ID   HUTI_BURCM              Reviewed;         407 AA.
AC   Q0BDL0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
DE   RecName: Full=Imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Imidazolone-5-propionate hydrolase;
GN   Name=hutI; OrderedLocusNames=Bamb_2207;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia
OS   cepacia (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
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., Pitluck S., Bruce D.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Parke J., Coenye T.,
RA   Konstantinidis K., Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-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.
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DR   EMBL; CP000440; ABI87763.1; -; Genomic_DNA.
DR   RefSeq; YP_774097.1; -.
DR   GeneID; 4310113; -.
DR   GenomeReviews; CP000440_GR; Bamb_2207.
DR   KEGG; bam:Bamb_2207; -.
DR   NMPDR; fig|339670.3.peg.3800; -.
DR   OMA; Q0BDL0; MNMACTL.
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    407       Imidazolonepropionase.
FT                                /FTId=PRO_0000306448.
FT   METAL        68     68       Zinc or iron (By similarity).
FT   METAL        70     70       Zinc or iron (By similarity).
FT   METAL       238    238       Zinc or iron (By similarity).
FT   METAL       313    313       Zinc or iron (By similarity).
FT   BINDING      77     77       Substrate (By similarity).
FT   BINDING      90     90       Substrate (By similarity).
FT   BINDING     140    140       Substrate (By similarity).
FT   BINDING     173    173       Substrate (By similarity).
FT   BINDING     241    241       Substrate (By similarity).
SQ   SEQUENCE   407 AA;  44170 MW;  2013728D15262FDA CRC64;
     MKPTVWHHLR LCPHGHPDET LDDAAIAVDE TGTIVWLGAF SALPHGYAHW QREDLHGAWV
     TPGLVDCHTH LVYGGTRADE FAQRLAGVSY EEIARQGGGI VSTVRATRAA DETTLFVQAA
     ARLQPLLAEG VSAIEIKSGY GLDLASERKM LRVARQLGER FPVSVYTTFL GAHALPPEYA
     GRADEYIDEV CERMLPTLAD EGLVDAVDVF CERIGFSLAQ TERVFEAATR RGLPVKLHAE
     QLSNAGGTAL AARYRALSAD HLEFLDEAGI EAMKAAGTVA VLLPGAYYFI RETQLPPIEL
     LRKHGVPIAL ATDHNPGTSP LESLLLTLNM GCTLFRMTVP EVLQGVTRHA AAALGRADRH
     GALEIGRQAD FAVWSVGSLA ELAYWIGRPL CEQVVRGGAT VFRRMNG
//