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TRHO_BUCAI
ID   TRHO_BUCAI              Reviewed;         324 AA.
AC   P57446;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=tRNA uridine(34) hydroxylase {ECO:0000255|HAMAP-Rule:MF_00469};
DE            EC=1.14.-.- {ECO:0000255|HAMAP-Rule:MF_00469};
DE   AltName: Full=tRNA hydroxylation protein O {ECO:0000255|HAMAP-Rule:MF_00469};
GN   Name=trhO {ECO:0000255|HAMAP-Rule:MF_00469}; OrderedLocusNames=BU365;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U)
CC       modification at position 34 in tRNAs. {ECO:0000255|HAMAP-
CC       Rule:MF_00469}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + O2 + uridine(34) in tRNA = 5-hydroxyuridine(34) in tRNA
CC         + A + H2O; Xref=Rhea:RHEA:64224, Rhea:RHEA-COMP:11727, Rhea:RHEA-
CC         COMP:13381, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:65315, ChEBI:CHEBI:136877;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00469};
CC   -!- SIMILARITY: Belongs to the TrhO family. {ECO:0000255|HAMAP-
CC       Rule:MF_00469}.
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DR   EMBL; BA000003; BAB13069.1; -; Genomic_DNA.
DR   RefSeq; NP_240183.1; NC_002528.1.
DR   RefSeq; WP_010896087.1; NC_002528.1.
DR   AlphaFoldDB; P57446; -.
DR   SMR; P57446; -.
DR   STRING; 107806.10039035; -.
DR   EnsemblBacteria; BAB13069; BAB13069; BAB13069.
DR   KEGG; buc:BU365; -.
DR   PATRIC; fig|107806.10.peg.379; -.
DR   eggNOG; COG1054; Bacteria.
DR   HOGENOM; CLU_038878_1_1_6; -.
DR   OMA; CDTHTNC; -.
DR   BioCyc; BAPH107806:GBZJ-358-MON; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProtKB-UniRule.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.250.10; -; 1.
DR   HAMAP; MF_00469; TrhO; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR022111; Rhodanese_C.
DR   InterPro; IPR020936; TrhO.
DR   InterPro; IPR040503; TRHO_N.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF12368; Rhodanese_C; 1.
DR   Pfam; PF17773; UPF0176_N; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome; tRNA processing.
FT   CHAIN           1..324
FT                   /note="tRNA uridine(34) hydroxylase"
FT                   /id="PRO_0000161455"
FT   DOMAIN          145..239
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT   ACT_SITE        199
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ   SEQUENCE   324 AA;  38405 MW;  9E7B019857D377FA CRC64;
     MSILHNIVSK KELKRRMFFE TEPRLTLSFY KYFFIKNTQE YRDRLYKTFY KYNVLGRIYV
     ASEGINAQIS VPKKYYSILK KFLYNFDIEL NNLRINKSLD NEKSFWVLCV KIKKKIVQDG
     IKEHFFNPNN VGIYIQSEQV NSMLNDKKTI FIDMRNSYEY AIGHFENAIE IKSITFREQL
     KKVIQLMAYA KNKKIVMYCT GGIRCEKATS WMLFNGFKHV YHLEGGIIGY VHDARKNGLP
     VLFKGKSFVF DNRMSEKISD EVISYCKQCG KSSDVYINCK YSSCHLLFIQ CENCSVKFHS
     CCSLECMKKY KFYMLNNDLK KISY
 
 
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