ID   IXPDE_UNKP              Reviewed;         482 AA.
AC   P0CI72;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Isoxanthopterin deaminase;
DE            EC=3.5.4.11;
OS   Unknown prokaryotic organism.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=2725;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ZINC IONS, NUCLEOTIDE
RP   SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, COFACTOR, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=20415463; DOI=10.1021/bi100252s;
RA   Hall R.S., Agarwal R., Hitchcock D., Sauder J.M., Burley S.K.,
RA   Swaminathan S., Raushel F.M.;
RT   "Discovery and structure determination of the orphan enzyme isoxanthopterin
RT   deaminase.";
RL   Biochemistry 49:4374-4382(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-amino-4-hydroxypteridine + H(+) + H2O = a 2,4-
CC         dihydroxypteridine + NH4(+); Xref=Rhea:RHEA:36055, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:73184,
CC         ChEBI:CHEBI:73186; EC=3.5.4.11;
CC         Evidence={ECO:0000269|PubMed:20415463};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:20415463};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20415463};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8 uM for isoxanthopterin {ECO:0000269|PubMed:20415463};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ATZ/TRZ family. {ECO:0000305}.
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DR   EMBL; EP885471; EDA75601.1; -; Genomic_DNA.
DR   PDB; 2PAJ; X-ray; 2.70 A; A=1-482.
DR   PDBsum; 2PAJ; -.
DR   AlphaFoldDB; P0CI72; -.
DR   SMR; P0CI72; -.
DR   BRENDA; 3.5.4.11; 12464.
DR   SABIO-RK; P0CI72; -.
DR   EvolutionaryTrace; P0CI72; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050228; F:pterin deaminase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.30.40.10; -; 2.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..482
FT                   /note="Isoxanthopterin deaminase"
FT                   /id="PRO_0000403657"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         79
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   BINDING         334
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
SQ   SEQUENCE   482 AA;  51752 MW;  B4EDD98108D5DE26 CRC64;
     MTTYDTQPST LIRNAAAIMT GGRGTADDPS RVPGPDIRIV GDTIDAIGAL APRPGETIVD
     ATDCVIYPAW VNTHHHLFQS LLKGEPAGLD ATLTPWLAAT PYRFRALFDE RRFRLAARIG
     LIELARSGCA TVADHNYVYY PGMPFDSSAI LFEEAEKLGL RFVLLRGGAT QTRQLEADLP
     TALRPETLDA YVADIERLAA RYHDASPRAM RRVVMAPTTV LYSISPREMR ETAAVARRLG
     LRMHSHLSET VGYQDSAYSM YGKSPVAFCG EHDWLGSDVW YAHLVKVDAD EIALLAQTGT
     GVAHCPQSNG RLGSGICPVR EMADAGVPVS IGVDGAASNE AADMISEVHM TWLAQRARLG
     MLAQPAYRGG SFEGGAGAAS IAEVIHWGTA GGARVMGLDE VGKVAVGYAA DIAVYRLDDP
     RYFGLHDPAI GPVASGGRPS VMALFSAGKR VVVDDLIEGV DIKELGGEAR RVVRELLREV
     VV