ID A0A0X3VDV5_9ACTN Unreviewed; 393 AA.
AC A0A0X3VDV5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=ADL22_14025 {ECO:0000313|EMBL:KUL42597.1};
OS Streptomyces sp. NRRL F-4489.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609095 {ECO:0000313|EMBL:KUL42597.1, ECO:0000313|Proteomes:UP000053256};
RN [1] {ECO:0000313|EMBL:KUL42597.1, ECO:0000313|Proteomes:UP000053256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-4489 {ECO:0000313|EMBL:KUL42597.1,
RC ECO:0000313|Proteomes:UP000053256};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL42597.1}.
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DR EMBL; LLZI01000158; KUL42597.1; -; Genomic_DNA.
DR RefSeq; WP_066978053.1; NZ_LLZI01000158.1.
DR AlphaFoldDB; A0A0X3VDV5; -.
DR STRING; 1609095.ADL22_14025; -.
DR OrthoDB; 9776455at2; -.
DR UniPathway; UPA00379; UER00551.
DR Proteomes; UP000053256; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000053256};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00372}.
FT DOMAIN 253..368
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT BINDING 75
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 77
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 84
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 142
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 142
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 169
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 232
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 235
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 306
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 308
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 310
FT /ligand="N-formimidoyl-L-glutamate"
FT /ligand_id="ChEBI:CHEBI:58928"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT BINDING 311
FT /ligand="4-imidazolone-5-propanoate"
FT /ligand_id="ChEBI:CHEBI:77893"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
SQ SEQUENCE 393 AA; 40711 MW; EA424143D8650964 CRC64;
MTTTSAPTTA ITHIAQLVTN DPSLGEGPLG LIQDAAVVID GDRIAWVGPS SKAPATDNAV
DAAGRAGLPG FVDSHSHLVF AGDRTEEFNA RMSGRPYSAG GIRTTVAATR AADDAALHAN
VARYLAEGLR QGTTTQEVKS GYGLTVEDEA RAVRIAAAHT DEVTFLGAHI VSPDYADDPA
GYVDLVTGPM LDACAPHARW VDVFCERGAF DGDQARAVLT AGKAKGLVPR VHANQLGHGP
GVQLAVELGA ASADHCTHLT AADIDALAQS DTVATLLPGA EFSTRAQWPD ARPLLDAGAT
VALSTDCNPG SSFTSSMPFC IALAVRDMGM TPDEAVWSAT AGGARALRRD DVGRIAPGAR
ADLLLLDAPS HVHLAYRPGV PLVTDVWHKG ARL
//
