ID HUTI_BRUAB Reviewed; 405 AA. AC Q579E7; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 99. 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=BruAb2_0304; OS Brucella abortus biovar 1 (strain 9-941). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=262698; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=9-941; RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005; RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.; RT "Completion of the genome sequence of Brucella abortus and comparison to RT the highly similar genomes of Brucella melitensis and Brucella suis."; RL J. Bacteriol. 187:2715-2726(2005). 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; AE017224; AAX75737.1; -; Genomic_DNA. DR RefSeq; WP_002965718.1; NC_006933.1. DR AlphaFoldDB; Q579E7; -. DR SMR; Q579E7; -. DR EnsemblBacteria; AAX75737; AAX75737; BruAb2_0304. DR GeneID; 3827134; -. DR KEGG; bmb:BruAb2_0304; -. DR HOGENOM; CLU_041647_0_0_5; -. DR UniPathway; UPA00379; UER00551. DR Proteomes; UP000000540; Chromosome II. 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; Histidine metabolism; Hydrolase; Iron; Metal-binding; Zinc. FT CHAIN 1..405 FT /note="Imidazolonepropionase" FT /id="PRO_0000306443" FT BINDING 73 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" 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 82 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 145 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 145 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 178 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 243 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 243 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 246 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 318 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 318 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 320 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" 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 323 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" SQ SEQUENCE 405 AA; 43520 MW; A55470DFB24E994E CRC64; MTKNSSTVFT HARIATLEEK AANLGLIEEA ALVVKDARIV YAGPENKLPD EYASFEKIDC GNRLITPGLI DCHTHLVHAG NRAHEFELRL QGATYEEVAR AGGGIVSSVR NLRAASEDDL VRETLPRLDA LIAEGVTTVE VKSGYGLDRD SEIKSLKAAR RLGEERDVAI RTTFLGAHAL PPEMNGDKAA YIDRVINDML PAIAEQGLAD AVDGFCEGIA FLPDEIARVF DAAKAHDIPV KLHADQLSNL HGAALAASYG ALSADHLEYT DADGAAAMAS AGTVAVLLPG AYYFIRETQK PPVEAFRAAG TKMALATDNN PGTSPLTSLL LTMNMGATLF RMTVEECIAG VTREAARALG ILDQTGTLEI GKDADLAIWD IERPAELVYR IGFNPLWKRV FKGQI //