ID HUTU_PSE14 Reviewed; 565 AA. AC Q48CE0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 14-DEC-2022, entry version 91. DE RecName: Full=Urocanate hydratase {ECO:0000255|HAMAP-Rule:MF_00577}; DE Short=Urocanase {ECO:0000255|HAMAP-Rule:MF_00577}; DE EC=4.2.1.49 {ECO:0000255|HAMAP-Rule:MF_00577}; DE AltName: Full=Imidazolonepropionate hydrolase {ECO:0000255|HAMAP-Rule:MF_00577}; GN Name=hutU {ECO:0000255|HAMAP-Rule:MF_00577}; OrderedLocusNames=PSPPH_4860; OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1448A / Race 6; RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R., RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., RA Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola RT 1448A reveals divergence among pathovars in genes involved in virulence and RT transposition."; RL J. Bacteriol. 187:6488-6498(2005). CC -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-5- CC propionate. {ECO:0000255|HAMAP-Rule:MF_00577}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-imidazolone-5-propanoate = H2O + trans-urocanate; CC Xref=Rhea:RHEA:13101, ChEBI:CHEBI:15377, ChEBI:CHEBI:17771, CC ChEBI:CHEBI:77893; EC=4.2.1.49; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00577}; CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00577}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00577}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00577}. CC -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000255|HAMAP- CC Rule:MF_00577}. 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; CP000058; AAZ37644.1; -; Genomic_DNA. DR RefSeq; WP_011169774.1; NC_005773.3. DR AlphaFoldDB; Q48CE0; -. DR SMR; Q48CE0; -. DR STRING; 264730.PSPPH_4860; -. DR EnsemblBacteria; AAZ37644; AAZ37644; PSPPH_4860. DR KEGG; psp:PSPPH_4860; -. DR eggNOG; COG2987; Bacteria. DR HOGENOM; CLU_018868_0_1_6; -. DR OMA; LVGDWAN; -. DR OrthoDB; 100619at2; -. DR UniPathway; UPA00379; UER00550. DR Proteomes; UP000000551; 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:histidine catabolic process to glutamate and formamide; IEA:UniProtKB-UniPathway. DR GO; GO:0019557; P:histidine catabolic process to glutamate and formate; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.10730; -; 1. DR HAMAP; MF_00577; HutU; 1. DR InterPro; IPR023637; Urocanase. 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 PANTHER; PTHR12216; 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 TIGRFAMs; TIGR01228; hutU; 1. DR PROSITE; PS01233; UROCANASE; 1. PE 3: Inferred from homology; KW Cytoplasm; Histidine metabolism; Lyase; NAD. FT CHAIN 1..565 FT /note="Urocanate hydratase" FT /id="PRO_1000025138" FT REGION 453..472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 419 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 61..62 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 139 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 185..187 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 205 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 210 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 251..252 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 272..276 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 282..283 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 331 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 501 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" SQ SEQUENCE 565 AA; 61760 MW; A94969B1B9C06C25 CRC64; MTENNQDLKQ NWTRHREGVV QAACGTQLTA KSWLTEAPLR MLMNNLDPEV AENPNELVVY GGIGRAARNW ECYDKIVESL TQLNDDETLL VQSGKPVGVF KTHSNAPRVL IANSNLVPHW ASWEHFNELD AKGLAMYGQM TAGSWIYIGS QGIVQGTYET FVEAGRQHYD GNLKGRWVLT AGLGGMGGAQ PLAATLAGAC SLNIECQQSR IDFRIKTRYV DEQAADLDDA LARIAKYTAE GKAISIALCG NAAEILPEMV RRGVRPDMVT DQTSAHDPLN GYLPKGWTWD EYRVRSVSEP ANVVKAAKQS MAEHVEAMLA FQQAGIPTFD YGNNIRQMAK EVGVANAFDF PGFVPAYIRP LFCRGIGPFR WAALSGDPED IYKTDAKVKE LIPDDDHLHN WLDMARERIS FQGLPARICW VGLGQRAKLG LAFNEMVRSG ELSAPVVIGR DHLDSGSVAS PNRETESMRD GSDAVSDWPL LNALLNTASG ATWVSLHHGG GVGMGFSQHS GMVIVCDGTD EAAERIARVL HNDPATGVMR HADAGYDIAI DCAREQGLNL PMIGR //