(data stored in ACNUC7421 zone)

SWISSPROT: HUTI_PSEPF

ID   HUTI_PSEPF              Reviewed;         401 AA.
AC   Q3KJE5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   RecName: Full=Imidazolonepropionase {ECO:0000255|HAMAP-Rule:MF_00372};
DE            EC=3.5.2.7 {ECO:0000255|HAMAP-Rule:MF_00372};
DE   AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00372};
GN   Name=hutI {ECO:0000255|HAMAP-Rule:MF_00372};
GN   OrderedLocusNames=Pfl01_0367;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-
CC         glutamate; Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58928, ChEBI:CHEBI:77893; EC=3.5.2.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00372};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00372};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00372};
CC       Note=Binds 1 zinc or iron ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00372};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00372}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00372}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. HutI family. {ECO:0000255|HAMAP-Rule:MF_00372}.
DR   EMBL; CP000094; ABA72111.1; -; Genomic_DNA.
DR   RefSeq; WP_011332050.1; NC_007492.2.
DR   SMR; Q3KJE5; -.
DR   STRING; 205922.Pfl01_0367; -.
DR   MEROPS; M38.980; -.
DR   PRIDE; Q3KJE5; -.
DR   EnsemblBacteria; ABA72111; ABA72111; Pfl01_0367.
DR   KEGG; pfo:Pfl01_0367; -.
DR   eggNOG; ENOG4105CI2; Bacteria.
DR   eggNOG; COG1228; LUCA.
DR   HOGENOM; HOG000218461; -.
DR   KO; K01468; -.
DR   OMA; PTFMGAH; -.
DR   BioCyc; PFLU205922:G1G4S-371-MONOMER; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050480; F:imidazolonepropionase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019556; P:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   CDD; cd01296; Imidazolone-5PH; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_00372; HutI; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR005920; HutI.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR42752; PTHR42752; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01224; hutI; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJE5.
DR   SWISS-2DPAGE; Q3KJE5.
KW   Complete proteome; Cytoplasm; Histidine metabolism; Hydrolase; Iron;
KW   Metal-binding; Zinc.
FT   CHAIN         1    401       Imidazolonepropionase.
FT                                /FTId=PRO_0000306489.
FT   METAL        66     66       Zinc or iron. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
FT   METAL        68     68       Zinc or iron. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
FT   METAL       236    236       Zinc or iron. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
FT   METAL       311    311       Zinc or iron. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
FT   BINDING      75     75       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
FT   BINDING      88     88       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
FT   BINDING     138    138       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
FT   BINDING     171    171       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
FT   BINDING     239    239       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00372}.
SQ   SEQUENCE   401 AA;  43335 MW;  CA17CF0569B8894C CRC64;
     MKTLWQHCHV ATMAQGVYSI IEDAAIVTSG ALIEWIGPRS QLPSGEYPAV NDLQGAWVTP
     GLIDCHTHTV FGGNRSGEFE KRLQGVSYAE IAAAGGGIAS TVRATREASE DELFASAAKR
     LKSLMRDGVT TVEMKSGYGL DLASERKILR VIRRLAAELP ISVRSTCLAA HALPPEYQDR
     ADDYIDHICA EMLPALAAEG LVDAVDAFCE YLAFSPEQVE RVFIAAQKLG LPVKLHAEQL
     SSLHGSSLAA RYHALSADHL EFMDEADAIA MAESDTVAVL LPGAFYFLRE TRLPPMEALR
     KHKVKIAIAS DLNPGTSPAL SLRLMLNMAC TCFRMTPEEA LAGATIHAAQ ALGMAETHGS
     LEVGKVADFV AWQIDRPADL AYWLGGELDK RVVRHGVESS L
//

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