ID C3K811_PSEFS Unreviewed; 402 AA. AC C3K811; DT 16-JUN-2009, integrated into UniProtKB/TrEMBL. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 109. 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 OrderedLocusNames=PFLU_0369 {ECO:0000313|EMBL:CAY46646.1}; OS Pseudomonas fluorescens (strain SBW25). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY46646.1}; RN [1] {ECO:0000313|EMBL:CAY46646.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY46646.1}; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M., RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(2009). RN [2] {ECO:0000313|EMBL:CAI2794693.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SBW25 {ECO:0000313|EMBL:CAI2794693.1}; RA Fortmann-Grote C.; RL Submitted (OCT-2023) 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00372}; CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; OV986001; CAI2794693.1; -; Genomic_DNA. DR EMBL; AM181176; CAY46646.1; -; Genomic_DNA. DR AlphaFoldDB; C3K811; -. DR STRING; 294.SRM1_00419; -. DR eggNOG; COG1228; Bacteria. DR HOGENOM; CLU_041647_0_0_6; -. DR UniPathway; UPA00379; UER00551. DR Proteomes; UP001152918; 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; 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 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 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|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00372}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00372}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00372}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00372}. FT DOMAIN 58..376 FT /note="Amidohydrolase-related" FT /evidence="ECO:0000259|Pfam:PF01979" FT BINDING 67 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 69 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 76 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 139 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 139 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 172 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 237 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 237 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 240 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 312 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 312 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 314 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 316 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" FT BINDING 317 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372" SQ SEQUENCE 402 AA; 43437 MW; 720EC70C8508BC5C CRC64; MMKTLWQHCH VATMAQGKYS IIEDAALVTA GSLIEWVGPR SQVPTADYAQ VHDLHGAWVT PGLIDCHTHT VFGGNRSGEF EQRLEGVSYA EIAAKGGGIA STVRATRAAT EDELFASAEK RLRSLLRDGV TTVEIKSGYG LDLVNERKLL RVARRLGEAL PVSVRATCLA AHALPPEYKD RADDYIDHIC TEMLPALAAE GLVDAVDAFC EYLAFSTEQV ERVFKVAQQL GLPVKLHAEQ LSSLHGSSLA ARYHALSADH LEFMTEEDAI AMAASGTVAV LLPGAFYFLR ETQLPPMEAL RKHGVKIAIA SDLNPGTSPA LSVRLMLNMA CTLFRMTPEE ALAGATQHAA TALGMGDTHG SLEVGKVADF VAWQIDRPAD LAYWLGGELD KRVVRHGVDV TV //