ID HUTI_AERHH Reviewed; 411 AA. AC A0KF84; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 03-MAY-2023, entry version 102. 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}; OrderedLocusNames=AHA_0377; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC RC 2358 / NCIMB 9240 / NCTC 8049; RX PubMed=16980456; DOI=10.1128/jb.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."; RL J. Bacteriol. 188:8272-8282(2006). RN [2] {ECO:0007744|PDB:2OOF} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 6-411 IN COMPLEX WITH IRON IONS. RA Tyagi R., Eswaramoorthy S., Burley S.K., Swaminathan S.; RT "The crystal structure of 4-imidazolone-5-propanoate amidohydrolase from RT environmental sample."; RL Submitted (JAN-2007) to the PDB data bank. RN [3] {ECO:0007744|PDB:2Q09} RP X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 6-411 IN COMPLEX WITH IRON IONS RP AND SUBSTRATE ANALOG 3-(2,5-DIOXO-IMIDAZOLIDIN-4-YL)-PROPANOATE. RX PubMed=18442260; DOI=10.1021/bi800180g; RA Tyagi R., Eswaramoorthy S., Burley S.K., Raushel F.M., Swaminathan S.; RT "A common catalytic mechanism for proteins of the HutI family."; RL Biochemistry 47:5608-5615(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; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00372}; CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; CC Evidence={ECO:0000305|PubMed:18442260, ECO:0000305|Ref.2}; 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 -!- SEQUENCE CAUTION: CC Sequence=ABK39901.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; CP000462; ABK39901.1; ALT_INIT; Genomic_DNA. DR RefSeq; YP_854906.1; NC_008570.1. DR PDB; 2OOF; X-ray; 2.20 A; A=6-411. DR PDB; 2Q09; X-ray; 1.97 A; A=6-411. DR PDBsum; 2OOF; -. DR PDBsum; 2Q09; -. DR AlphaFoldDB; A0KF84; -. DR SMR; A0KF84; -. DR STRING; 380703.AHA_0377; -. DR EnsemblBacteria; ABK39901; ABK39901; AHA_0377. DR KEGG; aha:AHA_0377; -. DR PATRIC; fig|380703.7.peg.364; -. DR eggNOG; COG1228; Bacteria. DR HOGENOM; CLU_041647_0_0_6; -. DR OrthoDB; 9776455at2; -. DR UniPathway; UPA00379; UER00551. DR EvolutionaryTrace; A0KF84; -. DR Proteomes; UP000000756; 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 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 TIGRFAMs; TIGR01224; hutI; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Histidine metabolism; Hydrolase; Iron; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1..411 FT /note="Imidazolonepropionase" FT /id="PRO_0000306422" FT BINDING 75 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000269|PubMed:18442260, FT ECO:0007744|PDB:2OOF, ECO:0007744|PDB:2Q09" 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:0000269|PubMed:18442260, FT ECO:0007744|PDB:2OOF, ECO:0007744|PDB:2Q09" 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:0000305|PubMed:18442260, FT ECO:0007744|PDB:2Q09" FT BINDING 147 FT /ligand="4-imidazolone-5-propanoate" FT /ligand_id="ChEBI:CHEBI:77893" FT /evidence="ECO:0000305|PubMed:18442260, FT ECO:0007744|PDB:2Q09" 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:0000305|PubMed:18442260, FT ECO:0007744|PDB:2Q09" FT BINDING 245 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000269|PubMed:18442260, FT ECO:0007744|PDB:2OOF, ECO:0007744|PDB:2Q09" 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:0000305|PubMed:18442260, FT ECO:0007744|PDB:2Q09" FT BINDING 320 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /evidence="ECO:0000269|PubMed:18442260, FT ECO:0007744|PDB:2OOF, ECO:0007744|PDB:2Q09" 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:0000305|PubMed:18442260, FT ECO:0007744|PDB:2Q09" FT STRAND 9..18 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 31..38 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 41..47 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 71..76 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 85..92 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 97..102 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 119..135 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 138..144 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 151..167 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 168..179 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 190..199 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 201..207 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 212..219 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 225..237 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 241..249 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 254..260 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 264..268 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 274..283 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 286..289 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 291..296 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 305..310 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 315..317 FT /evidence="ECO:0007829|PDB:2Q09" FT TURN 323..325 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 331..342 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 346..352 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 355..360 FT /evidence="ECO:0007829|PDB:2Q09" FT TURN 364..366 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 378..384 FT /evidence="ECO:0007829|PDB:2Q09" FT HELIX 388..391 FT /evidence="ECO:0007829|PDB:2Q09" FT STRAND 398..403 FT /evidence="ECO:0007829|PDB:2Q09" SQ SEQUENCE 411 AA; 44543 MW; 63D38DB562DC8EBF CRC64; MNKELLNCER VWLNVTPATL RSDLADYGLL EPHALGVHEG RIHALVPMQD LKGPYPAHWQ DMKGKLVTPG LIDCHTHLIF AGSRAEEFEL RQKGVPYAEI ARKGGGIIST VRATRAACEE QLFELALPRV KSLIREGVTT VEIKSGYGLT LEDELKMLRV ARRLGEALPI RVKTTLLAAH AVPPEYRDDP DSWVETICQE IIPAAAEAGL ADAVDVFCEH IGFSLAQTEQ VYLAADQYGL AVKGHMDQLS NLGGSTLAAN FGALSVDHLE YLDPEGIQAL AHRGVVATLL PTAFYFLKET KLPPVAALRK AGVPMAVSSD INPGTAPIVS LRMAMNMACT LFGLTPVEAM AGVTRHAARA LGEQEQLGQL RVGMLADFLV WNCGHPAELS YLIGVDQLVS RVINGEETLH G //