ID Q0S9X8_RHOJR Unreviewed; 526 AA.
AC Q0S9X8;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Possible metal-dependent amidohydrolase {ECO:0000313|EMBL:ABG95658.1};
GN OrderedLocusNames=RHA1_ro03858 {ECO:0000313|EMBL:ABG95658.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG95658.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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DR EMBL; CP000431; ABG95658.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0S9X8; -.
DR KEGG; rha:RHA1_ro03858; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_6_1_11; -.
DR Proteomes; UP000008710; 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:ABG95658.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 38..526
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 526 AA; 56639 MW; 208EA07A9D92159E CRC64;
MRTGHPDSPV TDALAVAGGR VVALGERARA MQSSRTKLID LRGGALLPSF GDGHVHPLMG
GLGLRGASIR DCGSVDEVLR EVRRWADENP GAGCVFGDGV SPTLAESGRF EARWLDSVVP
DRPVVLRTMD HHTAWVNSAA LRCAGLTRDT PDPAGGEIVR TADGELLGTL REWGAINPVL
ALVPEVTLDD RVDALATVSK MLAAAGITWV QDAWTELDDV EVWLTAADGG RLSTRANLAF
RATPETWEAD LEAFVLARRK VEERGGDAIR AGTVKFFADG VIEAGTAALL APYTDCPHSH
GISNWTTDEL SRAAAEVDRL GFQIHIHAIG DAGVRMALDA IEHVDRSNGP RDRRATIAHL
QLVDGDDLDR FTSLGAVANF QPLWAQLDAL MTELTIPRIG AERSAQQYRI GTLTERGARV
AFGSDWPITA YEPIKGIATA IHRQTPSGVP TEGWLPRERV GLERALAAYS AGVAYQGFEE
NLWGCLRPGM RADMIQLPVD PYDLSSTQAL SELAVTRTWL GGTQVH
//
