HUTI_PSEA8
ID HUTI_PSEA8 Reviewed; 402 AA.
AC B7V3I5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=PLES_54821;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(2009).
CC -!- FUNCTION: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond
CC in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is
CC the third step in the universal histidine degradation pathway.
CC {ECO:0000255|HAMAP-Rule:MF_00372}.
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(3+); Xref=ChEBI:CHEBI:29034;
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}.
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DR EMBL; FM209186; CAW30236.1; -; Genomic_DNA.
DR RefSeq; WP_012614637.1; NC_011770.1.
DR AlphaFoldDB; B7V3I5; -.
DR SMR; B7V3I5; -.
DR KEGG; pag:PLES_54821; -.
DR HOGENOM; CLU_041647_0_0_6; -.
DR OMA; CAPHARW; -.
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;
KW Cytoplasm; Histidine metabolism; Hydrolase; Iron; Metal-binding; Zinc.
FT CHAIN 1..402
FT /note="Imidazolonepropionase"
FT /id="PRO_1000121548"
FT BINDING 66
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 68
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 75
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 138
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 138
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 171
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 236
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 239
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 311
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 313
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 315
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
FT BINDING 316
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00372"
SQ SEQUENCE 402 AA; 43396 MW; 04C2A3A033827D8C CRC64;
MKRLWQHCHA ATLKGGKYSI VEDAALVTDG PLIHWIGPRA ELPPGDYAER IDLGGAWLTP
GLIDCHTHAV FGGNRSGEFE QRLEGVSYAV IAAAGGGIAS TVRATREASE EELLASARKR
LEPLLRDGVT ALEIKSGYGL DLASERKMLR VIRRLGERLP ATVRSTCLAA HALPPEYAGR
ADDYIEHICS TMLPALAGEG LVDAVDAFCE HLAFSPAQVE RVFIAARELG LPVKLHAEQL
SSLHGSSLAA RYRALSADHL EYMTEDDARA MGEAGTVAVL LPGAFYLLRE TQLPPIDALR
RHGVAMAIAS DLNPGTSPAL SLRLMLNMAC TLFRLTPEET LAGVTLHAAR ALGLEASHGS
LEVGKLADFV AWDIERPAEL AYWLGGDLPK RVIRHAEEVY RG
