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 16-SEP-2015, entry version 59. 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=AHA_0377; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / OS JCM 1027 / KCTC 2358 / NCIMB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240; 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 {ECO:0000255|HAMAP-Rule:MF_00372}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00372}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|HAMAP-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 HutI family. {ECO:0000255|HAMAP- CC 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 ProteinModelPortal; A0KF84; -. DR STRING; 380703.AHA_0377; -. DR MEROPS; M38.980; -. DR EnsemblBacteria; ABK39901; ABK39901; AHA_0377. DR GeneID; 4486961; -. DR KEGG; aha:AHA_0377; -. DR PATRIC; 20778238; VBIAerHyd135212_0364. DR eggNOG; COG1228; -. DR HOGENOM; HOG000218461; -. DR KO; K01468; -. DR OrthoDB; EOG63C0XD; -. DR BioCyc; AHYD380703:GH2M-378-MONOMER; -. 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-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. 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; 2.30.40.10; -; 2. DR HAMAP; MF_00372; HutI; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR005920; HutI. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; SSF51338; 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; Reference proteome; 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. {ECO:0000255|HAMAP- FT Rule:MF_00372}. FT BINDING 147 147 Substrate. FT BINDING 180 180 Substrate. FT BINDING 248 248 Substrate. FT STRAND 9 18 {ECO:0000244|PDB:2Q09}. FT STRAND 31 38 {ECO:0000244|PDB:2Q09}. FT STRAND 41 47 {ECO:0000244|PDB:2Q09}. FT HELIX 48 50 {ECO:0000244|PDB:2Q09}. FT STRAND 59 61 {ECO:0000244|PDB:2Q09}. FT STRAND 66 69 {ECO:0000244|PDB:2Q09}. FT STRAND 71 76 {ECO:0000244|PDB:2Q09}. FT HELIX 85 92 {ECO:0000244|PDB:2Q09}. FT HELIX 97 102 {ECO:0000244|PDB:2Q09}. FT HELIX 107 116 {ECO:0000244|PDB:2Q09}. FT HELIX 119 135 {ECO:0000244|PDB:2Q09}. FT STRAND 138 144 {ECO:0000244|PDB:2Q09}. FT HELIX 151 167 {ECO:0000244|PDB:2Q09}. FT STRAND 168 179 {ECO:0000244|PDB:2Q09}. FT HELIX 184 186 {ECO:0000244|PDB:2Q09}. FT HELIX 190 199 {ECO:0000244|PDB:2Q09}. FT HELIX 201 207 {ECO:0000244|PDB:2Q09}. FT STRAND 212 219 {ECO:0000244|PDB:2Q09}. FT HELIX 225 237 {ECO:0000244|PDB:2Q09}. FT STRAND 241 249 {ECO:0000244|PDB:2Q09}. FT HELIX 254 260 {ECO:0000244|PDB:2Q09}. FT STRAND 264 268 {ECO:0000244|PDB:2Q09}. FT HELIX 274 283 {ECO:0000244|PDB:2Q09}. FT STRAND 286 289 {ECO:0000244|PDB:2Q09}. FT HELIX 291 296 {ECO:0000244|PDB:2Q09}. FT HELIX 305 310 {ECO:0000244|PDB:2Q09}. FT STRAND 315 317 {ECO:0000244|PDB:2Q09}. FT TURN 323 325 {ECO:0000244|PDB:2Q09}. FT HELIX 331 342 {ECO:0000244|PDB:2Q09}. FT HELIX 346 352 {ECO:0000244|PDB:2Q09}. FT HELIX 355 360 {ECO:0000244|PDB:2Q09}. FT TURN 364 366 {ECO:0000244|PDB:2Q09}. FT STRAND 367 369 {ECO:0000244|PDB:2Q09}. FT STRAND 378 384 {ECO:0000244|PDB:2Q09}. FT HELIX 388 391 {ECO:0000244|PDB:2Q09}. FT STRAND 398 403 {ECO:0000244|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 //