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Database: UniProt
Entry: A0A2G5CN80_AQUCA
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ID   A0A2G5CN80_AQUCA        Unreviewed;       333 AA.
AC   A0A2G5CN80;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PIA32736.1};
GN   ORFNames=AQUCO_04400142v1 {ECO:0000313|EMBL:PIA32736.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA32736.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA32736.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001163};
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|ARBA:ARBA00001043};
CC   -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC       urate: step 3/3. {ECO:0000256|ARBA:ARBA00004754}.
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DR   EMBL; KZ305061; PIA32736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5CN80; -.
DR   STRING; 218851.A0A2G5CN80; -.
DR   InParanoid; A0A2G5CN80; -.
DR   OrthoDB; 324942at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033971; F:hydroxyisourate hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05822; TLP_HIUase; 1.
DR   Gene3D; 1.10.3330.10; Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase; 1.
DR   Gene3D; 2.60.40.180; Transthyretin/hydroxyisourate hydrolase domain; 1.
DR   InterPro; IPR014306; Hydroxyisourate_hydrolase.
DR   InterPro; IPR018020; OHCU_decarboxylase.
DR   InterPro; IPR036778; OHCU_decarboxylase_sf.
DR   InterPro; IPR023418; Thyroxine_BS.
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   NCBIfam; TIGR02962; hdxy_isourate; 1.
DR   PANTHER; PTHR43466; 2-OXO-4-HYDROXY-4-CARBOXY-5-UREIDOIMIDAZOLINE DECARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR43466:SF1; 2-OXO-4-HYDROXY-4-CARBOXY-5-UREIDOIMIDAZOLINE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF09349; OHCU_decarbox; 1.
DR   Pfam; PF00576; Transthyretin; 1.
DR   PRINTS; PR00189; TRNSTHYRETIN.
DR   SUPFAM; SSF49472; Transthyretin (synonym: prealbumin); 1.
DR   SUPFAM; SSF158694; UraD-Like; 1.
DR   PROSITE; PS00768; TRANSTHYRETIN_1; 1.
DR   PROSITE; PS00769; TRANSTHYRETIN_2; 1.
PE   4: Predicted;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Purine metabolism {ECO:0000256|ARBA:ARBA00022631};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069}.
FT   DOMAIN          8..158
FT                   /note="Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
FT                   decarboxylase"
FT                   /evidence="ECO:0000259|Pfam:PF09349"
FT   DOMAIN          214..332
FT                   /note="Transthyretin/hydroxyisourate hydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF00576"
FT   REGION          64..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         217
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600895-51"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600895-51"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600895-51"
SQ   SEQUENCE   333 AA;  36738 MW;  77115C251D4E300A CRC64;
     MDSRFEEKEF VACCGSIKFA QQLAAAAGGS DNLEELVETA RDIWFNKVDV NGWLEAFAAH
     PQIGQTSSPN TNTETSAQWS KGEQSTALAT STHSTLQELF DWNAQYRQKF GFVFLICASG
     RTTPEILSEL KMRYSNRPIV ELEIAAQEQM KITELRLAKL FAIKTTSKIN NEIPYGLVNK
     AGEDRVSLLS AHLNAGSYSA NKPSQVSNRT RPPITTHVLD VSRGSPAAGI EVQLEIWNGA
     KPPPFSGEVG SGFWIFQGSS ITNADGRSGH LMHIVDNVEP GVYRISFNTG KYSPDGFYPY
     VSIVFEIKES QKGEHFHVPI LLSPFSFSTY RGS
//
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