ID A0A3D8GQE1_9BACI Unreviewed; 553 AA.
AC A0A3D8GQE1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 18-JUN-2025, entry version 25.
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:RDU36502.1};
GN ORFNames=DRW41_13310 {ECO:0000313|EMBL:RDU36502.1};
OS Neobacillus piezotolerans.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Neobacillus.
OX NCBI_TaxID=2259171 {ECO:0000313|EMBL:RDU36502.1, ECO:0000313|Proteomes:UP000257144};
RN [1] {ECO:0000313|EMBL:RDU36502.1, ECO:0000313|Proteomes:UP000257144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-04 {ECO:0000313|EMBL:RDU36502.1,
RC ECO:0000313|Proteomes:UP000257144};
RA Yu L., Tang X.;
RT "Bacillus sp. YLB-04 draft genome sequence.";
RL Submitted (JUL-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:RDU36502.1}.
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DR EMBL; QNQT01000005; RDU36502.1; -; Genomic_DNA.
DR RefSeq; WP_115452495.1; NZ_QNQT01000005.1.
DR AlphaFoldDB; A0A3D8GQE1; -.
DR OrthoDB; 9764874at2; -.
DR UniPathway; UPA00379; UER00550.
DR Proteomes; UP000257144; 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:UP000257144}.
FT DOMAIN 12..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 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 553 AA; 60291 MW; 44D05A3B07799EAB CRC64;
MKAETKNKVV RYRGSELNTK GWIQEAALRM LMNNLDEEVA ENPDDLVVYG GIGKAARNWN
CFEAIVSALK KLESDETLLI QSGKPVAVFK SHPDAPRVLI ANSNLVPAWA NWDTFHELDK
KGLMMYGQMT AGSWIYIGSQ GIVQGTYETF AELARQHFTG SLKHTITLTA GLGGMGGAQP
LAVTLNGGVC LAIDTDIHHI QRRIETKYLD VVAESLEDAL AQAQEAKLQG IALSIGLEGN
AAEILPRMLE LGFVPDVLTD QTSAHDPLNG YIPEGYSLEE AAEFRKNDPD GYVKKSCESM
AVHVKAMLEM QKKGATTFDY GNNIRQVAKD AGVENAFDFP GFVPAYIRPL FCEGKGPFRW
VALSGDPEDI YKTDEVILRE FADNEHLCNW IRMAREKIQF QGLPSRICWL GYGERARFGK
IINDMVASGE LKAPIVIGRD HLDSGSVASP NRETEGMADG SDAVADWPIL NAMINAVGGA
SWVSVHHGGG VGMGYSLHAG MVIVADGTKE AERRLERVLT TDPGMGIVRH VDAGYDLAVD
AAKKNGLNIP MLD
//
