ID A0A5C4VU22_9ACTN Unreviewed; 561 AA.
AC A0A5C4VU22;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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=FHP29_11115 {ECO:0000313|EMBL:TNM39454.1};
OS Nocardioides albidus.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1517589 {ECO:0000313|EMBL:TNM39454.1, ECO:0000313|Proteomes:UP000313231};
RN [1] {ECO:0000313|EMBL:TNM39454.1, ECO:0000313|Proteomes:UP000313231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AB 2015297 {ECO:0000313|EMBL:TNM39454.1,
RC ECO:0000313|Proteomes:UP000313231};
RX PubMed=26530636; DOI=.1099/ijsem.0.000730;
RA Singh H., Du J., Trinh H., Won K., Yang J.E., Yin C., Kook M., Yi T.H.;
RT "Nocardioides albidus sp. nov., an actinobacterium isolated from garden
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 66:371-378(2016).
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:TNM39454.1}.
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DR EMBL; VDMP01000024; TNM39454.1; -; Genomic_DNA.
DR RefSeq; WP_139622945.1; NZ_VDMP01000024.1.
DR AlphaFoldDB; A0A5C4VU22; -.
DR OrthoDB; 9764874at2; -.
DR UniPathway; UPA00379; UER00550.
DR Proteomes; UP000313231; 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:UP000313231}.
FT DOMAIN 17..143
FT /note="Urocanase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17391"
FT DOMAIN 146..353
FT /note="Urocanase Rossmann-like"
FT /evidence="ECO:0000259|Pfam:PF01175"
FT DOMAIN 356..550
FT /note="Urocanase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17392"
FT ACT_SITE 415
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 58..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 182..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 207
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 248..249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 269..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 278..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 327
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
FT BINDING 497
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00577"
SQ SEQUENCE 561 AA; 60945 MW; F51F31FD64A3D889 CRC64;
MTTSSSQSGQ TNPRLPIHAA TGTELTAKSW QTEAPLRMLM NNLDPENAER PEDLVVYGGT
GKAARNWEAY DALVRTLRDL EDDETMLVQS GKPVGVWKTN KWAPRVLIAN SNLVGDWANW
EEFRRLEEMG LTMYGQMTAG SWIYIGTQGI LQGTFETFAA VADKRFDGTL AGTITLTAGL
GGMGGAQPLA VTMNDGVAIC VDVDQSRITR RIDHRYLDVQ ADSLEHALEL AVQARDEKRG
LSIGLLGNAA EVFPKLLEMK APIDIVTDQT SAHDPLSYLP VGVSFEDWQA AAERDPAGFT
KDAQASMAAH VRAMVEFQDA GAEVFDYGNS IRDEARKGGY ERAFEFPGFV PAYIRPLFCE
GKGPFRWAAL SGDPADIAAT DKAILELFPD NERLHKWIGM AQERVHYQGL PARICWLGYK
ERHLAGLKFN EMVKSGELKA PIVIGRDHLD CGSVASPYRE TEAMLDGSDA IADWPLLNAM
TAVASGATWV SLHHGGGVGM GRSIHSGQVC VADGTELAAA KIEAVLTNDP GMGVIRHVDA
GYDRAVEVAA ERGVRIPMQE G
//
