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Database: UniProt
Entry: A0A0J9GVT1_9RHOB
LinkDB: A0A0J9GVT1_9RHOB
Original site: A0A0J9GVT1_9RHOB 
ID   A0A0J9GVT1_9RHOB        Unreviewed;       465 AA.
AC   A0A0J9GVT1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   08-MAY-2019, entry version 19.
DE   SubName: Full=D-hydantoinase {ECO:0000313|EMBL:KMW57673.1};
DE            EC=3.5.2.2 {ECO:0000313|EMBL:KMW57673.1};
GN   ORFNames=AIOL_002638 {ECO:0000313|EMBL:KMW57673.1};
OS   Candidatus Rhodobacter lobularis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW57673.1, ECO:0000313|Proteomes:UP000037178};
RN   [1] {ECO:0000313|EMBL:KMW57673.1, ECO:0000313|Proteomes:UP000037178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGS {ECO:0000313|EMBL:KMW57673.1};
RA   Jourda C., Santini S., Claverie J.-M.;
RT   "Draft genome sequence of an Alphaproteobacteria species associated to
RT   the Mediterranean sponge Oscarella lobularis.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two
CC       divalent metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KMW57673.1}.
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DR   EMBL; LFTY01000002; KMW57673.1; -; Genomic_DNA.
DR   RefSeq; WP_049643374.1; NZ_LFTY01000002.1.
DR   EnsemblBacteria; KMW57673; KMW57673; AIOL_002638.
DR   PATRIC; fig|1675527.3.peg.2765; -.
DR   OrthoDB; 906155at2; -.
DR   Proteomes; UP000037178; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004157; F:dihydropyrimidinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01314; D-HYD; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000037178};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00321417,
KW   ECO:0000313|EMBL:KMW57673.1};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00321440};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037178}.
FT   DOMAIN        3     36       Urease_alpha. {ECO:0000259|Pfam:PF00449}.
FT   DOMAIN       49    441       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   MOD_RES     151    151       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR611778-50}.
SQ   SEQUENCE   465 AA;  50155 MW;  933BD94D8943DB88 CRC64;
     MTHDTVITGA RVVTASGTTH CDIGITDGRI AALGKDLQGE HVIDGHGLIA LPGGIDSHVH
     ISQPSGPGIE MADDFTSGTR SAACGGNTTV LPFCLPEEGR TLREAVADYR AKADGNCMTD
     VSFHLIVKDT DPVTLGQDLP ALIQAGYTSF KVFMTYAGLA LSDRQILEVM AVAKEQGAMV
     MVHAENEDAI EFLRDRADRN GETAPYHHAT TRPVPVEREA THRAISLAEI AGVPLTIVHV
     SNGEATEEIV RARQRGLTVF AETCPQYITL TASDLDRDGF DGAKYVCSPP PRTAEEWPKI
     WAGIEQGTFD LFSSDHCPFR FNDPAGKDAP GARQSFRNIP NGIPGVETRL PILFSEGVVK
     GRLSLERFAA ITATNHARLY GLFPRKGAIM VGADADIALW DPTLSKPIRQ ADLHHGSDYT
     PWEGFEVTGW PVRTILRGQT VMQNGDPVGA PSGSYLEREA PDLLL
//
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