRAA FTAHTRGGWR AVGRDDAGAL VPGAPADYAV
WRTDELVVQA PDDRVARWST DPRSGTPGLP DLTPGRELPV CLRTVVGGRT VFVRPGE
//
