ID   HUTI_COLP3              Reviewed;         418 AA.
AC   Q487V5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, 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=CPS_0911;
OS   Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS   psychroerythus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=167879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA   Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA   Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA   Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA   Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA   Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT   "The psychrophilic lifestyle as revealed by the genome sequence of
RT   Colwellia psychrerythraea 34H through genomic and proteomic
RT   analyses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ25600.1; -; Genomic_DNA.
DR   RefSeq; YP_267660.1; -.
DR   GeneID; 3519842; -.
DR   GenomeReviews; CP000083_GR; CPS_0911.
DR   KEGG; cps:CPS_0911; -.
DR   NMPDR; fig|167879.3.peg.878; -.
DR   TIGR; CPS_0911; -.
DR   HOGENOM; Q487V5; -.
DR   OMA; Q487V5; MNMACTL.
DR   BioCyc; CPSY167879:CPS_0911-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    418       Imidazolonepropionase.
FT                                /FTId=PRO_0000306458.
FT   METAL        79     79       Zinc or iron (By similarity).
FT   METAL        81     81       Zinc or iron (By similarity).
FT   METAL       249    249       Zinc or iron (By similarity).
FT   METAL       324    324       Zinc or iron (By similarity).
FT   BINDING      88     88       Substrate (By similarity).
FT   BINDING     101    101       Substrate (By similarity).
FT   BINDING     151    151       Substrate (By similarity).
FT   BINDING     184    184       Substrate (By similarity).
FT   BINDING     252    252       Substrate (By similarity).
SQ   SEQUENCE   418 AA;  45332 MW;  F56F59940883B432 CRC64;
     MTLFKHWQTL YINVNLATMT DGSESYGEIS QGALAISAGK IAWLGKESDL PEHFSVTDED
     IEVIDCKGQW LTPGLIDCHT HLVYGGNRAN EFEMRLQGKS YQEIANAGGG IVSTVTATRR
     ASEQELLASA LPRLTALHQQ GVTTVEIKSG YGLDTINEIK MLKVAGLLAD ELPVTIKRTF
     LGAHALPIEY KDNAEGYLDV VCEEMLPQVV SENLADAVDV FCEGIGFSLA QTKRVFDAAQ
     SHDLPIKVHA EQLSNLGASE LAANYNALSS DHIEFLDEAG IKAMKKSGMT AVLLPGAFYF
     LRETQLPPIE LLRKHQVPMA VATDANPGTS PIHNIHLMLN MACTLFRLTP SEALAGITCY
     GAKALGLSES KGQLAVGYDA DIALWNINQP AELCYQFGVN PLSRLIQNGQ QVLMNESA
//