(data stored in ACNUC1104 zone)

SWISSPROT: E6V092_VARPE

ID   E6V092_VARPE            Unreviewed;       575 AA.
AC   E6V092;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Urocanate hydratase {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693702};
DE            Short=Urocanase {ECO:0000256|HAMAP-Rule:MF_00577};
DE            EC=4.2.1.49 {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693702};
DE   AltName: Full=Imidazolonepropionate hydrolase {ECO:0000256|HAMAP-Rule:MF_00577};
GN   Name=hutU {ECO:0000256|HAMAP-Rule:MF_00577};
GN   OrderedLocusNames=Varpa_0184 {ECO:0000313|EMBL:ADU34406.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34406.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34406.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34406.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- FUNCTION: Catalyzes the conversion of urocanate to 4-imidazolone-
CC       5-propionate. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00577, ECO:0000256|SAAS:SAAS01115074};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00577};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693692}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00577}.
CC   -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00577, ECO:0000256|SAAS:SAAS00693689}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00577}.
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DR   EMBL; CP002417; ADU34406.1; -; Genomic_DNA.
DR   RefSeq; WP_013538653.1; NC_014931.1.
DR   STRING; 595537.Varpa_0184; -.
DR   EnsemblBacteria; ADU34406; ADU34406; Varpa_0184.
DR   GeneID; 29717656; -.
DR   KEGG; vpe:Varpa_0184; -.
DR   eggNOG; ENOG4105CGP; Bacteria.
DR   eggNOG; COG2987; LUCA.
DR   HOGENOM; HOG000237606; -.
DR   KO; K01712; -.
DR   OMA; VSFHHGG; -.
DR   OrthoDB; 100619at2; -.
DR   BioCyc; VPAR595537:G1GQO-185-MONOMER; -.
DR   UniPathway; UPA00379; UER00550.
DR   Proteomes; UP000008917; 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; E6V092.
DR   SWISS-2DPAGE; E6V092.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00577};
KW   Histidine metabolism {ECO:0000256|HAMAP-Rule:MF_00577,
KW   ECO:0000256|SAAS:SAAS00693681};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693676,
KW   ECO:0000313|EMBL:ADU34406.1};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00577, ECO:0000256|SAAS:SAAS00693683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917}.
FT   DOMAIN       25    151       Urocanase_N. {ECO:0000259|Pfam:PF17391}.
FT   DOMAIN      154    368       Urocanase. {ECO:0000259|Pfam:PF01175}.
FT   DOMAIN      371    565       Urocanase_C. {ECO:0000259|Pfam:PF17392}.
FT   NP_BIND      66     67       NAD. {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   NP_BIND     190    192       NAD. {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   NP_BIND     256    257       NAD. {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   NP_BIND     281    285       NAD. {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   NP_BIND     291    292       NAD. {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   ACT_SITE    430    430       {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   BINDING     144    144       NAD. {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   BINDING     210    210       NAD. {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   BINDING     342    342       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00577}.
FT   BINDING     512    512       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00577}.
SQ   SEQUENCE   575 AA;  62967 MW;  EB2ADFD2A9199813 CRC64;
     MNAPEKFALN NPDAADPRHD PTRVIRAPRG SELNCKSWLT EAPFRMLQNN LDAEVAERPQ
     DLVVYGGIGR AARNWECYDQ ILASLKELND DETLLIQSGK PVGVFKTHEN APRVLLANSN
     LVPKWGTWEH FNELDRKGLF MYGQMTAGSW IYIGSQGIVQ GTFETFVEAG RQHYNNSLAG
     KWILTAGLGG MGGAQPLAAT LAGAVSLNIE CQQSSIDFRL RTRYVDKQAR DIDHAFELIK
     QHCDAKEAVS IALLGNAADI LPELVKRAKA GAHKPDLVTD QTSAHDLING YLPSGWTVQQ
     WQAAMKDVSQ HDALKKAAAK SCAVHVQAML DFQSMGIPTV DYGNNIRQVA FDEGVKNAFD
     FPGFVPAYIR PLFCEGKGPF RWVALSGDPE DIYKTDAKIK ELFPENTHTH RWLDMARERI
     AFQGLPARIC WLGLGERHIA GLAFNEMVKN GELKAPIVIG RDHLDTGSVA SPNRETEAMK
     DGTDAVSDWP LLNALLNTAG GATWVSLHHG GGVGMGYSQH SGVVIVCDGT DAAAKRIERV
     LFNDPATGVM RHADAGYDIA IATAKKQGLK LPMVR
//

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