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 22-NOV-2017, entry version 76. 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}; GN 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., RA Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., RA Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., RA Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., RA Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., RA Mansfield J.W., Collmer A., Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. RT phaseolicola 1448A reveals divergence among pathovars in genes RT involved in virulence and transposition."; RL J. Bacteriol. 187:6488-6498(2005). CC -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone- CC 5-propionate. {ECO:0000255|HAMAP-Rule:MF_00577}. CC -!- CATALYTIC ACTIVITY: 3-(5-oxo-4,5-dihydro-3H-imidazol-4- CC yl)propanoate = urocanate + H(2)O. {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- CC 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 ProteinModelPortal; Q48CE0; -. DR SMR; Q48CE0; -. DR STRING; 264730.PSPPH_4860; -. DR EnsemblBacteria; AAZ37644; AAZ37644; PSPPH_4860. DR KEGG; psp:PSPPH_4860; -. DR eggNOG; ENOG4105CGP; Bacteria. DR eggNOG; COG2987; LUCA. DR HOGENOM; HOG000237606; -. DR KO; K01712; -. DR OMA; VSFHHGG; -. 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-EC. 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 HAMAP; MF_00577; HutU; 1. DR InterPro; IPR023637; Urocanase. DR InterPro; IPR035401; Urocanase_C. DR InterPro; IPR023636; Urocanase_CS. DR InterPro; IPR035400; Urocanase_N. DR InterPro; IPR035085; Urocanase_Rossmann-like. DR InterPro; IPR036190; Urocanase_sf. DR PANTHER; PTHR12216; PTHR12216; 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; SSF111326; 1. DR TIGRFAMs; TIGR01228; hutU; 1. DR PROSITE; PS01233; UROCANASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Histidine metabolism; Lyase; NAD. FT CHAIN 1 565 Urocanate hydratase. FT /FTId=PRO_1000025138. FT NP_BIND 61 62 NAD. {ECO:0000255|HAMAP-Rule:MF_00577}. FT NP_BIND 185 187 NAD. {ECO:0000255|HAMAP-Rule:MF_00577}. FT NP_BIND 251 252 NAD. {ECO:0000255|HAMAP-Rule:MF_00577}. FT NP_BIND 272 276 NAD. {ECO:0000255|HAMAP-Rule:MF_00577}. FT NP_BIND 282 283 NAD. {ECO:0000255|HAMAP-Rule:MF_00577}. FT ACT_SITE 419 419 {ECO:0000255|HAMAP-Rule:MF_00577}. FT BINDING 139 139 NAD. {ECO:0000255|HAMAP-Rule:MF_00577}. FT BINDING 205 205 NAD. {ECO:0000255|HAMAP-Rule:MF_00577}. FT BINDING 210 210 NAD. {ECO:0000255|HAMAP-Rule:MF_00577}. FT BINDING 331 331 NAD; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00577}. FT BINDING 501 501 NAD; via carbonyl oxygen. FT {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 //