ID HUTI_MARMM Reviewed; 402 AA. AC Q0AP91; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 02-SEP-2026, entry version 100. DE RecName: Full=Imidazolonepropionase {ECO:0000255|HAMAP-Rule:MF_00372}; DE EC=3.5.2.7 {ECO:0000255|HAMAP-Rule:MF_00372}; DE AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00372}; GN Name=hutI {ECO:0000255|HAMAP-Rule:MF_00372}; GN OrderedLocusNames=Mmar10_1604; OS Maricaulis maris (strain MCS10) (Caulobacter maris). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Maricaulales; Maricaulaceae; Maricaulis. OX NCBI_TaxID=394221; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS10; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., RA Stephens C., Richardson P.; RT "Complete sequence of Maricaulis maris MCS10."; RL Submitted (AUG-2006) 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:0000255|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:0000255|HAMAP- CC Rule:MF_00372}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00372}; CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00372}; CC Note=Binds 1 zinc or iron ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00372}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00372}. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC HutI family. {ECO:0000255|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; CP000449; ABI65896.1; -; Genomic_DNA. DR RefSeq; WP_011643543.1; NC_008347.1. DR AlphaFoldDB; Q0AP91; -. DR SMR; Q0AP91; -. DR STRING; 394221.Mmar10_1604; -. DR KEGG; mmr:Mmar10_1604; -. DR eggNOG; COG1228; Bacteria. DR HOGENOM; CLU_041647_0_0_5; -. DR OrthoDB; 9776455at2; -. DR UniPathway; UPA00379; UER00551. DR Proteomes; UP000001964; 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:0006548; P:L-histidine catabolic process; IEA:UniProtKB-UniRule. DR FunFam; 3.20.20.140:FF:000007; Imidazolonepropionase; 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; Histidine metabolism; Hydrolase; Iron; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1..402 FT /note="Imidazolonepropionase" FT /id="PRO_0000306472" FT BINDING 69 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 71 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 78 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 141 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 141 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 174 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 239 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 239 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 242 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 314 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 314 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 316 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 318 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 319 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" SQ SEQUENCE 402 AA; 42417 MW; 7EFC49E6950AA33D CRC64; MQFDRLLTEA RLATMVAGDD GYGVIEKAAL GIKDGRIAWI GPMSEIPGEA RETERLASRW VTPALIDCHT HLVFAGDRSD EFERRLGGES YESISRSGGG IARSVEATRA AGAAELAAGA LTRIDALAQE GVGTVEIKSG YGLTRESERT MLRAARGVER ASGMRVSATL LAAHAVPPEY KGESGRYIDE ICIPLIREAA REGLADAVDA YCEGIGFSPE ETRRLFIAAK AAGLPVKLHA DQLSDTGGAR LVAEFGGLSA DHIEYTNAEG IAAMAKAGTV GVLLPGAFYA LNETKKPPVE AMRAAGVDMA VATDANPGTS PLVSLLTAAN MACILFGLTL PEAFAGMTRN AARALGLHGE IGTLEVGKAA DLAIWDVERP AEIIQWIGRR PLHGRILAGE WQ //