ID HUTI_CHRVO Reviewed; 413 AA. AC Q7P192; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 1. DT 16-JUN-2009, entry version 37. DE RecName: Full=Imidazolonepropionase; DE EC=3.5.2.7; DE AltName: Full=Imidazolone-5-propionate hydrolase; GN Name=hutI; OrderedLocusNames=CV_0321; OS Chromobacterium violaceum. OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Chromobacterium. OX NCBI_TaxID=536; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131; RX MEDLINE=22882880; PubMed=14500782; DOI=10.1073/pnas.1832124100; RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., RA Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S., RA Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., RA Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., RA Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., RA Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., RA Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., RA Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., RA Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., RA di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., RA Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., RA Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., RA Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., RA Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., RA Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., RA Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., RA Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., RA Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., RA Vettore A., Wassem R., Zaha A., Simpson A.J.G.; RT "The complete genome sequence of Chromobacterium violaceum reveals RT remarkable and exploitable bacterial adaptability."; RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003). 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 http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE016825; AAQ58000.1; -; Genomic_DNA. DR RefSeq; NP_899991.1; -. DR GeneID; 2550792; -. DR GenomeReviews; AE016825_GR; CV_0321. DR KEGG; cvi:CV_0321; -. DR NMPDR; fig|243365.1.peg.321; -. DR HOGENOM; Q7P192; -. DR OMA; Q7P192; MNMACTL. DR BioCyc; CVIO243365:CV_0321-MON; -. DR BRENDA; 3.5.2.7; 415. 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 Pfam; PF01979; Amidohydro_1; 2. DR ProDom; PD001248; Amidohydro_like; 1. DR TIGRFAMs; TIGR01224; hutI; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Histidine metabolism; Hydrolase; Iron; KW Metal-binding; Zinc. FT CHAIN 1 413 Imidazolonepropionase. FT /FTId=PRO_0000306456. FT METAL 77 77 Zinc or iron (By similarity). FT METAL 79 79 Zinc or iron (By similarity). FT METAL 247 247 Zinc or iron (By similarity). FT METAL 322 322 Zinc or iron (By similarity). FT BINDING 86 86 Substrate (By similarity). FT BINDING 99 99 Substrate (By similarity). FT BINDING 149 149 Substrate (By similarity). FT BINDING 182 182 Substrate (By similarity). FT BINDING 250 250 Substrate (By similarity). SQ SEQUENCE 413 AA; 43634 MW; FA4D8A5F69C02F5F CRC64; MNVPHPHRPS LWLNARLATM DPAHGAPYGA LEGHALLLRD GHIEAVLPQA EADAAAFDGE VFDLQGRWVT PGFVDCHTHL VYGGSRAAEW EKRLTGVPYQ QIAAEGGGIV STVRATRWLD EEELALASLP RLKALMAEGV TTVEIKSGYG LTLADELKQL AAARRLQASL PVEVATTLLA AHAVPPEYAG DADGYVDLVV ESILPVAARA GLAEAVDAFC ESVGFSPAQT RRVFEAARAH GLKVKGHVEQ LSNLHGAELV AEFGGLSADH IEYLDDAGVA ALKRAGTVAV LLPGAFYFLR ETQKPPVDKL RAAGVPMAVS TDLNPGTSPF ASIRLAMNQA CVLFGLTPEE ALAGVTRHAA QALGRGATHG RLAAGCVADL LVWDIAHPAE LAYSVGVPLL KQRVFRGAAQ HID //