ID A0A0W1DA61_9SPHN Unreviewed; 403 AA.
AC A0A0W1DA61;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Imidazolonepropionase {ECO:0000256|ARBA:ARBA00012864, ECO:0000256|HAMAP-Rule:MF_00372};
DE EC=3.5.2.7 {ECO:0000256|ARBA:ARBA00012864, ECO:0000256|HAMAP-Rule:MF_00372};
DE AltName: Full=Imidazolone-5-propionate hydrolase {ECO:0000256|HAMAP-Rule:MF_00372};
GN Name=hutI {ECO:0000256|HAMAP-Rule:MF_00372};
GN ORFNames=ATE71_07875 {ECO:0000313|EMBL:KTE15010.1};
OS Sphingopyxis sp. H115.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759073 {ECO:0000313|EMBL:KTE15010.1, ECO:0000313|Proteomes:UP000054021};
RN [1] {ECO:0000313|EMBL:KTE15010.1, ECO:0000313|Proteomes:UP000054021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H115 {ECO:0000313|EMBL:KTE15010.1,
RC ECO:0000313|Proteomes:UP000054021};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00372};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00372};
CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00372};
CC Note=Binds 1 zinc or iron ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00372}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC HutI family. {ECO:0000256|HAMAP-Rule:MF_00372}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTE15010.1}.
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DR EMBL; LNSA01000008; KTE15010.1; -; Genomic_DNA.
DR RefSeq; WP_058802919.1; NZ_LNSA01000008.1.
DR AlphaFoldDB; A0A0W1DA61; -.
DR STRING; 1759073.ATE71_07875; -.
DR OrthoDB; 9776455at2; -.
DR UniPathway; UPA00379; UER00551.
DR Proteomes; UP000054021; Unassembled WGS sequence.
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; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 NCBIfam; TIGR01224; hutI; 1.
DR PANTHER; PTHR42752; IMIDAZOLONEPROPIONASE; 1.
DR PANTHER; PTHR42752:SF1; IMIDAZOLONEPROPIONASE-RELATED; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00372};
KW Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW Rule:MF_00372};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00372};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00372};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00372};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00372}.
FT DOMAIN 66..383
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 74
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 76
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 83
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 146
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 146
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 179
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 242
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 245
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 317
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 319
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 321
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 322
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
SQ SEQUENCE 403 AA; 42489 MW; 6E739EC9090079A9 CRC64;
MTHRRETVQM EQRWTNARLA TMAGDDLGLV DDGVVVADDG RITYAGPASG APAAAGTVHD
CEGRLIAPGL IDCHTHLVHG GNRANEWAMR LEGATYEDIA RAGGGIVSTM RATRAASEEE
LVESALPRLD ALIAEGVTTI EIKSGYGLST EDELKMLRAA RALGERRAIR IEPTFLGAHA
LPPEYQGDSD AYIDLVVNEM IPAAAPFATA VDAFCEGIGF SPGQCERVIE AAKARGLAVK
LHAEQLSALS GSALAARHGA LSADHLEHAT DDDVCAMAEA GTVAVLLPGA YYFMRETKLP
PVDAMRRHGV RIALATDNNP GTSPTTSLLL MLNMGATLFG LTVVEALRGV TVNAAAALGL
GNEIGTLEPG KACDLAIWDV GDPAELVYRI GFNPLHQRIK DGQ
//
