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Database: UniProt
Entry: A0A069IGI8_9BURK
LinkDB: A0A069IGI8_9BURK
Original site: A0A069IGI8_9BURK 
ID   A0A069IGI8_9BURK        Unreviewed;       631 AA.
AC   A0A069IGI8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KDP87934.1};
GN   ORFNames=CF70_033600 {ECO:0000313|EMBL:KDP87934.1};
OS   Cupriavidus sp. SK-3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP87934.1, ECO:0000313|Proteomes:UP000023560};
RN   [1] {ECO:0000313|EMBL:KDP87934.1, ECO:0000313|Proteomes:UP000023560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-3 {ECO:0000313|EMBL:KDP87934.1,
RC   ECO:0000313|Proteomes:UP000023560};
RA   Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT   "Cupriavidus sp. strain SK-3.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KDP87934.1}.
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DR   EMBL; JFJV02000079; KDP87934.1; -; Genomic_DNA.
DR   RefSeq; WP_035863036.1; NZ_JFJV02000079.1.
DR   AlphaFoldDB; A0A069IGI8; -.
DR   OrthoDB; 9031471at2; -.
DR   Proteomes; UP000023560; 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:KDP87934.1}.
FT   DOMAIN          53..537
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   631 AA;  69900 MW;  AC14377B3621FC04 CRC64;
     MSDSRPDLIF HNARITTLDR SRPVATAVAI QAGRFVAVGS DEEVLAQSGA NTRVIDLKRR
     SVLPGLFDNH THVVRGGLNY NMELRWDGVR SLADALDMLK RQVAVTPAPQ WVRVVGGFTE
     HQFVEKRLPT LEEINAIAPD TPVFLLHLYD RALLNGAALR AVGYTRNTPA PPGGEIVRDT
     AGNPTGLLIA KPNATILYAT LAKGPKLPLE YQVNSTRHFM RELNRLGVTG VIDAGGGFQN
     YPEDYEVIRK LADAGQITVR LAYNLFTQKP KEEKEDFLKW TSSVKYKQGD DYFRHNGAGE
     MLVYSAADFE DFRQPRPDMP PEMEGDLEEV VRILVQNQWP WRLHATYDET ISRALDVFEK
     VHRDTPIDGL NWFFDHAETI SDKSIDRIAA LGGGIAVQHR MAYQGEYFVE RYGARAAEAT
     PPIKRMLDKG VKVSAGSDAT RVASYNPWVS LSWMVTGKTV GGMKLYPQRN LLDRETALRM
     WTENVAWFSN EEGRRGRIQV GQLADFMVPS KDYFGIPEDE IAFLTSHLTV VGGRVVYGEG
     EFAPLDDNPL PPAMPDWSPT RTFKGYAAWG EPEGAGKNSL QPVNSRNMAA CGCGTSCGLH
     GHSHANAWAS SAPASDLQGF FGALGCSCWM V
//
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