ID   HUTI_BOVIN              Reviewed;         426 AA.
AC   A5PJV3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Probable imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Amidohydrolase domain-containing protein 1;
GN   Name=AMDHD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) 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; BC142251; AAI42252.1; -; mRNA.
DR   RefSeq; NP_001092342.1; NM_001098872.2.
DR   AlphaFoldDB; A5PJV3; -.
DR   SMR; A5PJV3; -.
DR   STRING; 9913.ENSBTAP00000021647; -.
DR   PaxDb; A5PJV3; -.
DR   PeptideAtlas; A5PJV3; -.
DR   Ensembl; ENSBTAT00000021647; ENSBTAP00000021647; ENSBTAG00000016275.
DR   GeneID; 505315; -.
DR   KEGG; bta:505315; -.
DR   CTD; 144193; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016275; -.
DR   VGNC; VGNC:25860; AMDHD1.
DR   eggNOG; KOG3968; Eukaryota.
DR   GeneTree; ENSGT00390000008645; -.
DR   HOGENOM; CLU_041647_2_0_1; -.
DR   InParanoid; A5PJV3; -.
DR   OMA; CAPHARW; -.
DR   OrthoDB; 776380at2759; -.
DR   TreeFam; TF312878; -.
DR   Reactome; R-BTA-70921; Histidine catabolism.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000016275; Expressed in liver and 98 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; 2.
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..426
FT                   /note="Probable imidazolonepropionase"
FT                   /id="PRO_0000314849"
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   426 AA;  46749 MW;  4FB869F59608701B CRC64;
     MAGGHRLLLE NARQVVLVCA RGERFLTRDA LRSLEVLEGA SLVVGTDGFI KAIGPADAIQ
     KQFSEETFEE RIDCSGKCIL PGLVDAHTHP VWAGERVHEF AMKLAGATYM DIHQAGGGIN
     FTVERTRQAS EEELYSSFQQ RLGCMMRAGT TLVECKSGYG LNLETELKML RVIERARQEL
     DIGISATYCG AHSVPKGKTA SEAADDIIKN HLPRLKELGR NGEIHVDNID VFCEKDVFDL
     DSTRRILQSG KDIGLQINFH GDELHPMKAA ELGVELGAQA ISHLEEVSDE GIAAMASARC
     SAVLLPTTAY MLRLKQPRAR KMLDEGVIVA LGSDFNPNAY CFSMPMVMHL ACVNMRMSMP
     EALAAATINA AYALGKSHTQ GSLEVGKQGD LIIINSPRWE HLIYQFGGHH ELIDYVIAKG
     KVIYKK