ID   A0A383YSV9_BALAS        Unreviewed;       426 AA.
AC   A0A383YSV9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Probable imidazolonepropionase {ECO:0000256|ARBA:ARBA00013406};
DE            EC=3.5.2.7 {ECO:0000256|ARBA:ARBA00012864};
DE   AltName: Full=Amidohydrolase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00030968};
GN   Name=AMDHD1 {ECO:0000313|RefSeq:XP_007165923.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007165923.1};
RN   [1] {ECO:0000313|RefSeq:XP_007165923.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007165923.1};
RG   RefSeq;
RL   Submitted (JAN-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00000853};
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC         Evidence={ECO:0000256|ARBA:ARBA00001965};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004758}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       HutI family. {ECO:0000256|ARBA:ARBA00008002}.
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DR   RefSeq; XP_007165923.1; XM_007165861.2.
DR   AlphaFoldDB; A0A383YSV9; -.
DR   STRING; 310752.A0A383YSV9; -.
DR   GeneID; 103010310; -.
DR   KEGG; bacu:103010310; -.
DR   CTD; 144193; -.
DR   InParanoid; A0A383YSV9; -.
DR   OrthoDB; 2429159at2759; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000261681; Unplaced.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR005920; HutI.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR01224; hutI; 1.
DR   PANTHER; PTHR42752; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR42752:SF1; IMIDAZOLONEPROPIONASE-RELATED; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Histidine metabolism {ECO:0000256|ARBA:ARBA00022808};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          79..422
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   426 AA;  46581 MW;  42DEF8F6EE5BDB2C CRC64;
     MAGGHRLLLE NARQVVLVCA RGERFLARDA LRSLAVLEDA SLVVGIDGFI KAIGPGDAIQ
     KQFSEETFQE RIDCTGKCIL PGLVDAHTHP VWAGERVHEF AMKLAGATYM DIHQAGGGIN
     FTVERTRQAS EEALFSSFRQ RLGCMMRAGT TLAECKSGYG LNLETELKML RVIERARREL
     DIGISATYCG AHSVPKGKTA TEAADDIINN HLPKLKELGR NGEIHVDNID VFCEKGVFDL
     DSTRRILQSG KDIGLQINFH GDELHPMKAA ELGVELGAKA ISHLEEVSDE GIAAMAAARC
     SAVLLPTTAY MLRLKQPRAR KMLDEGVIVA LGSDFNPNAY CFSMPMVMHL ACVNMRMSMP
     EALAAATINA AYALGKSHTH GSLEVGKQGD LIIINSSRWE HLIYQFGGHH ELIDYVIAKG
     KVIYKK
//