DUHM_BPPM6
ID DUHM_BPPM6 Reviewed; 351 AA.
AC P0DTK3;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 1.
DT 03-AUG-2022, entry version 1.
DE RecName: Full=Deoxyuridylate hydroxymethyltransferase {ECO:0000305};
DE Short=Deoxyuridylate hydroxymethylase {ECO:0000305};
DE EC=2.1.2.- {ECO:0000269|PubMed:34522950};
DE AltName: Full=dUMP hydroxymethylase {ECO:0000303|PubMed:34522950};
DE Short=dUMP-HMase {ECO:0000305};
DE AltName: Full=gp58 {ECO:0000303|PubMed:34522950};
OS Pseudomonas phage M6.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Yuavirus.
OX NCBI_TaxID=2911432;
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16428425; DOI=10.1128/jb.188.3.1184-1187.2006;
RA Kwan T., Liu J., Dubow M., Gros P., Pelletier J.;
RT "Comparative genomic analysis of 18 Pseudomonas aeruginosa
RT bacteriophages.";
RL J. Bacteriol. 188:1184-1187(2006).
RN [2]
RP FUNCTION.
RX PubMed=29555775; DOI=10.1073/pnas.1714812115;
RA Lee Y.J., Dai N., Walsh S.E., Mueller S., Fraser M.E., Kauffman K.M.,
RA Guan C., Correa I.R. Jr., Weigele P.R.;
RT "Identification and biosynthesis of thymidine hypermodifications in the
RT genomic DNA of widespread bacterial viruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E3116-E3125(2018).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=34522950; DOI=10.1093/nar/gkab781;
RA Lee Y.J., Dai N., Mueller S.I., Guan C., Parker M.J., Fraser M.E.,
RA Walsh S.E., Sridar J., Mulholland A., Nayak K., Sun Z., Lin Y.C.,
RA Comb D.G., Marks K., Gonzalez R., Dowling D.P., Bandarian V., Saleh L.,
RA Correa I.R., Weigele P.R.;
RT "Pathways of thymidine hypermodification.";
RL Nucleic Acids Res. 0:0-0(2021).
CC -!- FUNCTION: Catalyzes formation of 5-hydroxymethyldeoxyuridylate
CC (5HMdUMP) as a step in the pathway that replaces dTMP by thymidine
CC hypermodifications in the viral genome (PubMed:34522950). As a final
CC result of the pathway of hypermodification, 5-aminoethyl-2'-
CC deoxyuridine (5-NedU) substitutes for about 30% of thymidines in the
CC viral DNA (PubMed:34522950, PubMed:29555775). These modifications
CC probably prevent degradation of viral genome by the host restriction-
CC modification antiviral defense system (PubMed:34522950).
CC {ECO:0000269|PubMed:29555775, ECO:0000269|PubMed:34522950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + 5-hydroxymethyl-dUMP;
CC Xref=Rhea:RHEA:48424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:90409, ChEBI:CHEBI:246422;
CC Evidence={ECO:0000269|PubMed:34522950};
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ163916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; YP_001294566.1; NC_007809.1.
PE 1: Evidence at protein level;
KW Host-virus interaction; Methyltransferase;
KW Restriction-modification system evasion by virus; Transferase.
FT CHAIN 1..351
FT /note="Deoxyuridylate hydroxymethyltransferase"
FT /id="PRO_0000456263"
SQ SEQUENCE 351 AA; 40200 MW; 7EBD9B3E7528D2AB CRC64;
MKVIKTRNVQ QALPEALYQL SFEGVRRDSR NGPVFMFPEP VTTVYLRPAE RVLFWAERDA
NPFFHLMESL WMLGGRNDVE YVARFVDRMR SYSDDGLTFH GAYGFRWRQH FFEDQLPKII
AALKENRDDR RQVLSMWDAD ADLGRQGKDL PCNLQAIFQI ACDGRLDMTV TNRSNDLIWG
AYGANAVHFS YLHEYVARSV GVEQGIYRQV SANFHAYEEV LNKVAPLADL AANPMTGTET
PDPYAAGIAE PYPLMSTDPE EWNQELMMFL SEPDAVGFRD PFFRRVAIPM MKAHKAFKQT
SNPSRFDAAL AELDNVAATD WKLAGVEWIE RRRAAFEARK ARAMDDGVAY E
