ID A0A964E0D4_9PROT Unreviewed; 556 AA.
AC A0A964E0D4;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
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=ASILVAE211_17780 {ECO:0000313|EMBL:MCB8877049.1};
OS Acidisoma silvae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Acetobacterales; Acidocellaceae; Acidisoma.
OX NCBI_TaxID=2802396 {ECO:0000313|EMBL:MCB8877049.1, ECO:0000313|Proteomes:UP000708298};
RN [1] {ECO:0000313|EMBL:MCB8877049.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HW T2.11 {ECO:0000313|EMBL:MCB8877049.1};
RX PubMed=34683374;
RA Mieszkin S., Pouder E., Uroz S., Simon-Colin C., Alain K.;
RT "Acidisoma silvae sp. nov. and Acidisomacellulosilytica sp. nov., Two
RT Acidophilic Bacteria Isolated from Decaying Wood, Hydrolyzing Cellulose and
RT Producing Poly-3-hydroxybutyrate.";
RL Microorganisms 9:0-0(2021).
RN [2] {ECO:0000313|EMBL:MCB8877049.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HW T2.11 {ECO:0000313|EMBL:MCB8877049.1};
RA Mieszkin S., Pouder E., Alain K.;
RL Submitted (JAN-2021) 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:MCB8877049.1}.
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DR EMBL; JAESVB010000010; MCB8877049.1; -; Genomic_DNA.
DR RefSeq; WP_227322706.1; NZ_JAESVB010000010.1.
DR Proteomes; UP000708298; 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:0006548; P:L-histidine catabolic process; IEA:UniProtKB-UniRule.
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; 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:UP000708298}.
FT DOMAIN 11..136
FT /note="Urocanase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17391"
FT DOMAIN 140..348
FT /note="Urocanase Rossmann-like"
FT /evidence="ECO:0000259|Pfam:PF01175"
FT DOMAIN 351..544
FT /note="Urocanase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17392"
FT BINDING 52..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 176..178
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 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 242..243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 263..267
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 273..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 491
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
SQ SEQUENCE 556 AA; 59777 MW; FEA7E026C872AB46 CRC64;
MTASLPNSRS IRAPRGLTLN AKSWHTEAPL RMLMNNLDSE VAERPEDLVV YGGRGKAARN
WESFDRIVST LKAMDADETL LIQSGKPVGV IRTHADAPRV LIANANLVGK WATAEVFDEL
ERRGLMMYGQ MTAGSWTYIG SQGIIGGTFE TFVEAGRQHY GGDLSGRWLL TAGLGGMGGA
QPLAGVMAGC SVLAVEMRAE RIERRIESGF LDKRADNLDD ALALIETARR SGAPVSVGLI
GNAAEVYEAI LSRGVMPDLV TDQTAAHDPL HGYIPAGWSI QDWEARRESD PAGVIAAAKA
TMARQVRAML AFRARGIPVF DYGNNIRQMA RDAGVEEAFA FPGFIAAYVR PQFCRGRTQF
RWVALTGEAQ DIAVSSSKLK GVVADSSFAR WIDMAETRIR FQGLPSRSYW MGLQDRVAAG
LALNDMVARG EVSGPILVTR DHISSGSVAS PNRESEGMLD GSDAVSDWPM LNALAACASG
ATWVSLHHGG GVGIGYSQHA GFAVVADGTP DAARRLSRVL SNDSSVAVFR HADAGYEDAI
ETVHREGLVM PFAMPR
//
