ID   HUTI_DANRE              Reviewed;         433 AA.
AC   Q7SXK5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Probable imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Amidohydrolase domain-containing protein 1;
GN   Name=amdhd1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH55559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC055559; AAH55559.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001159825.2; NM_001166353.2.
DR   AlphaFoldDB; Q7SXK5; -.
DR   SMR; Q7SXK5; -.
DR   STRING; 7955.ENSDARP00000028107; -.
DR   PaxDb; Q7SXK5; -.
DR   GeneID; 402826; -.
DR   KEGG; dre:402826; -.
DR   CTD; 144193; -.
DR   ZFIN; ZDB-GENE-160728-110; amdhd1.
DR   eggNOG; KOG3968; Eukaryota.
DR   InParanoid; Q7SXK5; -.
DR   OrthoDB; 776380at2759; -.
DR   PhylomeDB; Q7SXK5; -.
DR   Reactome; R-DRE-70921; Histidine catabolism.
DR   UniPathway; UPA00379; UER00551.
DR   PRO; PR:Q7SXK5; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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..433
FT                   /note="Probable imidazolonepropionase"
FT                   /id="PRO_0000282584"
FT   BINDING         160
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         160
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U8Z6"
FT   BINDING         193
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         261
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:A0KF84"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         264
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         335
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:A0KF84"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         337
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U8Z6"
SQ   SEQUENCE   433 AA;  46904 MW;  6E818B948306DE19 CRC64;
     MSANSFKLLV KNATQLVLVC RNGEKYLTRD EMQALAVLEN ASVLIGHDGL IKAVGPADVI
     ETQFEGAKFD NVLDASGMCV LPGLVDAHTH PVWAGDRVHE FAMKLAGATY MEVHEAGGGI
     HFTVAHTRSA SEQHLLAALK SRLERMMRAG TTLVECKSGY GLELDIEVKM LRVINSARKS
     LPIGISATYC GAHAVPKGKT MEEATKDIVA VQLPKIKHLS ASGDLQVDNI DVFCEKGVFD
     LTSTRCILQA GKDMGLNINF HGDELHPMNS AHLGAELGAL AISHLEEVTD DGIVAMAKSK
     TSAVLLPTTA YILRLTPPRA RDMLDAGVIV ALGSDFNPNA YCFSMPMVMH LACVMMKMSM
     PEALAASTIN AAYALNRSQT HGSLEVGKQG DLVIINAPRW EHLVYQFGGH QELIRYVIIK
     GDFVYENDKV LNL