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Database: UniProt
Entry: A0A3L7JZA7_9BACI
LinkDB: A0A3L7JZA7_9BACI
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ID   A0A3L7JZA7_9BACI        Unreviewed;       554 AA.
AC   A0A3L7JZA7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   18-JUN-2025, entry version 23.
DE   RecName: Full=Urocanate hydratase {ECO:0000256|ARBA:ARBA00011992, ECO:0000256|HAMAP-Rule:MF_00577};
DE            Short=Urocanase {ECO:0000256|HAMAP-Rule:MF_00577};
DE            EC=4.2.1.49 {ECO:0000256|ARBA:ARBA00011992, ECO:0000256|HAMAP-Rule:MF_00577};
DE   AltName: Full=Imidazolonepropionate hydrolase {ECO:0000256|ARBA:ARBA00031640, ECO:0000256|HAMAP-Rule:MF_00577};
GN   Name=hutU {ECO:0000256|HAMAP-Rule:MF_00577,
GN   ECO:0000313|EMBL:RLQ95469.1};
GN   ORFNames=D9X91_10575 {ECO:0000313|EMBL:RLQ95469.1};
OS   Falsibacillus albus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Falsibacillus.
OX   NCBI_TaxID=2478915 {ECO:0000313|EMBL:RLQ95469.1, ECO:0000313|Proteomes:UP000276770};
RN   [1] {ECO:0000313|EMBL:RLQ95469.1, ECO:0000313|Proteomes:UP000276770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GY 10110 {ECO:0000313|EMBL:RLQ95469.1,
RC   ECO:0000313|Proteomes:UP000276770};
RA   Shi S.;
RT   "Falsibacillus sp. genome draft.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5-
CC       propionate. {ECO:0000256|ARBA:ARBA00056569, ECO:0000256|HAMAP-
CC       Rule:MF_00577}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-imidazolone-5-propanoate = trans-urocanate + H2O;
CC         Xref=Rhea:RHEA:13101, ChEBI:CHEBI:15377, ChEBI:CHEBI:17771,
CC         ChEBI:CHEBI:77893; EC=4.2.1.49;
CC         Evidence={ECO:0000256|ARBA:ARBA00047623, ECO:0000256|HAMAP-
CC         Rule:MF_00577};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00577};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|HAMAP-Rule:MF_00577};
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004794, ECO:0000256|HAMAP-Rule:MF_00577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00577}.
CC   -!- SIMILARITY: Belongs to the urocanase family.
CC       {ECO:0000256|ARBA:ARBA00007578, ECO:0000256|HAMAP-Rule:MF_00577}.
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:RLQ95469.1}.
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DR   EMBL; RCVZ01000006; RLQ95469.1; -; Genomic_DNA.
DR   RefSeq; WP_121680584.1; NZ_RCVZ01000006.1.
DR   AlphaFoldDB; A0A3L7JZA7; -.
DR   OrthoDB; 9764874at2; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000276770; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016153; F:urocanate hydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019556; P:L-histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019557; P:L-histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway.
DR   FunFam; 3.40.50.10730:FF:000001; Urocanate hydratase; 1.
DR   Gene3D; 3.40.50.10730; Urocanase like domains; 1.
DR   Gene3D; 3.40.1770.10; Urocanase superfamily; 1.
DR   HAMAP; MF_00577; HutU; 1.
DR   InterPro; IPR055351; Urocanase.
DR   InterPro; IPR023637; Urocanase-like.
DR   InterPro; IPR035401; Urocanase_C.
DR   InterPro; IPR038364; Urocanase_central_sf.
DR   InterPro; IPR023636; Urocanase_CS.
DR   InterPro; IPR035400; Urocanase_N.
DR   InterPro; IPR035085; Urocanase_Rossmann-like.
DR   InterPro; IPR036190; Urocanase_sf.
DR   NCBIfam; TIGR01228; hutU; 1.
DR   NCBIfam; NF003820; PRK05414.1; 1.
DR   PANTHER; PTHR12216; UROCANATE HYDRATASE; 1.
DR   PANTHER; PTHR12216:SF4; UROCANATE HYDRATASE; 1.
DR   Pfam; PF01175; Urocanase; 1.
DR   Pfam; PF17392; Urocanase_C; 1.
DR   Pfam; PF17391; Urocanase_N; 1.
DR   PIRSF; PIRSF001423; Urocanate_hydrat; 1.
DR   SUPFAM; SSF111326; Urocanase; 1.
DR   PROSITE; PS01233; UROCANASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00577};
KW   Histidine metabolism {ECO:0000256|ARBA:ARBA00022808, ECO:0000256|HAMAP-
KW   Rule:MF_00577};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00577};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00577};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276770}.
FT   DOMAIN          11..135
FT                   /note="Urocanase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17391"
FT   DOMAIN          138..346
FT                   /note="Urocanase Rossmann-like"
FT                   /evidence="ECO:0000259|Pfam:PF01175"
FT   DOMAIN          349..543
FT                   /note="Urocanase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17392"
FT   ACT_SITE        408
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         50..51
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         128
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         174..176
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         194
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         199
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         240..241
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         261..265
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         271..272
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         320
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         490
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
SQ   SEQUENCE   554 AA;  60760 MW;  66C3CB0599CE02E5 CRC64;
     MKADTNRSIT NYQGSELHAK GWVQEAALRM LMNNLNKDVA EKPEELVVYG GIGKAARNWE
     SYDAIVRTLH ELETDETLLV QSGKPVAVFK THSDAPRVLI ANSNLVPAWA NWETFHELDR
     KGLMMYGQMT AGSWIYIGSQ GIVQGTYETF AELGRQHFNG SLKQTITLTA GLGGMGGAQP
     LAVTMNDGVC IAIEIDKTRI QRRIDTRYLD VSTDSLDEAI EMAKKAKADG KALSIGLLGN
     AAEVLPEMIE KGFIPDVLTD QTSAHDPLNG YVPEGYSLNQ ADELREKNPN DYVKRSKASM
     ANHVKAMLVM QEKGAITFDY GNNIRQVALD EGVQNAFEFP GFVPAYIRPQ FCEGKGPFRW
     VALSGDPEDI RKTDEVILKE FKENEALCKW IRMAQEKIQF QGLPSRICWL GYGERARFGK
     IINDMVASGE LSAPIVIGRD HLDSGSVASP NRETEGMKDG SDAVADWPIL NALINAVGGA
     SWVSVHHGGG VGMGYSLHAG MVIVADGTKE AEKRLERVLT TDPGMGVVRH VDAGYELAEE
     TARKNGINIP MMKD
//
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