ID HUTU_KLEP3 Reviewed; 562 AA. AC B5XZ80; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 1. DT 27-MAR-2024, 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=KPK_3778; OS Klebsiella pneumoniae (strain 342). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=507522; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=342; RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141; RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H., RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y., RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W., RA Methe B.A.; RT "Complete genome sequence of the N2-fixing broad host range endophyte RT Klebsiella pneumoniae 342 and virulence predictions verified in mice."; RL PLoS Genet. 4:E1000141-E1000141(2008). 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; Evidence={ECO:0000255|HAMAP- CC 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; CP000964; ACI09126.1; -; Genomic_DNA. DR AlphaFoldDB; B5XZ80; -. DR SMR; B5XZ80; -. DR KEGG; kpe:KPK_3778; -. DR HOGENOM; CLU_018868_0_1_6; -. DR UniPathway; UPA00379; UER00550. DR Proteomes; UP000001734; 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; Urocanase like domains; 1. DR Gene3D; 3.40.1770.10; Urocanase superfamily; 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 NCBIfam; TIGR01228; hutU; 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; Histidine metabolism; Lyase; NAD. FT CHAIN 1..562 FT /note="Urocanate hydratase" FT /id="PRO_1000129565" FT ACT_SITE 410 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 52..53 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 130 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 176..178 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 196 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 201 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 242..243 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 263..267 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 273..274 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 322 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" FT BINDING 492 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00577" SQ SEQUENCE 562 AA; 61562 MW; 8F984F14F7AC1AC3 CRC64; MSQSKYRQLD VRAPRGTTLT ARSWLTEAPL RMLMNNLDPD VAENPHELVV YGGIGRAARN WECYDAIVKA LKNLESDETL LVQSGKPVGV FKTHENSPRV LIANSNLVPH WATWEHFNEL DAKGLAMYGQ MTAGSWIYIG SQGIVQGTYE TFVEAGRQHY QGSLKGRWVL TAGLGGMGGA QPLAATLAGA CSLNIECQQS RIDFRLRTRY VDEQATSLDD ALARIKKYTA EGRAISIALC GNAADIVPEL VKRGVRPDMV TDQTSAHDPL HGYLPKGWSW EEYQQKAESD PQGTILAAKR SMADHVQAML AFNEMGVPTF DYGNNIRQMA QEMGVSNAFD FPGFVPAYIR PLFCRGIGPF RWVALSGDPQ DIYKTDAKVK EIIKDDKHLH HWLDMARERI SFQGLPARIC WVGLEWRQKL GLAFNEMVRS GEVSAPIVIG RDHLDSGSVA SPNRETEAMR DGSDAVSDWP LLNALLNTAS GATWVSLHHG GGVGMGFSQH SGMVIVCDGT DEAAARIARV LRNDPATGVM RHADAGYDIA IECAAEQGLN LPMVAATQGN AK //