(data stored in ACNUC7421 zone)

SWISSPROT: HUTU_RUBXD

ID   HUTU_RUBXD              Reviewed;         554 AA.
AC   Q1AYH3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 84.
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=Rxyl_0583;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000386; ABG03555.1; -; Genomic_DNA.
DR   RefSeq; WP_011563573.1; NC_008148.1.
DR   SMR; Q1AYH3; -.
DR   STRING; 266117.Rxyl_0583; -.
DR   EnsemblBacteria; ABG03555; ABG03555; Rxyl_0583.
DR   KEGG; rxy:Rxyl_0583; -.
DR   eggNOG; ENOG4105CGP; Bacteria.
DR   eggNOG; COG2987; LUCA.
DR   HOGENOM; HOG000237606; -.
DR   KO; K01712; -.
DR   OMA; LVGDWAN; -.
DR   OrthoDB; 100619at2; -.
DR   BioCyc; RXYL266117:G1G6P-587-MONOMER; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000006637; 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; 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;
DR   PRODOM; Q1AYH3.
DR   SWISS-2DPAGE; Q1AYH3.
KW   Cytoplasm; Histidine metabolism; Lyase; NAD; Reference proteome.
FT   CHAIN           1..554
FT                   /note="Urocanate hydratase"
FT                   /id="PRO_1000082351"
FT   NP_BIND         50..51
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   NP_BIND         174..176
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   NP_BIND         240..241
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   NP_BIND         261..265
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   NP_BIND         271..272
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   ACT_SITE        408
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         128
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         194
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         199
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         320
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
FT   BINDING         490
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00577"
SQ   SEQUENCE   554 AA;  60214 MW;  0EA81E7E227B2F83 CRC64;
     MTDGKTTTVR APRGTELSCK GWHQEGALRM LMNNLDPEVA ERPEELVVYG GTGKAARSWE
     CFWAIVEALR GLDGDETLLV QSGKPVAVFR THPWAPRVLI ANSLLVPEWA DWETFRELER
     AGLTMFGQMT AGSWIYIGTQ GILQGTYETF AALAEQRFGG TLRGRVCLTA GLGGMGGAQP
     LAITMNEGVA LCVEVDPRRI DRRLEHRYLD ERIDDLDAAV ERAEEARREG EPLSIGIPGN
     AAEVFPALLE RGYVPDAVTD QTSAHDPLGG YIPAGYTLEE AAELREADPG RYVREARASM
     ARHCAAMVGF MERGAEVFDY GNNLRGEARL GGFERAFSYP GFVPAYIRPL FCEGKGPFRW
     AALSGDPDDI AATDEAVLEL FPENGRLVRW IRQARERVRF QGLPARICWL GAGERHRAGL
     RFNELVAGGT ISAPIVIGRD HLDSGSVASP YRETEGMRDG SDAIADWPVL NALLNTASGA
     SWVAVHHGGG VGIGKSIHAG AQVVVDGTEE GAARIERVLT NDPSLGVVRH ADAGYERARE
     AARALGIRMP MLGR
//

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