ID   HUTI_CAUSK              Reviewed;         401 AA.
AC   B0SYU7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   16-JUN-2009, entry version 10.
DE   RecName: Full=Imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Imidazolone-5-propionate hydrolase;
GN   Name=hutI; OrderedLocusNames=Caul_1298;
OS   Caulobacter sp. (strain K31).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=366602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S.,
RA   Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stephens C., Richardson P.;
RT   "Complete sequence of chromosome of Caulobacter sp. K31.";
RL   Submitted (JAN-2008) 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; CP000927; ABZ70428.1; -; Genomic_DNA.
DR   RefSeq; YP_001682926.1; -.
DR   GeneID; 5898753; -.
DR   GenomeReviews; CP000927_GR; Caul_1298.
DR   KEGG; cak:Caul_1298; -.
DR   OMA; B0SYU7; 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   TIGRFAMs; TIGR01224; hutI; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Histidine metabolism; Hydrolase; Iron;
KW   Metal-binding; Zinc.
FT   CHAIN         1    401       Imidazolonepropionase.
FT                                /FTId=PRO_1000079821.
FT   METAL        70     70       Zinc or iron (By similarity).
FT   METAL        72     72       Zinc or iron (By similarity).
FT   METAL       240    240       Zinc or iron (By similarity).
FT   METAL       315    315       Zinc or iron (By similarity).
FT   BINDING      79     79       Substrate (By similarity).
FT   BINDING      92     92       Substrate (By similarity).
FT   BINDING     142    142       Substrate (By similarity).
FT   BINDING     175    175       Substrate (By similarity).
FT   BINDING     243    243       Substrate (By similarity).
SQ   SEQUENCE   401 AA;  42469 MW;  FEFFCF6033706BB3 CRC64;
     MRCDRVWSKA RLATFAAGRP GIGVVEDGVV ASLSGRIVYA GPATEAPAFE ALETLDCEGR
     WITPGLIDPH THLVFGGDRA REFELRLAGA TYEEIARAGG GIVSTMKATR AASEGELVAS
     ALPRLDALIA EGLTTIEIKS GYGLSLDDEL KSLRAARALA DVRKVSVTTT FLGAHALPPE
     YEGDPDGYID HVCYQMIPAV AAEGLADAVD AFCEGIGFSR AQTRRVFQAA RERGLPVKLH
     AEQLSNLDGA ALAAEFGALS ADHLEHLDGA GIAAMAQAGT TAVLLPGAFY FVRETRLPPI
     QALRAAGVPL ALATDCNPGT SPLTSLLLTL NMAATLFRMT VDECLAGVTR EAARAIGRLD
     HIGTLEAGKS CDLAIWDIER PAQLVYRMGF NPLHARVWKG L
//