(data stored in ACNUC7421 zone)

SWISSPROT: D6XY46_BACIE

ID   D6XY46_BACIE            Unreviewed;       112 AA.
AC   D6XY46;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=5-hydroxyisourate hydrolase {ECO:0000256|RuleBase:RU361270};
DE            Short=HIU hydrolase {ECO:0000256|RuleBase:RU361270};
DE            Short=HIUHase {ECO:0000256|RuleBase:RU361270};
DE            EC=3.5.2.17 {ECO:0000256|RuleBase:RU361270};
GN   OrderedLocusNames=Bsel_0583 {ECO:0000313|EMBL:ADH98119.1};
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:ADH98119.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98119.1, 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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-
CC         dihydro-1H-imidazole-5-carboxylate + H(+); Xref=Rhea:RHEA:23736,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18072,
CC         ChEBI:CHEBI:58639; EC=3.5.2.17;
CC         Evidence={ECO:0000256|RuleBase:RU361270};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361270}.
CC   -!- SIMILARITY: Belongs to the transthyretin family. 5-hydroxyisourate
CC       hydrolase subfamily. {ECO:0000256|RuleBase:RU361270}.
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DR   EMBL; CP001791; ADH98119.1; -; Genomic_DNA.
DR   RefSeq; WP_013171548.1; NC_014219.1.
DR   STRING; 439292.Bsel_0583; -.
DR   EnsemblBacteria; ADH98119; ADH98119; Bsel_0583.
DR   KEGG; bse:Bsel_0583; -.
DR   eggNOG; ENOG4105VT2; Bacteria.
DR   eggNOG; COG2351; LUCA.
DR   HOGENOM; HOG000251776; -.
DR   KO; K07127; -.
DR   OMA; DEHYHVP; -.
DR   OrthoDB; 1955791at2; -.
DR   BioCyc; BSEL439292:G1GLR-626-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0033971; F:hydroxyisourate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.180; -; 1.
DR   InterPro; IPR014306; Hydroxyisourate_hydrolase.
DR   InterPro; IPR000895; Transthyretin/HIU_hydrolase.
DR   InterPro; IPR023416; Transthyretin/HIU_hydrolase_d.
DR   InterPro; IPR036817; Transthyretin/HIU_hydrolase_sf.
DR   InterPro; IPR023419; Transthyretin_CS.
DR   PANTHER; PTHR10395; PTHR10395; 1.
DR   Pfam; PF00576; Transthyretin; 1.
DR   PRINTS; PR00189; TRNSTHYRETIN.
DR   SUPFAM; SSF49472; SSF49472; 1.
DR   TIGRFAMs; TIGR02962; hdxy_isourate; 1.
DR   PROSITE; PS00769; TRANSTHYRETIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XY46.
DR   SWISS-2DPAGE; D6XY46.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Hydrolase {ECO:0000256|RuleBase:RU361270,
KW   ECO:0000313|EMBL:ADH98119.1};
KW   Purine metabolism {ECO:0000256|RuleBase:RU361270};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN        4    111       TR_THY. {ECO:0000259|Pfam:PF00576}.
SQ   SEQUENCE   112 AA;  12440 MW;  50B8DDAC701734C8 CRC64;
     MGRLTTHVLN TATGLPAVGM KLILRKGNEE GGYTMLSDTV TNHDGRVDAP LLEGDAFTSG
     VYELTFFVGD YFQTEDAFLD EVPIRFTVDD ATRHYHVPLL VTPYSYTTYR GS
//

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