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HUTU_CAEEL
ID   HUTU_CAEEL              Reviewed;         670 AA.
AC   Q9NAE2;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable urocanate hydratase;
DE            Short=Urocanase;
DE            EC=4.2.1.49;
DE   AltName: Full=Imidazolonepropionate hydrolase;
GN   ORFNames=Y51H4A.7;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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; AL132952; CAB61139.2; -; Genomic_DNA.
DR   RefSeq; NP_502964.2; NM_070563.4.
DR   AlphaFoldDB; Q9NAE2; -.
DR   SMR; Q9NAE2; -.
DR   BioGRID; 43538; 13.
DR   STRING; 6239.Y51H4A.7.1; -.
DR   EPD; Q9NAE2; -.
DR   PaxDb; Q9NAE2; -.
DR   PeptideAtlas; Q9NAE2; -.
DR   EnsemblMetazoa; Y51H4A.7.1; Y51H4A.7.1; WBGene00013103.
DR   EnsemblMetazoa; Y51H4A.7.2; Y51H4A.7.2; WBGene00013103.
DR   UCSC; Y51H4A.7.1; c. elegans.
DR   WormBase; Y51H4A.7; CE35671; WBGene00013103; -.
DR   eggNOG; ENOG502QR75; Eukaryota.
DR   GeneTree; ENSGT00390000015136; -.
DR   HOGENOM; CLU_018868_3_0_1; -.
DR   InParanoid; Q9NAE2; -.
DR   OMA; LVGDWAN; -.
DR   OrthoDB; 536177at2759; -.
DR   PhylomeDB; Q9NAE2; -.
DR   Reactome; R-CEL-70921; Histidine catabolism.
DR   UniPathway; UPA00379; UER00550.
DR   PRO; PR:Q9NAE2; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00013103; Expressed in larva and 3 other tissues.
DR   GO; GO:0016153; F:urocanate hydratase activity; IBA:GO_Central.
DR   GO; GO:0006548; P:histidine catabolic process; IBA:GO_Central.
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   PROSITE; PS01233; UROCANASE; 1.
PE   3: Inferred from homology;
KW   Histidine metabolism; Lyase; NAD; Reference proteome.
FT   CHAIN           1..670
FT                   /note="Probable urocanate hydratase"
FT                   /id="PRO_0000207376"
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         250..252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         270
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         316..317
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         338..342
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         349..350
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         398
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
FT   BINDING         590
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P25503"
SQ   SEQUENCE   670 AA;  74407 MW;  C0BFBFE972DBAFDC CRC64;
     MNIPSLFVDP FSPLLEHPTE QRAKNVAHAP KRPCNLTQTE KMLAVRNALR YIPKEHHVLL
     ATEFAEELNT YGHIYGYRFM PNFDLFAPPV SEIGAHCEQA SAIILMILNN LDKRVAQFPQ
     ELVTYGGNGQ VFSNWIQFRL VLRYLYTMTD HQTLVLYSGH PLGLFPSTPD SPRMTVTNGM
     MIPSYSTKEL YDKYFALGVT QYGQMTAGSF CYIGPQGIVH GTTITVLNAG RRMGLDSLAG
     KVFVTAGLGG MSGAQPKAAK IAGCIGVIAE ISDTALLKRH QQGWLDVYSK DLEEIVNWIK
     EYREKKEAIS IGYLGNVVDL WERLAEEPEC LVELGSDQTS LHNPFLGGFY PAGLTFEQSN
     QMMTSDPVKF KKLVQNSLIR QIAAIDKIAA KGMYFWDYGN AFLLECQRAG ANLLREDAQD
     DKSFRYPSYM QDIMGDIFSM GFGPFRWVCT SGKPEDLRLT DQTACKIIDE LKDTDVPEYV
     KQQYLDNKKW IEEAEKNKLV VGSQARILYS DRAGRVALAS AFNELVKSGK VSAAIVISRD
     HHDVSGTDSP FRETSNVYDG SAFTADMAVQ NCIGDSFRGA TWVALHNGGG VGWGDVINGG
     FGIVLDGSSD AARRAEGMLN WDVPNGVTRR SWSGNAKAQE AIQRAEKQVD GLRVTLPVEA
     DEELLKKLKF
 
 
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