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Database: UniProt
Entry: A0A220U244_9BACI
LinkDB: A0A220U244_9BACI
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ID   A0A220U244_9BACI        Unreviewed;       550 AA.
AC   A0A220U244;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   18-JUN-2025, entry version 30.
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:ASK62006.1};
GN   ORFNames=CFK37_07455 {ECO:0000313|EMBL:ASK62006.1};
OS   Virgibacillus phasianinus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Virgibacillus.
OX   NCBI_TaxID=2017483 {ECO:0000313|EMBL:ASK62006.1, ECO:0000313|Proteomes:UP000198312};
RN   [1] {ECO:0000313|EMBL:ASK62006.1, ECO:0000313|Proteomes:UP000198312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM2416 {ECO:0000313|EMBL:ASK62006.1,
RC   ECO:0000313|Proteomes:UP000198312};
RA   Tak E.J., Bae J.-W.;
RT   "Virgibacillus sp. LM2416.";
RL   Submitted (JUL-2017) 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}.
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DR   EMBL; CP022315; ASK62006.1; -; Genomic_DNA.
DR   RefSeq; WP_089061266.1; NZ_CP022315.1.
DR   AlphaFoldDB; A0A220U244; -.
DR   KEGG; vil:CFK37_07455; -.
DR   OrthoDB; 9764874at2; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000198312; Chromosome.
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:UP000198312}.
FT   DOMAIN          6..132
FT                   /note="Urocanase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17391"
FT   DOMAIN          135..343
FT                   /note="Urocanase Rossmann-like"
FT                   /evidence="ECO:0000259|Pfam:PF01175"
FT   DOMAIN          346..540
FT                   /note="Urocanase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17392"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         47..48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         171..173
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         196
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         237..238
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         258..262
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         268..269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         317
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT   BINDING         487
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
SQ   SEQUENCE   550 AA;  60391 MW;  2A20EB95A591F385 CRC64;
     MNKVDVRAKK GLELECKGWE QEAALRMLYN NLDPEVAENP EELVVYGGIG KAARNWESFH
     AIVKTLRNLE NDETMLIQSG KPVGVFKTHK HAPRVLLSNS VLVPKWANWE HFHELDQKGL
     MMYGQMTAGS WIYIGTQGIL QGTYETFSSL AKKHYNGSLK GTITLTAGLG GMGGAQPLAV
     TMNEGVVIAV EVDKSRIEKR LKTKYCDVMT ESIDEAISLA KEAKEAGKAL SIALLGNAAE
     IHHELLTKDI QIDIVTDQTS AHDPLNGYVP VGFTVEEAET LRKKDPEAYT VKSKASMAKH
     VEAMLLHKDN GSIVFDYGNN IRQVAHDEGV EKAFDFPGFV PAYIRPLFTE GKGPFRWAAL
     SGDPEDIYRT DQLIKELFPE NKALIRWIDM AQEQIAFQGL PSRICWLGYG ERMKMGLAIN
     ELVRKGELKA PVVIGRDHLD CGSVASPNRE TEGMKDGSDA VGDWAVLNAL INTAAGGSWI
     SFHHGGGVGM GYSLHAGMVA LADGTDLAHE RLERVLTTDP GMGIIRHADA GYESAINFAE
     EHNITIPTKK
//
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