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 13-NOV-2007, entry version 10. DE Imidazolonepropionase (EC 3.5.2.7) (Imidazolone-5-propionate DE hydrolase). GN Name=hutI; OrderedLocusNames=AHA_0377; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16980456; DOI=10.1128/JB.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., RA Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., RA Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all RT trades."; RL J. Bacteriol. 188:8272-8282(2006). CC -!- CATALYTIC ACTIVITY: (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4- CC yl)propanoate + H(2)O = N-formimidoyl-L-glutamate + H(+). CC -!- COFACTOR: Binds 1 zinc or iron ion per subunit (By similarity). CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L- CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SIMILARITY: Belongs to the hutI family. 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; -. DR PDB; 2OOF; X-ray; 2.20 A; A=6-411. DR PDB; 2Q09; X-ray; 1.97 A; A=6-411. DR SMR; A0KF84; 29-433. DR GeneID; 4486961; -. DR GenomeReviews; CP000462_GR; AHA_0377. DR KEGG; aha:AHA_0377; -. DR TIGR; AHA_0377; -. DR GO; GO:0050480; F:imidazolonepropionase activity; IEA:EC. DR HAMAP; MF_00372; -; 1. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR011550; Amidohydro_like. DR InterPro; IPR005920; HutI. DR Pfam; PF01979; Amidohydro_1; 1. DR ProDom; PD001248; Amidohydro_like; 1. DR TIGRFAMs; TIGR01224; hutI; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Histidine metabolism; KW Hydrolase; Iron; Metal-binding; Zinc. FT CHAIN 1 411 Imidazolonepropionase. FT /FTId=PRO_0000306422. FT METAL 75 75 Zinc or iron (By similarity). FT METAL 77 77 Zinc or iron (By similarity). FT METAL 245 245 Zinc or iron (By similarity). FT METAL 320 320 Zinc or iron (By similarity). FT BINDING 84 84 Substrate (By similarity). FT BINDING 97 97 Substrate (By similarity). FT BINDING 147 147 Substrate (By similarity). FT BINDING 180 180 Substrate (By similarity). FT BINDING 248 248 Substrate (By similarity). 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 //