ID   HUTI_ARTAT              Reviewed;         409 AA.
AC   A1R4S6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
DE   RecName: Full=Imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Imidazolone-5-propionate hydrolase;
GN   Name=hutI; OrderedLocusNames=AAur_1464;
OS   Arthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of
RT   Arthrobacter aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM06836.1; -; Genomic_DNA.
DR   RefSeq; YP_947238.1; -.
DR   GeneID; 4638746; -.
DR   GenomeReviews; CP000474_GR; AAur_1464.
DR   KEGG; aau:AAur_1464; -.
DR   TIGR; AAur_1464; -.
DR   OMA; A1R4S6; 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; 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    409       Imidazolonepropionase.
FT                                /FTId=PRO_0000306425.
FT   METAL        70     70       Zinc or iron (By similarity).
FT   METAL        72     72       Zinc or iron (By similarity).
FT   METAL       225    225       Zinc or iron (By similarity).
FT   METAL       312    312       Zinc or iron (By similarity).
FT   BINDING      79     79       Substrate (By similarity).
FT   BINDING      92     92       Substrate (By similarity).
FT   BINDING     137    137       Substrate (By similarity).
FT   BINDING     164    164       Substrate (By similarity).
FT   BINDING     228    228       Substrate (By similarity).
SQ   SEQUENCE   409 AA;  42887 MW;  0E5E2C6F86B6216F CRC64;
     MSATNSASTL ITNIGELMTQ DMEHRVLKDA AIVIEGERIA WLGSTKDAPA ADENIDAQGR
     AVLPGWVDSH SHLVFAGDRT AEFEARMAGE SYSAGGIAVT TGATRSVSDD ELTRLVRDRV
     AEAVSQGTTY LESKTGYGLD VENEARSARI AAAEVDEVTY LGAHLVPDGS DPEEYTDLVC
     GPMLDAVLPH VRWADVFCER GAFTEDQSRR VLRAARDAGL GLRVHGNQLG EGPGVALAVE
     FAAASVDHVN YLSDKDVLAL AGTWAGWDPA TGAGTKGTVA TCLPACDLST RQPLAPGREL
     IDAGVQIALA ANCNPGTSYT SSMAFCVTTA VLQMHLSVHE AVRAATYGGA LALGRESGND
     VDGERAVGSL AVGHRADLHM LKAPSATHLA YRPGIPLTGS VWRAGVRVV
//