ID   HUTI_BURTA              Reviewed;         407 AA.
AC   Q2SXJ3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-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=BTH_I1824;
OS   Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 /
OS   CIP 106301).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R.,
RA   Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D.,
RA   Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P.,
RA   Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F.,
RA   Roberts K., Hatch B., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) 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; CP000086; ABC38786.1; -; Genomic_DNA.
DR   RefSeq; YP_442356.1; -.
DR   GeneID; 3849678; -.
DR   GenomeReviews; CP000086_GR; BTH_I1824.
DR   KEGG; bte:BTH_I1824; -.
DR   TIGR; BTH_I1824; -.
DR   HOGENOM; Q2SXJ3; -.
DR   OMA; Q2SXJ3; MNMACTL.
DR   BioCyc; BTHA271848:BTH_I1824-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; 1.
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_0000306454.
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;  43715 MW;  D3D5C541E99057CC CRC64;
     MKSTLWHNLK LCAHGDPNDT IADAAIAVNG DGTIAWTGRA SDVPAGYVHW PREDLRGAWV
     TPGLVDCHTH LVYGGQRADE FAQRLAGVSY EEIARRGGGI VSTVRATRDA SEATLFEQAA
     ARLRPLLAEG VTAIEIKSGY GLELASERRM LRVARQLGER FPVSVYTTFL GAHALPPEYA
     GRADEYVDEV CERMLPALAD EGLVDAVDVF CERIGFTLAQ SERVFEAAAR RGLPVKMHAE
     QLSGGGGAAL AARYRALSAD HLEYLDEAGV AAMRASGTTA VLLPGAYYFI RETKQPPIDL
     LRRHGVPIAL ATDHNPGTSP LTSLLLTMNM GCTLFKLTVQ EALLGVTRHA AAALGAGDRH
     GSLAPGRQAD FAVWSAATLA ELAYWFGRPL CERVVKGGVT VFARDAR
//