(data stored in ACNUC7421 zone)

SWISSPROT: HUTI_LEGPC

ID   HUTI_LEGPC              Reviewed;         403 AA.
AC   A5IGJ7;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 73.
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}; OrderedLocusNames=LPC_2582;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate;
CC         Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377, ChEBI:CHEBI:58928,
CC         ChEBI:CHEBI:77893; EC=3.5.2.7; Evidence={ECO:0000255|HAMAP-
CC         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 superfamily.
CC       HutI family. {ECO:0000255|HAMAP-Rule:MF_00372}.
DR   EMBL; CP000675; ABQ56497.1; -; Genomic_DNA.
DR   SMR; A5IGJ7; -.
DR   EnsemblBacteria; ABQ56497; ABQ56497; LPC_2582.
DR   KEGG; lpc:LPC_2582; -.
DR   HOGENOM; HOG000218461; -.
DR   KO; K01468; -.
DR   OMA; DHCTHLT; -.
DR   UniPathway; UPA00379; UER00551.
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; A5IGJ7.
DR   SWISS-2DPAGE; A5IGJ7.
KW   Cytoplasm; Histidine metabolism; Hydrolase; Iron; Metal-binding; Zinc.
FT   CHAIN           1..403
FT                   /note="Imidazolonepropionase"
FT                   /id="PRO_0000306468"
FT   METAL           69
FT                   /note="Zinc or iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   METAL           71
FT                   /note="Zinc or iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   METAL           239
FT                   /note="Zinc or iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   METAL           314
FT                   /note="Zinc or iron"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         78
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         91
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         141
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         174
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT   BINDING         242
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
SQ   SEQUENCE   403 AA;  43709 MW;  F025EE2CBAB83340 CRC64;
     MFACDELLLN ASTIDATGLQ LSNQAIVIKK GRIEWCGSED QLPAHFQESA KSRKDCHGQL
     ITPGLIDCHT HLVYAGHRAA EFRLKLQGVS YADIAKSGGG ILSTVQMTRD ASEEELIDQS
     LPRLLALKNE GVTTVEIKSG YGLDLQNELK MLKVARQLGE MAGVRVKTTF LGAHAVGPEF
     KGNSQAYVDF LCNEMLPAAK NMDLVDTVDV FCESIAFSIR QAEQIFQAAK DLNLPIKCHA
     EQLSNMGASS LAARYGALSC DHLEFLDENG ALNMVKANTV AVLLPGAFYF LKEKQKPPVD
     LLRQVGVGMA IATDSNPGSS PTTSLLLMMS MACQFFSMSI PEVLSAVTYQ ASRALGMEKD
     IGSIEAGKIA DLVLWSIKDS AALCYYFAYP LPHQTMVAGE WVS
//

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