ID   HUTI_HAHCH              Reviewed;         403 AA.
AC   Q2SEP8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Imidazolone-5-propionate hydrolase;
GN   Name=hutI; OrderedLocusNames=HCH_04169;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC30876.1; -; Genomic_DNA.
DR   RefSeq; YP_435301.1; -.
DR   GeneID; 3841617; -.
DR   GenomeReviews; CP000155_GR; HCH_04169.
DR   KEGG; hch:HCH_04169; -.
DR   NMPDR; fig|349521.5.peg.3643; -.
DR   HOGENOM; Q2SEP8; -.
DR   OMA; Q2SEP8; MNMACTL.
DR   BioCyc; HCHE349521:HCH_04169-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    403       Imidazolonepropionase.
FT                                /FTId=PRO_0000306465.
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   403 AA;  43948 MW;  17A95162680EAD0B CRC64;
     MDWWINARIA TLDPDAQHAY GLLESHALGV AHGKVEAIVP MSEWDGDASD NITDANGRLI
     TPGLVDCHTH LVYGGDRAAE FEMRLQGVSY ADIAKQGGGI ISTVRATRAA TEKELLQQSE
     KRLLALLREG VTTVEIKSGY GLDLESELKM LHVARRLGQR YPVNVRTTLL AAHALPPEYA
     GRSDDYISWI CEEALPVAHE QKLADAVDVF CESIAFTPEQ CRRVFEAAQK LGLPVKGHME
     QLTLSGGSAL AAEFNALSVD HVEYLDEASV QAIAASGTVA TLLPGAFYFL RETQRPPMEL
     LRKHKVPMAL ATDLNPGSCP LASMRLMMNM GCTFFGMTPE ETLAGVTRHG AKALGMQDRI
     GHLAPGMAAD FIVWDCQHPA QLSYEFGVTG PHQRVFHGEI HNV
//