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Database: UniProt
Entry: I1MM35_SOYBN
LinkDB: I1MM35_SOYBN
Original site: I1MM35_SOYBN 
ID   I1MM35_SOYBN            Unreviewed;       332 AA.
AC   I1MM35;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRH07309.1, ECO:0000313|EnsemblPlants:KRH07309};
GN   ORFNames=GLYMA_16G080700 {ECO:0000313|EMBL:KRH07309.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH07309.1};
RN   [1] {ECO:0000313|EMBL:KRH07309.1, ECO:0000313|EnsemblPlants:KRH07309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH07309};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH07309.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH07309}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH07309};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH07309.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH07309.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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; CM000849; KRH07309.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1MM35; -.
DR   SMR; I1MM35; -.
DR   STRING; 3847.I1MM35; -.
DR   PaxDb; 3847-GLYMA16G08930-1; -.
DR   EnsemblPlants; KRH07309; KRH07309; GLYMA_16G080700.
DR   Gramene; KRH07309; KRH07309; GLYMA_16G080700.
DR   eggNOG; KOG3006; Eukaryota.
DR   InParanoid; I1MM35; -.
DR   OrthoDB; 324942at2759; -.
DR   Proteomes; UP000008827; Chromosome 16.
DR   ExpressionAtlas; I1MM35; baseline and differential.
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; IBA:GO_Central.
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:UP000008827}.
FT   DOMAIN          9..157
FT                   /note="Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline
FT                   decarboxylase"
FT                   /evidence="ECO:0000259|Pfam:PF09349"
FT   DOMAIN          213..331
FT                   /note="Transthyretin/hydroxyisourate hydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF00576"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600895-51"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600895-51"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600895-51"
SQ   SEQUENCE   332 AA;  36413 MW;  866B9097F1246FE3 CRC64;
     MEFSFDEKDF ASCCGSTKFA KEMASASPFR SFQDAVSVAK GVWFNSVDVN GWLQAFSAHP
     QIGQTHAPSV ASEASAQWSK GEQSTALATA TGSSLQELSE WNARYREKFG FVFLICAAGR
     STDEILAELK RRYTNRPIVE FEIAAQEQMK ITELRLAKLF SSRENISSSV DKYSAAKKAE
     EDRISIIGGH VTAASEISTA KLIHHPARTR PPITTHVLDV SQGSPAAGIE VLLEVWRGTQ
     SRPTFGASGG GSWVFQGSST TDLDGRSGQL LSIVDDVNPG IYRISFNTGK YIPNGFFPYV
     SLVFEIKESQ KREHFHVPLL LSPFSFSTYR GS
//
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