ID HUTI_NOCFA Reviewed; 392 AA. AC Q5Z0G2; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 16-JUN-2009, entry version 32. DE RecName: Full=Imidazolonepropionase; DE EC=3.5.2.7; DE AltName: Full=Imidazolone-5-propionate hydrolase; GN Name=hutI; OrderedLocusNames=NFA_12340; OS Nocardia farcinica. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Nocardiaceae; Nocardia. OX NCBI_TaxID=37329; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 10152; RX PubMed=15466710; DOI=10.1073/pnas.0406410101; RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., RA Shiba T., Hattori M.; RT "The complete genomic sequence of Nocardia farcinica IFM 10152."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004). 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; AP006618; BAD56079.1; -; Genomic_DNA. DR RefSeq; YP_117443.1; -. DR GeneID; 3109583; -. DR GenomeReviews; AP006618_GR; NFA_12340. DR KEGG; nfa:nfa12340; -. DR NMPDR; fig|247156.1.peg.1265; -. DR HOGENOM; Q5Z0G2; -. DR OMA; Q5Z0G2; MNMACTL. DR BioCyc; NFAR247156:NFA12340-MON; -. DR BRENDA; 3.5.2.7; 290697. 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; 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 1 392 Imidazolonepropionase. FT /FTId=PRO_0000306475. FT METAL 70 70 Zinc or iron (By similarity). FT METAL 72 72 Zinc or iron (By similarity). FT METAL 227 227 Zinc or iron (By similarity). FT METAL 301 301 Zinc or iron (By similarity). FT BINDING 79 79 Substrate (By similarity). FT BINDING 92 92 Substrate (By similarity). FT BINDING 137 137 Substrate (By similarity). FT BINDING 164 164 Substrate (By similarity). FT BINDING 230 230 Substrate (By similarity). SQ SEQUENCE 392 AA; 41273 MW; D3B6F77810B9482C CRC64; MPTTALTGIG QLVTNDPALG EGPLGLRRDA AIVFEDGVVA WVGDSAHVPA TDTAHDLDGR AVLPGFVESH SHLVFAGDRA EEFAARMSGR PYGAGGIRTT IEATRAATDE QLGANVRRLL DESLRAGSTT VECKSGYGQS VEHELRSVRV AGRYTDEVTL LAAHVPPPEY AGRVDDYVAM ACAEMIPRCA PHAKWIDVFC EQGAFDRDQA HAVLTAGIAH GLVPRVHGNQ LHRGPGVQLA VEVGAASVDH VTYIDDADIE ALAHSDTVAT LLPGADFCTR NSYPDARALL DAGVTVALGA DCNPGTSYTT SLPFCIALAV RELRMTPDEA VWAATAGGAR ALRRGDVGVL TPGARADALA LDAPSHLHLA YRPGVPLISR VWREGTLAYA TN //