GenomeNet

Database: UniProt
Entry: A0A4U0F9C1_9BACL
LinkDB: A0A4U0F9C1_9BACL
Original site: A0A4U0F9C1_9BACL 
ID   A0A4U0F9C1_9BACL        Unreviewed;       556 AA.
AC   A0A4U0F9C1;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, entry version 22.
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   ORFNames=E5161_16140 {ECO:0000313|EMBL:TJY40684.1};
OS   Cohnella pontilimi.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Cohnella.
OX   NCBI_TaxID=2564100 {ECO:0000313|EMBL:TJY40684.1, ECO:0000313|Proteomes:UP000309673};
RN   [1] {ECO:0000313|EMBL:TJY40684.1, ECO:0000313|Proteomes:UP000309673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAU 1483 {ECO:0000313|EMBL:TJY40684.1,
RC   ECO:0000313|Proteomes:UP000309673};
RA   Kim W.;
RT   "Cohnella sp. nov., isolated from soil.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5-
CC       propionate. {ECO:0000256|HAMAP-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:TJY40684.1}.
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; SUPK01000008; TJY40684.1; -; Genomic_DNA.
DR   RefSeq; WP_136778874.1; NZ_SUPK01000008.1.
DR   AlphaFoldDB; A0A4U0F9C1; -.
DR   OrthoDB; 9764874at2; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000309673; 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   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; 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.
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:UP000309673}.
FT   DOMAIN          11..134
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..542
FT                   /note="Urocanase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17392"
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         490
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
SQ   SEQUENCE   556 AA;  60756 MW;  0D027442AFB177A2 CRC64;
     MGEKGGNVEL IKAARGTELR CKGWRQEALL RMLENVLENG ENQKELIVYA ALGKAARNWG
     SYHAIVDTLT NLEDDETLVI QSGKPIGIMK THALAPIVIM ANCNMVGKWA TSENFYDLQE
     KGLIIWGGLT AAAWQYIGSQ GVIQGTYEIF STIRSQHFGG SLAGRFILTA GLGGMGGAQP
     LAGVMVGAAI LCVEADESRV DKRIEVGYLQ KKTRSLDEAL AWIREAMERK ESVSVGLVGN
     AAEIYPELVE RGITPDIVTD QTSAHDLMYG YIPVGLSQEE VRSMRGQHPE ELQSKAGASI
     ARQVEAMLAF KRKGAIVFDN GNNIRTQAQQ YGVKDAFDID IFTEAFLRPL FARAIGPFRW
     VALTGDPEDI RKIDQYILKH FADNEIVTNW ISLANKYVPF QGLPARIGWF GHGERTKLAL
     AVNQMVREGV LSGPVAFSRD HLDAGAMTHP NIMTERMKDG SDAISDWPLL NAMLNCSSMA
     DLVAIHSGGG GYSGYMTSAG VTIVADGTEM SDLRLKTALD NDTGIGVLRY ADAGYEESFD
     EIDKKGIRRI ETEGVK
//
DBGET integrated database retrieval system