ID   HUTI_MESSB              Reviewed;         417 AA.
AC   Q11E17;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Imidazolone-5-propionate hydrolase;
GN   Name=hutI; OrderedLocusNames=Meso_2986;
OS   Mesorhizobium sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG64358.1; -; Genomic_DNA.
DR   RefSeq; YP_675523.1; -.
DR   SMR; Q11E17; 14-416.
DR   GeneID; 4181422; -.
DR   GenomeReviews; CP000390_GR; Meso_2986.
DR   KEGG; mes:Meso_2986; -.
DR   NMPDR; fig|266779.1.peg.1514; -.
DR   HOGENOM; Q11E17; -.
DR   OMA; Q11E17; MNMACTL.
DR   BioCyc; MSP266779:MESO_2986-MON; -.
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    417       Imidazolonepropionase.
FT                                /FTId=PRO_0000306473.
FT   METAL        83     83       Zinc or iron (By similarity).
FT   METAL        85     85       Zinc or iron (By similarity).
FT   METAL       253    253       Zinc or iron (By similarity).
FT   METAL       328    328       Zinc or iron (By similarity).
FT   BINDING      92     92       Substrate (By similarity).
FT   BINDING     105    105       Substrate (By similarity).
FT   BINDING     155    155       Substrate (By similarity).
FT   BINDING     188    188       Substrate (By similarity).
FT   BINDING     256    256       Substrate (By similarity).
SQ   SEQUENCE   417 AA;  44374 MW;  D1324AD0C3186A5F CRC64;
     MTRNNFSGAA AHSARSIWRN GRLATLREDL QGLGIVENGA VVCEGGRILF AGPEGELPAE
     LIENTEITDL EGRWVTPGLV DCHTHIVYGG NRAREFEMRL QGATYEEIAR AGGGIVSSVK
     ATNALSVEGL VEAALPRLDT LISEGVTTVE IKSGYGLNIE AELKMLCAAR ALEQIRPVRV
     VTSYLGAHAT PVEYKGRNGD YISEVVLPGL ERAHAEGLVD AVDGFCEGIA FSVDEIRRVF
     DKARSLGIPV KLHAEQLSNL GGAKLAASYG ALSADHLEYL DEDGARAMAA AGTVAVLLPG
     AFYAINEKQK PPVEALRQAG VHIAIATDSN PGTSPLTSLL LTMNMSATLF RLTVEECIAG
     ATREGARALG LLAETGTIEA GKSADLAIWN IESPAELVYR IGFNPLHAHI FKGRRID
//