ID HUTI_AERS4 Reviewed; 411 AA. AC A4SSN5; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 04-NOV-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=ASA_3955; OS Aeromonas salmonicida (strain A449). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Aeromonadales; Aeromonadaceae; Aeromonas. OX NCBI_TaxID=382245; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A449; RX PubMed=18801193; DOI=10.1186/1471-2164-9-427; RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., RA Brown L.L.; RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into RT the evolution of a fish pathogen."; RL BMC Genomics 9:427-427(2008). 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; CP000644; ABO91907.1; -; Genomic_DNA. DR RefSeq; WP_005316411.1; NC_009348.1. DR SMR; A4SSN5; -. DR STRING; 29491.GCA_000820065_02688; -. DR KEGG; asa:ASA_3955; -. DR PATRIC; fig|382245.13.peg.3921; -. DR eggNOG; COG1228; Bacteria. DR HOGENOM; CLU_041647_0_0_6; -. DR OMA; AAHMFPK; -. DR UniPathway; UPA00379; UER00551. 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 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 NCBIfam; TIGR01224; hutI; 1. 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 AlphaFoldDB; A4SSN5; -. PE 3: Inferred from homology; KW Cytoplasm; Histidine metabolism; Hydrolase; Iron; Metal-binding; Zinc. FT CHAIN 1..411 FT /note="Imidazolonepropionase" FT /id="PRO_0000306423" FT BINDING 75 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 77 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 77 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 84 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 147 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 147 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 180 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 245 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 245 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 248 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 320 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 320 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 322 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 324 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 325 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" SQ SEQUENCE 411 AA; 44527 MW; 821EDD22C8AA6D1F CRC64; MNKELLNCER VWLNVTPATL RPDLADYGLL EPHALGVHEG KIHALVPMQD LKGPYPAHWQ DMKGKLATPG LIDCHTHLIF AGSRAEEFEL RQKGVPYAEI ARKGGGILST VRATRAASEE QLFTLAAARI KSLIREGVTT VEIKSGYGLT LEDELKMLRV ARRLGEALPI RVKTTLLAAH AVPPEYRDDP DSWVETICQE IIPAAAEAGL ADAVDVFCEH IGFSLAQTEQ VYLAADQYGL PVKGHMEQLS NLGGSALAAN FGALSVDHLE HLDQEGIQAL AHRGVVATLL PTAFYFLKET KLPPVAALRK AHVPMAVSSD INPGTAPIVS LRMAMNMACT LFGLTPVEAM VGVTRNAARA LGEQERLGQL RVGMLADFLV WNCAHPAELS YLIGVDQLVS RVVNGEETLH G //