ID HUTI_HERA2 Reviewed; 427 AA. AC A9AW17; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, 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=Haur_0607; OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95). OC Bacteria; Bacillati; Chloroflexota; Chloroflexia; Herpetosiphonales; OC Herpetosiphonaceae; Herpetosiphon. OX NCBI_TaxID=316274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 23779 / DSM 785 / 114-95; RX PubMed=22675585; DOI=10.4056/sigs.2194987; RA Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A., RA Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H., RA Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C., RA Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N., RA Goeker M., Woyke T., Klenk H.P., Bryant D.A.; RT "Complete genome sequence of the filamentous gliding predatory bacterium RT Herpetosiphon aurantiacus type strain (114-95(T))."; RL Stand. Genomic Sci. 5:356-370(2011). 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; CP000875; ABX03255.1; -; Genomic_DNA. DR AlphaFoldDB; A9AW17; -. DR SMR; A9AW17; -. DR FunCoup; A9AW17; 44. DR STRING; 316274.Haur_0607; -. DR KEGG; hau:Haur_0607; -. DR eggNOG; COG1228; Bacteria. DR HOGENOM; CLU_041647_0_1_0; -. DR InParanoid; A9AW17; -. DR UniPathway; UPA00379; UER00551. DR Proteomes; UP000000787; 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 CDD; cd01296; Imidazolone-5PH; 1. 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..427 FT /note="Imidazolonepropionase" FT /id="PRO_1000121544" FT BINDING 78 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 80 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 80 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 87 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 150 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 150 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 183 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 255 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 255 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 258 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 330 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 330 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 332 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 334 FT /ligand="N-formimidoyl-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58928" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" FT BINDING 335 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372" SQ SEQUENCE 427 AA; 45338 MW; 27B954844CEBAE2E CRC64; MPHADQLITN IGRLVTGPQA PLRGQQLAQL TAIDQAVVAV QAGNIVALGS QAELSAWTAD QTIDAGGYLA IPGFVDPHTH ACYAGDRAHE FELRIKGASY SELMAAGGGI MSTVHATRAA SKAELVAQTR PRLDQLLAHG TTTVEIKSGY GLDTATELTM LEAIAELAQT HPIGIVPTFM GAHAIPAEYR DNPEAFVDLV VDEMLPAVAA WWQQQTIWQE PLACDIFCEN GAFSVAQSQR ILVKAKALGF RLKLHVDEFE PLGGTPLAVE LGAISVDHLV ATPPEHIAIL ANSETVGVSL PGTPFGLGKS QFSPARSLIE ANGILALATD CNPGTSPCES MPMAIAIACR YLRLTPAEAL NAATVNSAFA IRQHERVGSL AVGMQADLAL LNLPDERHIG YKFGTNPVAI VIKTGRVVRR NQLHADR //