ID   HUTI_XENLA              Reviewed;         438 AA.
AC   Q561L6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Probable imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Amidohydrolase domain-containing protein 1;
GN   Name=amdhd1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate;
CC         Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377, ChEBI:CHEBI:58928,
CC         ChEBI:CHEBI:77893; EC=3.5.2.7;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc or iron ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       HutI family. {ECO:0000305}.
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DR   EMBL; BC093541; AAH93541.1; -; mRNA.
DR   RefSeq; NP_001089368.1; NM_001095899.1.
DR   AlphaFoldDB; Q561L6; -.
DR   SMR; Q561L6; -.
DR   BioGRID; 592199; 1.
DR   GeneID; 734418; -.
DR   KEGG; xla:734418; -.
DR   CTD; 734418; -.
DR   Xenbase; XB-GENE-5845072; amdhd1.L.
DR   OrthoDB; 776380at2759; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 734418; Expressed in kidney and 10 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050480; F:imidazolonepropionase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   CDD; cd01296; Imidazolone-5PH; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR005920; HutI.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR42752; PTHR42752; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01224; hutI; 1.
PE   2: Evidence at transcript level;
KW   Histidine metabolism; Hydrolase; Iron; Metal-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..438
FT                   /note="Probable imidazolonepropionase"
FT                   /id="PRO_0000282585"
FT   BINDING         159
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         159
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U8Z6"
FT   BINDING         192
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         260
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:A0KF84"
FT   BINDING         260
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         263
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         334
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:A0KF84"
FT   BINDING         334
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         336
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U8Z6"
SQ   SEQUENCE   438 AA;  47810 MW;  65BA083A3FD16222 CRC64;
     MASKFRLLLE NAEQIVVVCT KEEQYLLEDG MQHLAVLEKS SLVIGNDGCI KAVGPAETIR
     NHFSNASFEN IIDCSGKCIL PGFVDAHIHP VWAGDRVHEF AMKLAGATYM DIHQAGGGIN
     YTVEHTTAAS VEELFCSFKH RLERMLRAGT TLVECKSGYG LKLETELKML RVIERAHREL
     DIAVSSTYCG AHSVPKGKSA QEAADDIINN HLPALKQMSL NGEIHVDNID VFCEKGVFDL
     ESTGRILQAG KAIGLNLNFH GDELNPMNSA ELGAELGAHA VSHLEEVSDK GIAALAKAKC
     SAVLLPTTAY ILRLKQPRAR DMLKAGVIVS LGSDFNPNAY CFSMPMVMHL ACVNMKMSLK
     EALAAATINA AYALGRAHTH GSLEVGKQGD VVVINASRWE HVIYQFGGHQ ELIECVVIKG
     KIVYKNEKFS ICRMDLLK