(data stored in ACNUC7421 zone)

SWISSPROT: D6XY37_BACIE

ID   D6XY37_BACIE            Unreviewed;       470 AA.
AC   D6XY37;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   SubName: Full=Allantoinase {ECO:0000313|EMBL:ADH98110.1};
GN   OrderedLocusNames=Bsel_0574 {ECO:0000313|EMBL:ADH98110.1};
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:ADH98110.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98110.1, 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; ADH98110.1; -; Genomic_DNA.
DR   RefSeq; WP_013171539.1; NC_014219.1.
DR   STRING; 439292.Bsel_0574; -.
DR   EnsemblBacteria; ADH98110; ADH98110; Bsel_0574.
DR   KEGG; bse:Bsel_0574; -.
DR   eggNOG; ENOG4105CD3; Bacteria.
DR   eggNOG; COG0044; LUCA.
DR   HOGENOM; HOG000219146; -.
DR   KO; K01466; -.
DR   OMA; HFNEPGR; -.
DR   OrthoDB; 906155at2; -.
DR   BioCyc; BSEL439292:G1GLR-617-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0004038; F:allantoinase activity; IEA:InterPro.
DR   GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000256; P:allantoin catabolic process; IEA:InterPro.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR017593; Allantoinase.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR03178; allantoinase; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PE   4: Predicted;
DR   PRODOM; D6XY37.
DR   SWISS-2DPAGE; D6XY37.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00329261};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00329250};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN       59    435       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
SQ   SEQUENCE   470 AA;  51612 MW;  DEE2BA47D32039FF CRC64;
     MEVFVIGTQW IRNGTVWTGT SFVRQDIEIR DGIIDRLFDS HTSVQPEPGA RITDAADRLV
     VPGFIDPHVH FNDPGRRIWE GIDTGSKAAV AGGITTFIDM PLNSHPSVTN GHLARDKKKA
     IEGRSHAHYG LWGGITRTNC RDQGALDAQL DAGVIGFKGF MSESGIEDFP YLDRDALREA
     MGYCGEHRVT LALHAEAEAV LERYRHLSGP DPASFLASRP PEAEWQALDW IIEDALRFQT
     AVHVVHVSTA DGVRMLHEAK MSGADITIET CPHYLLFTDT DFIKKGPLLK CAPPLRPLSE
     QEALWQTVAD GLVDIIGSDH SPCPLEMKEA GNDDIRNAWG GIPGVQSGHA ALLSEAVKRG
     VPLETVLPMM TDAPARRFFP ERQIGRIAPG FAADLTLLSK SSHTITEKEL LNRHPYSPYT
     GLTVDMTVSG VFLGGVHIYQ SGKGIKSPLL GHHFVKGGHD HDNRSLRRIY
//

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