GenomeNet

Database: UniProt
Entry: A0A095XZ31_9BACT
LinkDB: A0A095XZ31_9BACT
Original site: A0A095XZ31_9BACT 
ID   A0A095XZ31_9BACT        Unreviewed;       414 AA.
AC   A0A095XZ31;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=HMPREF1640_12410 {ECO:0000313|EMBL:KGF15091.1};
OS   Prevotella sp. S7-1-8.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1284775 {ECO:0000313|EMBL:KGF15091.1, ECO:0000313|Proteomes:UP000029597};
RN   [1] {ECO:0000313|EMBL:KGF15091.1, ECO:0000313|Proteomes:UP000029597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S7-1-8 {ECO:0000313|EMBL:KGF15091.1,
RC   ECO:0000313|Proteomes:UP000029597};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-2014) 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:KGF15091.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JRNC01000082; KGF15091.1; -; Genomic_DNA.
DR   RefSeq; WP_036894807.1; NZ_JRNC01000082.1.
DR   AlphaFoldDB; A0A095XZ31; -.
DR   eggNOG; COG1228; Bacteria.
DR   OrthoDB; 9776455at2; -.
DR   UniPathway; UPA00379; UER00551.
DR   Proteomes; UP000029597; 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}; Reference proteome {ECO:0000313|Proteomes:UP000029597};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00372}.
FT   DOMAIN          71..389
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   BINDING         79
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         81
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         88
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         151
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         151
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         184
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         249
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         252
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         323
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         325
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         327
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
FT   BINDING         328
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00372"
SQ   SEQUENCE   414 AA;  45278 MW;  99E849A6E34D7CD4 CRC64;
     MKLLVTNIDI LAGVGHDGKR CLKGDEMARI DTIEHAYLYV EDGRIAAYGK RSDMPQIDSD
     TTVVDAEGGA VLPSFCDSHT HIVYAGSREG EFVDKIRGLS YAEIAKRGGG ILNSADRLHE
     LSEDELYTQA MKRVDEVIRK GTGAIEIKSG YGLNLEDELK MLRVIRRVKE TSPVKVVANF
     LGAHAVGRAF AGRQKEYVDH VINDMLPAVA KENLADFIDV FCDEGFFTPE ETRRILKAGE
     KYGLRGKIHA EELAVSGGVD VAVECDALSV DHLEAMDDHD IELLKNTNTI PTALPGTSFF
     LNMPFAPARK MIEAGLPMAI ASDYNPGSTP SGDMKFAVSL ACIKMRLMPA EAINAATLNS
     ACAMGLSEDY GSITKGKVAN FYITDPIPSV DFIPYAYTTP IIRRIFLKGV EYRK
//
DBGET integrated database retrieval system