ID   HUTI_ANADE              Reviewed;         421 AA.
AC   Q2IHZ6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-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=Adeh_1507;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-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   -!- 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; CP000251; ABC81280.1; -; Genomic_DNA.
DR   RefSeq; YP_464717.1; -.
DR   GeneID; 3887917; -.
DR   GenomeReviews; CP000251_GR; Adeh_1507.
DR   KEGG; ade:Adeh_1507; -.
DR   HOGENOM; Q2IHZ6; -.
DR   OMA; Q2IHZ6; MNMACTL.
DR   BioCyc; ADEH290397:ADEH_1507-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   TIGRFAMs; TIGR01224; hutI; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Histidine metabolism; Hydrolase; Iron;
KW   Metal-binding; Zinc.
FT   CHAIN         1    421       Imidazolonepropionase.
FT                                /FTId=PRO_0000306424.
FT   METAL        76     76       Zinc or iron (By similarity).
FT   METAL        78     78       Zinc or iron (By similarity).
FT   METAL       247    247       Zinc or iron (By similarity).
FT   METAL       322    322       Zinc or iron (By similarity).
FT   BINDING      85     85       Substrate (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     148    148       Substrate (By similarity).
FT   BINDING     182    182       Substrate (By similarity).
FT   BINDING     250    250       Substrate (By similarity).
SQ   SEQUENCE   421 AA;  43894 MW;  89EA666B75B8992F CRC64;
     MSRPAATLVL RNAVVATCDR GPSDAGLLPG AAVAVEGRRV AWVGRERDVE AEVNLAGAQV
     IDARGGLVTP GLVDSHTHLV FAGERAGEFA LRCAGRTYLQ VALSGGGIAV TTRETRAAPD
     EQLLAAAAAR ARRLIAQGVT TLEVKSGYGL DAPEELRLLR IVHQLGRALG GDATILPTLL
     FHAVPPEQVG DRAGFVRDAC ASLIPQVARE RLAQFCDVFV EDGAFAPDEA RLLLQAAKDR
     GLVPRVHAEQ LTAGGGARLA AELGCSSADH LEELDDAGIA ALAQARVVAG LLPLSTLFLG
     SERYAPARRL LEAGVPVSLA TNMNPGSAMS ENVGLTLSLA CLKLRLTPAE ALVAFTAGGA
     RALRQPDLGR VARGADADLV LWGCGSPEHL AWHMAVNHAL VVVKHGRVVH EAPPAAMVDC
     R
//