ID   HUTI_MARMM              Reviewed;         402 AA.
AC   Q0AP91;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Imidazolone-5-propionate hydrolase;
GN   Name=hutI; OrderedLocusNames=Mmar10_1604;
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Maricaulis.
OX   NCBI_TaxID=394221;
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Viollier P., Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
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; CP000449; ABI65896.1; -; Genomic_DNA.
DR   RefSeq; YP_756834.1; -.
DR   GeneID; 4283926; -.
DR   GenomeReviews; CP000449_GR; Mmar10_1604.
DR   KEGG; mmr:Mmar10_1604; -.
DR   NMPDR; fig|394221.5.peg.1567; -.
DR   HOGENOM; Q0AP91; -.
DR   OMA; Q0AP91; 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    402       Imidazolonepropionase.
FT                                /FTId=PRO_0000306472.
FT   METAL        69     69       Zinc or iron (By similarity).
FT   METAL        71     71       Zinc or iron (By similarity).
FT   METAL       239    239       Zinc or iron (By similarity).
FT   METAL       314    314       Zinc or iron (By similarity).
FT   BINDING      78     78       Substrate (By similarity).
FT   BINDING      91     91       Substrate (By similarity).
FT   BINDING     141    141       Substrate (By similarity).
FT   BINDING     174    174       Substrate (By similarity).
FT   BINDING     242    242       Substrate (By similarity).
SQ   SEQUENCE   402 AA;  42417 MW;  7EFC49E6950AA33D CRC64;
     MQFDRLLTEA RLATMVAGDD GYGVIEKAAL GIKDGRIAWI GPMSEIPGEA RETERLASRW
     VTPALIDCHT HLVFAGDRSD EFERRLGGES YESISRSGGG IARSVEATRA AGAAELAAGA
     LTRIDALAQE GVGTVEIKSG YGLTRESERT MLRAARGVER ASGMRVSATL LAAHAVPPEY
     KGESGRYIDE ICIPLIREAA REGLADAVDA YCEGIGFSPE ETRRLFIAAK AAGLPVKLHA
     DQLSDTGGAR LVAEFGGLSA DHIEYTNAEG IAAMAKAGTV GVLLPGAFYA LNETKKPPVE
     AMRAAGVDMA VATDANPGTS PLVSLLTAAN MACILFGLTL PEAFAGMTRN AARALGLHGE
     IGTLEVGKAA DLAIWDVERP AEIIQWIGRR PLHGRILAGE WQ
//