ID A0A7Y4FMW0_9VIBR Unreviewed; 408 AA. AC A0A7Y4FMW0; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 22-FEB-2023, entry version 6. DE RecName: Full=Imidazolonepropionase {ECO:0000256|HAMAP-Rule:MF_00372}; DE EC=3.5.2.7 {ECO:0000256|HAMAP-Rule:MF_00372}; DE AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000256|HAMAP-Rule:MF_00372}; GN Name=hutI {ECO:0000256|HAMAP-Rule:MF_00372}; GN ORFNames=F0237_17765 {ECO:0000313|EMBL:NOI82519.1}; OS Vibrio tubiashii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio; Vibrio oreintalis group. OX NCBI_TaxID=29498 {ECO:0000313|EMBL:NOI82519.1, ECO:0000313|Proteomes:UP000572722}; RN [1] {ECO:0000313|EMBL:NOI82519.1, ECO:0000313|Proteomes:UP000572722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=01-65-5-1 {ECO:0000313|EMBL:NOI82519.1, RC ECO:0000313|Proteomes:UP000572722}; RA Kehlet-Delgado H., Mueller R.S.; RT "Draft genome sequencing and comparative genomics of hatchery-associated RT Vibrios."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond CC in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is CC the third step in the universal histidine degradation pathway. CC {ECO:0000256|HAMAP-Rule:MF_00372}. 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00372}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00372}; CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00372}; CC Note=Binds 1 zinc or iron ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00372}; 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|HAMAP-Rule:MF_00372}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC HutI family. {ECO:0000256|HAMAP-Rule:MF_00372}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NOI82519.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VTXO01000008; NOI82519.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7Y4FMW0; -. DR UniPathway; UPA00379; UER00551. DR Proteomes; UP000572722; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050480; F:imidazolonepropionase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. 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 HAMAP; MF_00372; HutI; 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; 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. DR TIGRFAMs; TIGR01224; hutI; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372}; KW Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP- KW Rule:MF_00372}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00372, ECO:0000313|EMBL:NOI82519.1}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00372}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00372}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00372}. FT DOMAIN 64..384 FT /note="Amidohydrolase-related" FT /evidence="ECO:0000259|Pfam:PF01979" FT BINDING 73 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 75 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 82 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 145 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 145 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 178 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 243 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 243 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 246 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 318 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 318 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 320 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 322 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 323 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" SQ SEQUENCE 408 AA; 44057 MW; 5B579FCA640CCFD2 CRC64; MSLTSDLILV NAKIVSMTEG SDGYSVSPLC NIYIKDGRIQ SIAQETLDSE VNPSGNCYDC KGKLVTPGFI DCHTHLIFAG SRANEFEMRL KGVPYQEIAK QGGGILSTVR ATREASEQQL TELALPRLDG LIQSGVTSVE VKSGYGLTLN DELKMLRAAK ALEEHRKIRV STTLLAAHAL PPEYSGRADD YIELVCQEII PAAAQENLAT SVDVFCESIG FNLAQTEKVY QAAIDNGLAI KGHTEQLSNL GGTALTAKYN GLSADHIEFL DENGVIALAQ SNTVATLLPG AFYFLRETQL PPIELLRQHK IPMAIATDLN PGTSPFADLT MIMNMGCTLF GLTPEETLRG VTNHAAQAIG FGESRGQIKQ GFDADLAIWD VTHPAEFSYF QGAPRLSARL VAGELDHV //