HIUH_SOYBN
ID HIUH_SOYBN Reviewed; 560 AA.
AC Q8S3J3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Hydroxyisourate hydrolase;
DE Short=HIU hydrolase;
DE Short=HIUHase;
DE EC=3.5.2.17;
DE Flags: Precursor;
GN Name=HIUH;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLU-199 AND GLU-408,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12481089; DOI=10.1104/pp.011049;
RA Raychaudhuri A., Tipton P.A.;
RT "Cloning and expression of the gene for soybean hydroxyisourate hydrolase.
RT Localization and implications for function and mechanism.";
RL Plant Physiol. 130:2061-2068(2002).
RN [2]
RP PROTEIN SEQUENCE OF 32-47, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10567345; DOI=10.1074/jbc.274.48.33863;
RA Sarma A.D., Serfozo P., Kahn K., Tipton P.A.;
RT "Identification and purification of hydroxyisourate hydrolase, a novel
RT ureide-metabolizing enzyme.";
RL J. Biol. Chem. 274:33863-33865(1999).
CC -!- FUNCTION: Involved in the conversion of hydroxyisourate to ureides such
CC as allantoin, the major form of nitrogen transport in legumes.
CC {ECO:0000269|PubMed:12481089}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for hydroxyisourate {ECO:0000269|PubMed:10567345};
CC -!- PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from
CC urate: step 2/3.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10567345}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:12481089}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12481089}.
CC -!- TISSUE SPECIFICITY: Highly expressed in uninfected root nodules.
CC Detected in leaves, stems and roots. {ECO:0000269|PubMed:12481089}.
CC -!- DEVELOPMENTAL STAGE: Expression in nodules increased with increasing
CC plant age up to 21 days, then decreased.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AF486839; AAL92115.1; -; mRNA.
DR RefSeq; NP_001236535.1; NM_001249606.1.
DR AlphaFoldDB; Q8S3J3; -.
DR SMR; Q8S3J3; -.
DR STRING; 3847.GLYMA02G02230.3; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR PRIDE; Q8S3J3; -.
DR GeneID; 547954; -.
DR KEGG; gmx:547954; -.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q8S3J3; -.
DR BioCyc; MetaCyc:MON-13506; -.
DR BRENDA; 3.5.2.17; 2483.
DR SABIO-RK; Q8S3J3; -.
DR UniPathway; UPA00394; UER00651.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR GO; GO:0033971; F:hydroxyisourate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate 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 InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Peroxisome;
KW Purine metabolism; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..560
FT /note="Hydroxyisourate hydrolase"
FT /id="PRO_0000380689"
FT TOPO_DOM 32..517
FT /note="Peroxisomal"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 408
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 199
FT /note="E->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:12481089"
FT MUTAGEN 408
FT /note="E->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:12481089"
SQ SEQUENCE 560 AA; 63767 MW; CFCD946245D9E528 CRC64;
MMEPPQTRLM INVFIVSFLA LLVNLVVGVL GADNYSRDDF PLDFVFGSGT SAYQVEGAAN
KDGRTPSIWD TFAYAGYAHG ENGDVACDGY HKYKEDVQLM LETGLDAYRF SISWSRLLPN
GRGPVNPKGL QYSNNLINEL ISNGIQPHAT LYNFDLPQVL EDEYGGWISR DIIRDFTYYA
EVEFREFGDR VLYWTTVNEP NVFALGGYDQ GNSPPRRCSP PFCATNDTMG NSTYEPYLAV
HHILLSHSSA ARLYWRKYRD KQHGFVGISI YTFGIFPQTN TEKDRVASQR ARDFFVGWIM
EPLQYGDYPI SMKTNAGERI PAFTNHESKQ VKGSFDFIGV IHYTNLNVSD NSDALKNQLR
DFTADMAANI FGEDLFSNEE YLITPWGLRQ ELNKFKLLYG NPPIFIHENG QRTASNSSLQ
DVDKGEILHG YIGSVLDALR DASNIKGYFR MAFPGFVRVA RWIQVSFGLY YVDRDDPQLK
KIPKLFCKNG TTGFLKGRRT SILDLFELEQ DPITCSKSPI IFSKISKWVL ASLLFLIQHK
IKFMWREPLP GQIPLKLVMF
