ID   HUTI_HYPNA              Reviewed;         406 AA.
AC   Q0BZK3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-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=HNE_2395;
OS   Hyphomonas neptunium (strain ATCC 15444).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Hyphomonadaceae; Hyphomonas.
OX   NCBI_TaxID=228405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980487; DOI=10.1128/JB.00111-06;
RA   Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T.,
RA   Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E.,
RA   Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A.,
RA   Rosovitz M.J., Madupu R., Brinkac L.M., Durkin A.S., Daugherty S.C.,
RA   Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D.,
RA   Davidsen T.M., Yang Q., Zafar N., Ward N.L.;
RT   "Comparative genomic evidence for a close relationship between the
RT   dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT   crescentus.";
RL   J. Bacteriol. 188:6841-6850(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   -!- 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; CP000158; ABI76937.1; -; Genomic_DNA.
DR   RefSeq; YP_761090.1; -.
DR   GeneID; 4289897; -.
DR   GenomeReviews; CP000158_GR; HNE_2395.
DR   KEGG; hne:HNE_2395; -.
DR   NMPDR; fig|228405.5.peg.2309; -.
DR   TIGR; HNE_2395; -.
DR   HOGENOM; Q0BZK3; -.
DR   OMA; Q0BZK3; MNMACTL.
DR   BioCyc; HNEP81032:HNE_2395-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    406       Imidazolonepropionase.
FT                                /FTId=PRO_0000306466.
FT   METAL        75     75       Zinc or iron (By similarity).
FT   METAL        77     77       Zinc or iron (By similarity).
FT   METAL       245    245       Zinc or iron (By similarity).
FT   METAL       320    320       Zinc or iron (By similarity).
FT   BINDING      84     84       Substrate (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
FT   BINDING     147    147       Substrate (By similarity).
FT   BINDING     180    180       Substrate (By similarity).
FT   BINDING     248    248       Substrate (By similarity).
SQ   SEQUENCE   406 AA;  43060 MW;  7A65FA6FEF7D3823 CRC64;
     MQKKRIWTNA RLATMAAGLP GLGIVEDGLI AAEGDRITFA GLASDFPYTE GPSTQGYEVT
     DCGGRWILPG LIDCHTHLVW AGSRADEFER RLAGASYEEI ARSGGGIRST VSAVRAASEA
     ELVAESLPRL NALIGEGVTT IEIKSGYGLN IEDELKQLRA ARALGEVRPI DVETTLLAAH
     TLPPEYEGRA DAYIDLVCNE IIPAAAQAGL ASAVDAFCET IGFTPEQTGR VLSAARHHGL
     AVKLHADQLS NLQGGALAAR HNALSADHLE YLDEAGIAAM AQAGMVAVML PGAYYVLRET
     HPPPLEGLRR AGVSLAISTD CNPGTSPLTS ILLAMNMGAT LFRMTVEECL LGTTRHAARA
     LGLEKATGTL EAGKLCNLSI WDIDRPAELV NAMGLNPLHT RVWRGQ
//