ID A0A7Y4FMW0_9VIBR Unreviewed; 408 AA. AC A0A7Y4FMW0; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=Imidazolonepropionase {ECO:0000256|ARBA:ARBA00012864, ECO:0000256|HAMAP-Rule:MF_00372}; DE EC=3.5.2.7 {ECO:0000256|ARBA:ARBA00012864, 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 -!- 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, 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(2+); Xref=ChEBI:CHEBI:29033; 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|ARBA:ARBA00004758, 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 UniPathway; UPA00379; UER00551. DR Proteomes; UP000572722; Unassembled WGS sequence. DR GO; GO:0050480; F:imidazolonepropionase activity; IEA:UniProtKB-EC. DR CDD; cd01296; Imidazolone-5PH; 1. DR Gene3D; 2.30.40.10; -; 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; PTHR42752; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; SSF51338; 1. DR SUPFAM; SSF51556; SSF51556; 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..386 FT /note="Amidohydro-rel" FT /evidence="ECO:0000259|Pfam:PF01979" FT METAL 73 FT /note="Zinc or iron" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT METAL 75 FT /note="Zinc or iron" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT METAL 243 FT /note="Zinc or iron" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT METAL 318 FT /note="Zinc or iron" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 82 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 95 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 145 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 178 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 246 FT /note="Substrate" 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 //