(data stored in ACNUC7421 zone)

SWISSPROT: D6XY47_BACIE

ID   D6XY47_BACIE            Unreviewed;       419 AA.
AC   D6XY47;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   SubName: Full=Amidase, hydantoinase/carbamoylase family {ECO:0000313|EMBL:ADH98120.1};
DE            EC=3.5.1.87 {ECO:0000313|EMBL:ADH98120.1};
GN   OrderedLocusNames=Bsel_0584 {ECO:0000313|EMBL:ADH98120.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98120.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98120.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001791; ADH98120.1; -; Genomic_DNA.
DR   RefSeq; WP_013171549.1; NC_014219.1.
DR   STRING; 439292.Bsel_0584; -.
DR   EnsemblBacteria; ADH98120; ADH98120; Bsel_0584.
DR   KEGG; bse:Bsel_0584; -.
DR   eggNOG; ENOG4105CE7; Bacteria.
DR   eggNOG; COG0624; LUCA.
DR   HOGENOM; HOG000241291; -.
DR   KO; K02083; -.
DR   OMA; IWPHGRW; -.
DR   OrthoDB; 829830at2; -.
DR   BioCyc; BSEL439292:G1GLR-627-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050538; F:N-carbamoyl-L-amino-acid hydrolase activity; IEA:UniProtKB-EC.
DR   CDD; cd03884; M20_bAS; 1.
DR   InterPro; IPR010158; Amidase_Cbmase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   PANTHER; PTHR32494; PTHR32494; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   TIGRFAMs; TIGR01879; hydantase; 1.
PE   4: Predicted;
DR   PRODOM; D6XY47.
DR   SWISS-2DPAGE; D6XY47.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Hydrolase {ECO:0000313|EMBL:ADH98120.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   METAL        86     86       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   METAL        97     97       Zinc 1. {ECO:0000256|PIRSR:PIRSR001235-
FT                                1}.
FT   METAL        97     97       Zinc 2. {ECO:0000256|PIRSR:PIRSR001235-
FT                                1}.
FT   METAL       132    132       Zinc 2. {ECO:0000256|PIRSR:PIRSR001235-
FT                                1}.
FT   METAL       196    196       Zinc 1; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001235-1}.
FT   METAL       386    386       Zinc 2; via tele nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR001235-1}.
SQ   SEQUENCE   419 AA;  44941 MW;  F238B75F4FE0BAD3 CRC64;
     MQTMTGIDQL RLWRTLMDLR QIGAGATEAD GITRLAFSPP ELEAKAYIRV LMEECGLDVY
     TDAVGNVFGV YQGREPDLPV IMTGSHVDSV IRGGAFDGTL GVLGAIEAVR TMKEAGIRPR
     RTIEIVSFSD EEGTRFGAGY MGSKALAGKL DDRFLTLTDQ EGESYETVLT KAGYEPSAYP
     KAKRDSREIG AFLEMHIEQG RVLEEADIAA GIVTTIQGPL WLQVTIEGAA DHAGATPMAI
     RKDASLAMAE AMLAVEEAAV THGGVGTVGS LKVKPGGINI IPGEVVFTVD MRHGDTTLRD
     RMLTDIEASF SAIAGKRGVS FKTLVTKKEP PATCSEDIRA SIHQAANTCG IPVKDMPCGA
     GHDALIMSTV TRMGMILVRS QDGISHNPQE WTSQEDCAKG TELLMRTLHS LAEERGDEA
//

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