HUTU_MOUSE
ID HUTU_MOUSE Reviewed; 676 AA.
AC Q8VC12; E9QNN2;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Urocanate hydratase;
DE Short=Urocanase;
DE EC=4.2.1.49;
DE AltName: Full=Imidazolonepropionate hydrolase;
GN Name=Uroc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-534, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
CC -!- SIMILARITY: Belongs to the urocanase family. {ECO:0000305}.
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DR EMBL; AC122521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022133; AAH22133.1; -; mRNA.
DR CCDS; CCDS39561.1; -.
DR RefSeq; NP_659189.2; NM_144940.2.
DR AlphaFoldDB; Q8VC12; -.
DR SMR; Q8VC12; -.
DR STRING; 10090.ENSMUSP00000127114; -.
DR iPTMnet; Q8VC12; -.
DR PhosphoSitePlus; Q8VC12; -.
DR SwissPalm; Q8VC12; -.
DR jPOST; Q8VC12; -.
DR MaxQB; Q8VC12; -.
DR PaxDb; Q8VC12; -.
DR PRIDE; Q8VC12; -.
DR ProteomicsDB; 267072; -.
DR Antibodypedia; 52455; 72 antibodies from 17 providers.
DR DNASU; 243537; -.
DR Ensembl; ENSMUST00000046128; ENSMUSP00000040424; ENSMUSG00000034456.
DR GeneID; 243537; -.
DR KEGG; mmu:243537; -.
DR UCSC; uc009cxc.2; mouse.
DR CTD; 131669; -.
DR MGI; MGI:2385332; Uroc1.
DR VEuPathDB; HostDB:ENSMUSG00000034456; -.
DR eggNOG; ENOG502QR75; Eukaryota.
DR GeneTree; ENSGT00390000015136; -.
DR HOGENOM; CLU_018868_3_0_1; -.
DR InParanoid; Q8VC12; -.
DR Reactome; R-MMU-70921; Histidine catabolism.
DR UniPathway; UPA00379; UER00550.
DR BioGRID-ORCS; 243537; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8VC12; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VC12; protein.
DR Bgee; ENSMUSG00000034456; Expressed in left lobe of liver and 34 other tissues.
DR ExpressionAtlas; Q8VC12; baseline and differential.
DR Genevisible; Q8VC12; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016153; F:urocanate hydratase activity; ISO:MGI.
DR GO; GO:0006548; P:histidine catabolic process; ISO:MGI.
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 1: Evidence at protein level;
KW Histidine metabolism; Lyase; NAD; Reference proteome.
FT CHAIN 1..676
FT /note="Urocanate hydratase"
FT /id="PRO_0000207375"
FT BINDING 126..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT BINDING 251..253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT BINDING 271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT BINDING 317..318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT BINDING 343..347
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT BINDING 354..355
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT BINDING 403
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT BINDING 594
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P25503"
FT MOD_RES 534
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 295
FT /note="R -> H (in Ref. 2; AAH22133)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="H -> R (in Ref. 2; AAH22133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 74590 MW; 097A6CADE3573C64 CRC64;
MSSLQELCSG LPLRPLPENR GRWAGVPHAP VRTPNLSPEE EQLALRNALR YFPPDVQKLL
ALEFAQELRQ FGHIYMYRFC PSIEMRAYPI DQYPCRTRAA AAIMHMIMNN LDPAVAQFPQ
ELVTYGGNGQ VFSNWAQFRL TMSYLSKMTE EQTLVMYSGH PLGLFPSSPR APRLVITNGM
VIPNYSSRTE YEKLFALGVT MYGQMTAGSY CYIGPQGIVH GTVLTVLNAG RRYLGIENLA
GKVFVTSGLG GMSGAQAKAA AIVGCIGVIA EVDKAALVKR HRQGWLMEVT DSLDRCIARL
REARKKKEVL SLGYHGNVVD LWERLVHELD TTGELLVDLG SDQTSCHNPF NGGYYPVQLS
FSEAQSLMSS NPAAFKHLVQ ESLRRHVAAI NRLAQEKFFF WDYGNAFLLE AQRAGADVEK
KGANKMEFRY PSYVQHIMGD IFSQGFGPFR WVCTSGDPQD LAVTDHLATS VLEKAIADGV
KASVKLQYMD NIRWIREAAK HQLVVGSQAR ILYSDQKGRV AIAVAINQAI ASGKIKAPVV
LSRDHHDVSG TDSPFRETSN IYDGSAFCAD MAVQNFVGDA CRGATWVALH NGGGVGWGEV
INGGFGLVLD GTAEAEQKAR MMLSWDVSNG VARRCWSGNP KAYEIICQTM QENSGLVVTL
PHEVADEQVL QQALRP
