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URAD_HALVD
ID   URAD_HALVD              Reviewed;         168 AA.
AC   D4GPU8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase;
DE            Short=OHCU decarboxylase;
DE            EC=4.1.1.97;
GN   OrderedLocusNames=HVO_B0301;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG   Plasmid pHV3.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
CC   -!- FUNCTION: Catalyzes the stereoselective decarboxylation of 2-oxo-4-
CC       hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-
CC         carboxylate + H(+) = (S)-allantoin + CO2; Xref=Rhea:RHEA:26301,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15678, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:58639; EC=4.1.1.97;
CC   -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC       urate: step 3/3.
CC   -!- SIMILARITY: Belongs to the OHCU decarboxylase family. {ECO:0000305}.
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DR   EMBL; CP001953; ADE01468.1; -; Genomic_DNA.
DR   RefSeq; WP_004041239.1; NZ_AOHU01000021.1.
DR   AlphaFoldDB; D4GPU8; -.
DR   SMR; D4GPU8; -.
DR   STRING; 309800.C498_02150; -.
DR   EnsemblBacteria; ADE01468; ADE01468; HVO_B0301.
DR   GeneID; 8919056; -.
DR   KEGG; hvo:HVO_B0301; -.
DR   eggNOG; arCOG11423; Archaea.
DR   HOGENOM; CLU_092522_1_1_2; -.
DR   OMA; KICHLRL; -.
DR   OrthoDB; 98147at2157; -.
DR   UniPathway; UPA00394; UER00652.
DR   Proteomes; UP000008243; Plasmid pHV3.
DR   GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IEA:RHEA.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000255; P:allantoin metabolic process; IEA:InterPro.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.3330.10; -; 1.
DR   InterPro; IPR018020; OHCU_decarboxylase.
DR   InterPro; IPR017580; OHCU_decarboxylase-1.
DR   InterPro; IPR036778; OHCU_decarboxylase_sf.
DR   Pfam; PF09349; OHCU_decarbox; 1.
DR   SUPFAM; SSF158694; SSF158694; 1.
DR   TIGRFAMs; TIGR03164; UHCUDC; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Oxidoreductase; Plasmid; Purine metabolism;
KW   Reference proteome.
FT   CHAIN           1..168
FT                   /note="2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
FT                   decarboxylase"
FT                   /id="PRO_0000411958"
FT   REGION          70..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        70
FT                   /note="Proton donor; for OHCU decarboxylase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         83..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         118..122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   168 AA;  19373 MW;  4D5CA9344E2CBFA6 CRC64;
     MHELTLQQVN RLDDDSFVDA FGEIYEHSPW VAERARSSRP FSSVDELRSA MKRAVEDASR
     EKQLQLLRAH PDLGERTEMT DASEAEQASA ELDSLSRSQY ETFQRLNETY RERFGFPFVM
     AVKDENPDAI AAAMERRVDH SESTEFRTAL DEVHTIAELR LAERFSSE
 
 
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