ID H2MPX8_ORYLA Unreviewed; 432 AA.
AC H2MPX8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 66.
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|Ensembl:ENSORLP00000020791.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000020791.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000020791.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000020791.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000020791.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000020791.2};
RG Ensembl;
RL Submitted (NOV-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_004083259.1; XM_004083211.2.
DR AlphaFoldDB; H2MPX8; -.
DR STRING; 8090.ENSORLP00000020791; -.
DR Ensembl; ENSORLT00000020792.2; ENSORLP00000020791.2; ENSORLG00000016609.2.
DR GeneID; 101169652; -.
DR KEGG; ola:101169652; -.
DR CTD; 144193; -.
DR eggNOG; KOG3968; Eukaryota.
DR GeneTree; ENSGT00390000008645; -.
DR HOGENOM; CLU_041647_2_0_1; -.
DR InParanoid; H2MPX8; -.
DR OrthoDB; 2429159at2759; -.
DR TreeFam; TF312878; -.
DR UniPathway; UPA00379; UER00551.
DR Proteomes; UP000001038; Chromosome 23.
DR Bgee; ENSORLG00000016609; Expressed in liver and 14 other cell types or 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; 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:UP000001038};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 79..423
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 432 AA; 46786 MW; 62AC67E0AF2DEFE9 CRC64;
MSENQRLLVK NAKQVVLICR NGEKFLNKDG MKSLSVIENG SVVIGRDGLI KAVGPAETIS
AQYPESSCDH VIDATDMCVL PGLVDAHTHP VWAGDRVHEF AMKLAGASYM DVHRAGGGIH
FTVEHTRAAA ASELLDALTR RLQRMLRAGT TLVECKSGYG LELQTEVKML EVIEAARRSL
PINISSTYCG AHAVPKGRTE AEATADVLQV QLPRLKELMS AGTLQVDNID VFCERGVFGL
SSTHRILQAG RDMGLNINFH GDELHPMNSA QLGAELGALA ISHLEEVTDE GIVAMATAKT
AAILLPTTAY ILRLPQPRAR DMLDAGVIVA LGSDFNPNAF CCSMPIVMHL ACVNMRMSMS
EALAAATINA AYALGRAHTH GSLEVSKHGD LLVLNCSRWE HLIYQLGGHQ EILRYVVIKG
NIVHDNDKTM QM
//
