ID   HUTI_POLSJ              Reviewed;         425 AA.
AC   Q12EQ4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Imidazolone-5-propionate hydrolase;
GN   Name=hutI; OrderedLocusNames=Bpro_1035;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591;
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., Brettin T., Bruce D., Han C., Tapia R., Munk A.C.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I., Richardson P.;
RT   "Complete sequence of chromosome of Polaromonas sp. JS666.";
RL   Submitted (APR-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; CP000316; ABE42988.1; -; Genomic_DNA.
DR   RefSeq; YP_547886.1; -.
DR   GeneID; 4012156; -.
DR   GenomeReviews; CP000316_GR; Bpro_1035.
DR   KEGG; pol:Bpro_1035; -.
DR   NMPDR; fig|296591.1.peg.3371; -.
DR   HOGENOM; Q12EQ4; -.
DR   OMA; Q12EQ4; MNMACTL.
DR   BioCyc; PSP296591:BPRO_1035-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; IPR013108; Amidohydro_3.
DR   InterPro; IPR005920; HutI.
DR   Pfam; PF07969; Amidohydro_3; 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    425       Imidazolonepropionase.
FT                                /FTId=PRO_0000306481.
FT   METAL        78     78       Zinc or iron (By similarity).
FT   METAL        80     80       Zinc or iron (By similarity).
FT   METAL       248    248       Zinc or iron (By similarity).
FT   METAL       323    323       Zinc or iron (By similarity).
FT   BINDING      87     87       Substrate (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     150    150       Substrate (By similarity).
FT   BINDING     183    183       Substrate (By similarity).
FT   BINDING     251    251       Substrate (By similarity).
SQ   SEQUENCE   425 AA;  44819 MW;  1D52F947C74FA752 CRC64;
     MTTAPHPAAD GIWEHLRLMP GALADDSPVA TNTEAAIVVT EGRIRWIGAS AALPAGFSAL
     PRFDGGGALV TPGLVDCHTH LVYGGQRANE FAMRLAGASY EEVAKAGGGI VSSVRATRAA
     GEDELFAQAA PRLEQLLADG VCAIEIKSGY GLALEHERKQ LRVARRLGEA YGVTVRTTFL
     GAHALPPEYA GRSQDYIDLV CREMLPALAA EGLVDAVDVF CERIAFSLSE TEQVFQAAQR
     LGLPVKLHAE QLSDMGGAAL AARYGALSCD HIEHLSQAGI DAMRAAGTVA VLLPGAYYTL
     RDTHLPPIAA LREAGVPMAV STDHNPGTSP ALSLLLMANM ACTLFRLTVP EALAGITRHA
     ARALGLQDTH GALGVGRPAN FVLWQLNDSA ELAYWLGQQA PRTIVRQGRV ALDGLQIAPN
     ARITP
//