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 24-NOV-2009, entry version 20. DE RecName: Full=Imidazolonepropionase; DE EC=3.5.2.7; DE AltName: Full=Imidazolone-5-propionate 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 PDBsum; 2OOF; -. DR PDBsum; 2Q09; -. DR SMR; A0KF84; 29-433. DR STRING; A0KF84; -. DR GeneID; 4486961; -. DR GenomeReviews; CP000462_GR; AHA_0377. DR KEGG; aha:AHA_0377; -. DR TIGR; AHA_0377; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050480; F:imidazolonepropionase activity; IEA:HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0019556; P:histidine catabolic process to glutamate an...; IEA:InterPro. DR HAMAP; MF_00372; -; 1. DR InterPro; IPR006680; Amidohydro_1. DR InterPro; IPR005920; HutI. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR Pfam; PF01979; Amidohydro_1; 2. 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. FT METAL 77 77 Zinc or iron. FT METAL 245 245 Zinc or iron. FT METAL 320 320 Zinc or iron. FT BINDING 84 84 Substrate. FT BINDING 97 97 Substrate (By similarity). FT BINDING 147 147 Substrate. FT BINDING 180 180 Substrate. FT BINDING 248 248 Substrate. FT STRAND 8 18 FT STRAND 31 38 FT STRAND 41 47 FT HELIX 48 50 FT STRAND 57 61 FT STRAND 66 69 FT STRAND 71 76 FT HELIX 85 93 FT HELIX 97 102 FT HELIX 107 116 FT HELIX 119 135 FT STRAND 138 144 FT HELIX 151 167 FT STRAND 170 179 FT HELIX 184 186 FT HELIX 190 199 FT HELIX 201 207 FT STRAND 212 219 FT HELIX 225 237 FT STRAND 241 249 FT HELIX 254 260 FT STRAND 264 268 FT HELIX 274 283 FT STRAND 286 289 FT HELIX 291 296 FT HELIX 305 310 FT STRAND 315 317 FT TURN 323 325 FT HELIX 331 342 FT HELIX 346 352 FT HELIX 355 360 FT TURN 364 366 FT STRAND 367 369 FT STRAND 378 384 FT HELIX 388 391 FT STRAND 392 394 FT STRAND 398 403 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 //