ID A0A7Z3C0X0_PSEFL Unreviewed; 401 AA. AC A0A7Z3C0X0; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. 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=C6Y56_01830 {ECO:0000313|EMBL:QJP93379.1}; OS Pseudomonas fluorescens. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=294 {ECO:0000313|EMBL:QJP93379.1, ECO:0000313|Proteomes:UP000501669}; RN [1] {ECO:0000313|EMBL:QJP93379.1, ECO:0000313|Proteomes:UP000501669} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G7 {ECO:0000313|EMBL:QJP93379.1, RC ECO:0000313|Proteomes:UP000501669}; RA Gao C.-H., Li Z., Cai P.; RT "Complete genome sequence of Pseudomonas fluorescens sp. G7."; RL Submitted (MAR-2018) 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 --------------------------------------------------------------------------- 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; CP027561; QJP93379.1; -; Genomic_DNA. DR UniPathway; UPA00379; UER00551. DR Proteomes; UP000501669; Chromosome. 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; 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}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00372}; 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 57..374 FT /note="Amidohydro-rel" FT /evidence="ECO:0000259|Pfam:PF01979" FT METAL 66 FT /note="Zinc or iron" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT METAL 68 FT /note="Zinc or iron" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT METAL 236 FT /note="Zinc or iron" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT METAL 311 FT /note="Zinc or iron" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 75 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 88 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 138 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 171 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 239 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" SQ SEQUENCE 401 AA; 43279 MW; BF9D9EB11BFE0AC0 CRC64; MKTLWQHCHV ATMAQGVYSI IEDAAIVTSG ALIEWIGPRS QLPSGEYPAV NDLQGAWVTP GLIDCHTHTV FGGNRSGEFE KRLQGVSYAE IAAAGGGIAS TVRATREASE DELFASAAKR LKSLMRDGVT TVEMKSGYGL DLASERKILR VIRRLAAELP ISVRSTCLAA HALPPEYKDR ADDYIDHICA EMLPALAAEG LVDAVDAFCE YLAFSPEQVE RVFIAAQKLG LPVKLHAEQL SSLHGSSLAA RYHALSADHL EFMDEADAIA MAESDTVAVL LPGAFYFLRE TQLPPMEALR KHKVKIAIAS DLNPGTSPAL SLRLMLNMAC TCFRMTPEEA LAGATIHAAQ ALGMAETHGS LEAGKVADFV AWQIDRPADL AYWLGGELDK RVVRHGVESS L //