TRHO_PROMS
ID TRHO_PROMS Reviewed; 310 AA.
AC A2BRS3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=A9601_12001;
OS Prochlorococcus marinus (strain AS9601).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=146891;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS9601;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000551; ABM70484.1; -; Genomic_DNA.
DR RefSeq; WP_011818631.1; NC_008816.1.
DR AlphaFoldDB; A2BRS3; -.
DR SMR; A2BRS3; -.
DR STRING; 146891.A9601_12001; -.
DR EnsemblBacteria; ABM70484; ABM70484; A9601_12001.
DR KEGG; pmb:A9601_12001; -.
DR eggNOG; COG1054; Bacteria.
DR HOGENOM; CLU_038878_0_0_3; -.
DR OMA; CDTHTNC; -.
DR OrthoDB; 684577at2; -.
DR Proteomes; UP000002590; 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; IPR020936; TrhO.
DR InterPro; IPR040503; TRHO_N.
DR PANTHER; PTHR43268; PTHR43268; 1.
DR Pfam; PF00581; Rhodanese; 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; tRNA processing.
FT CHAIN 1..310
FT /note="tRNA uridine(34) hydroxylase"
FT /id="PRO_1000013757"
FT DOMAIN 127..225
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
FT ACT_SITE 185
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00469"
SQ SEQUENCE 310 AA; 36001 MW; 83D80F859627EE14 CRC64;
MKGKNYKITS LYSFFPFQEN LIFDLKNKLL EIENENDLSG LLIFASEGIN GTICAEKNVI
DIVINLIKEY TDSRNLNIKV NFSKKKVFKK LKIKIKKEIV TMGVPEINPS ENNGTYIDSA
GWNKLIKNQN TIVIDTRNHY EISVGTFQNS INPNTRNFSE FPKWVDDHLN THLENKDSTN
IAMFCTGGIR CEKATSLLKK KGYKNIYHLK GGILQYLDDI PKKENLFEGE CYVFDKRVAL
DQELEKGSYS ICHACGMPIS IQDQKRKEYR KGIQCHFCID QFSDNDRKRF EERQKQIDRL
KVENNKINKD