ID   HUTI_XENTR              Reviewed;         432 AA.
AC   Q68EP2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Probable imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Amidohydrolase domain-containing protein 1;
GN   Name=amdhd1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) 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; BC080159; AAH80159.1; -; mRNA.
DR   RefSeq; NP_001007888.1; NM_001007887.1.
DR   RefSeq; XP_012814327.1; XM_012958873.2.
DR   RefSeq; XP_017947532.1; XM_018092043.1.
DR   AlphaFoldDB; Q68EP2; -.
DR   SMR; Q68EP2; -.
DR   STRING; 8364.ENSXETP00000046755; -.
DR   MEROPS; M38.980; -.
DR   PaxDb; Q68EP2; -.
DR   Ensembl; ENSXETT00000046755; ENSXETP00000046755; ENSXETG00000021636.
DR   GeneID; 493273; -.
DR   KEGG; xtr:493273; -.
DR   CTD; 144193; -.
DR   Xenbase; XB-GENE-5845038; amdhd1.
DR   eggNOG; KOG3968; Eukaryota.
DR   HOGENOM; CLU_041647_2_0_1; -.
DR   InParanoid; Q68EP2; -.
DR   OMA; CAPHARW; -.
DR   OrthoDB; 776380at2759; -.
DR   Reactome; R-XTR-70921; Histidine catabolism.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000021636; Expressed in mesonephros and 13 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050480; F:imidazolonepropionase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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..432
FT                   /note="Probable imidazolonepropionase"
FT                   /id="PRO_0000282586"
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   432 AA;  47191 MW;  B5587A46171B83AD CRC64;
     MACKFRLLLE NAEQIVVVCS KEEEYLLEDG MQHLAILEKA SLVIGNDGFI KDVGPAETIR
     NQFSNASFEN IIDCSGKCVL PGFVDAHTHP VWAGDRVHEF AMKLAGATYM DIHKAGGGIN
     YTVEHTTTAS EEELFCSFKH RLERMLRAGT TLVECKSGYG LKLETELKML RVIERAHQEL
     DIAVSSTYCG AHSVPKGKSA QEATDDIIAN HLPALKQMAL NGEIHVDNID VFCEKGVFDL
     DSTRKILQAG KAIGLNLNFH GDELNPMNSA ELGAELGAHA VSHLEEVSDK GIAALAKAKC
     SAVLLPTTAY ILRLKQPRAR DMLKAGVIVS LGSDFNPNAY CFSMPMVMHL ACVNMKMSLK
     EALAAATINA AYALGRAHTH GSLEVGKQGD VVVINASRWE HVIYQFGGHQ ELIEYVVIKG
     KIVYKNENVL CL