ID   HUTI_NEMVE              Reviewed;         429 AA.
AC   A7RX26;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Amidohydrolase domain-containing protein 1 homolog;
GN   Name=amdhd1; ORFNames=v1g163675;
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6;
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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; DS469549; EDO43954.1; -; Genomic_DNA.
DR   RefSeq; XP_001636017.1; XM_001635967.1.
DR   AlphaFoldDB; A7RX26; -.
DR   SMR; A7RX26; -.
DR   STRING; 45351.EDO43954; -.
DR   EnsemblMetazoa; EDO43954; EDO43954; NEMVEDRAFT_v1g163675.
DR   GeneID; 5515844; -.
DR   KEGG; nve:5515844; -.
DR   eggNOG; KOG3968; Eukaryota.
DR   HOGENOM; CLU_041647_2_0_1; -.
DR   InParanoid; A7RX26; -.
DR   OMA; CAPHARW; -.
DR   OrthoDB; 776380at2759; -.
DR   PhylomeDB; A7RX26; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Histidine metabolism; Hydrolase; Iron; Metal-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..429
FT                   /note="Probable imidazolonepropionase"
FT                   /id="PRO_0000328425"
FT   BINDING         161
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         161
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U8Z6"
FT   BINDING         194
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         262
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:A0KF84"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         265
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         336
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250|UniProtKB:A0KF84"
FT   BINDING         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P42084"
FT   BINDING         338
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000250|UniProtKB:Q8U8Z6"
SQ   SEQUENCE   429 AA;  46548 MW;  71ECB5C11687CF0A CRC64;
     MKNLIIRHAR QVVLVCKNGE RILKGEALKN IAILEGSVNR GISVVADEFG KIECIGYDDD
     VEPQYNQCSF ASEIDATGMC VLPGLIDGHT HPVWVGDRVH EFAMKLAGAS YMDVHKAGGG
     INFTVEHVHK ATEDELYEPL KQRLNRMLQC GTTLVEAKSG YGLNTENEMK MLKVIERAKK
     ELPIEISSTF CGAHAIPRGS TAKQAADNII NEQIPTLVKA IKAGELDVEN IDVFCEKGVF
     EVEETRVILQ AGKDAGLAIN FHGDELHPIK GAELGAELGA RAISHLEEIS EEGIKAMSKS
     SVIGVLLPTT AYILRLKPPP ARAMIDAGVA IALGTDFNPN AYCLSMPLTM HLACCILRMS
     MTEALAGATI NAAASLGRAD THGSLEVGKF ADMVVINAER WEHLIYQIGG HDDIIQHVVK
     HGKVVFSKR