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Database: UniProt
Entry: C0ZTP9_RHOE4
LinkDB: C0ZTP9_RHOE4
Original site: C0ZTP9_RHOE4 
ID   C0ZTP9_RHOE4            Unreviewed;       571 AA.
AC   C0ZTP9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   OrderedLocusNames=RER_56070 {ECO:0000313|EMBL:BAH36315.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH36315.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH36315.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT   strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
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DR   EMBL; AP008957; BAH36315.1; -; Genomic_DNA.
DR   RefSeq; WP_020909525.1; NC_012490.1.
DR   AlphaFoldDB; C0ZTP9; -.
DR   KEGG; rer:RER_56070; -.
DR   PATRIC; fig|234621.6.peg.6181; -.
DR   eggNOG; COG1574; Bacteria.
DR   HOGENOM; CLU_009942_2_0_11; -.
DR   Proteomes; UP000002204; 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:SF24; AMIDOHYDROLASE FAMILY 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;
FT   DOMAIN          67..553
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   571 AA;  61437 MW;  864BFCE351FCF924 CRC64;
     MRKLHTHEAS PLDATATIFT GAKIHTVDDS TAGAEAFLVF GNRFAAVGTL EECRTEARRL
     STRTTAVVEL DGATVVPGFV DPHAHPLMYG QMLSWVDCGP EKAHSIPGII ALLQEAALTA
     PAGVPIRGYG YEHRNLIEGR HPLKEELDQV ATDREVYLMN ASGHGGVVNS FTFDKHGIDA
     STENPAGGEF FRDADGELTG ELSDAACNIL TGVNGVKVGH HGPNFHLEDE PEEHLRQLSV
     AQDKFLAGGV TTIGDCQVTR REFDMYLRLA EQDQLKTRVS MYMLSHLLDH VIDTGMHGAF
     GNSRLAFGGI KFYADGTLGG WTAYFPDGYV GDPCRTGQLY HEPADYSELI AKAHSVGLQT
     ATHAQSPTAI DMVLDAIEAA QKAHPDADAR HRIEHCGLPT AEQIARMNLA GVYPVNQPQH
     YYNWGEGVTA AIGTPGERFN PLGEFIAAEV PVTISSDAPV AEPKPLEAIQ AAVTRVTRQG
     HQLGSDALRI SADQALQAHT LNGARALGRE AELGSISVGK RADFVILGAD LLEVPADAIA
     QIEVRETWID GELAHSGYNH LLSSTSTTEE K
//
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