ID   DUHM_BPW14              Reviewed;         357 AA.
AC   C9DGK1;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 33.
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};
GN   Name=230 {ECO:0000312|EMBL:ACV50252.1};
OS   Delftia phage PhiW-14 (Deftia acidovorans bacteriophage phiW-14).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Ionavirus; Delftia virus PhiW14.
OX   NCBI_TaxID=665032;
OH   NCBI_TaxID=80866; Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kropinski A.M., Villegas A., Lingohr E.J.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=7373713; DOI=10.1128/jvi.34.2.347-353.1980;
RA   Neuhard J., Maltman K.L., Warren R.A.;
RT   "Bacteriophage phi W-14-infected Pseudomonas acidovorans synthesizes
RT   hydroxymethyldeoxyuridine triphosphate.";
RL   J. Virol. 34:347-353(1980).
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 (Probable). As a final result of
CC       the pathway of hypermodification, 5-Nalpha-putrescinylthymidine
CC       (Nalpha-PutT) substitutes for about 50% of thymidines in the viral DNA
CC       (Probable). These modifications probably prevent degradation of viral
CC       genome by the host restriction-modification antiviral defense system
CC       (Probable). {ECO:0000305|PubMed:34522950, ECO:0000305|PubMed:7373713}.
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   -!- INDUCTION: Hydroxymethylase appears immediately after infection.
CC       {ECO:0000269|PubMed:7373713}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR   EMBL; GQ357915; ACV50252.1; -; Genomic_DNA.
DR   RefSeq; YP_003359084.1; NC_013697.1.
DR   GeneID; 8684178; -.
DR   KEGG; vg:8684178; -.
DR   Proteomes; UP000008986; Genome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.572.10; -; 1.
DR   InterPro; IPR045097; Thymidate_synth/dCMP_Mease.
DR   InterPro; IPR023451; Thymidate_synth/dCMP_Mease_dom.
DR   InterPro; IPR036926; Thymidate_synth/dCMP_Mease_sf.
DR   PANTHER; PTHR11548; PTHR11548; 1.
DR   Pfam; PF00303; Thymidylat_synt; 1.
DR   SUPFAM; SSF55831; SSF55831; 1.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Methyltransferase; Reference proteome;
KW   Restriction-modification system evasion by virus; Transferase.
FT   CHAIN           1..357
FT                   /note="Deoxyuridylate hydroxymethyltransferase"
FT                   /id="PRO_0000456264"
SQ   SEQUENCE   357 AA;  40126 MW;  ECBCC881DC376FFB CRC64;
     MNPFNIISDT GVSAAVYAGL SRAKCTGQYK ECRNGGSTFL RNVKFHITDP RNRNLTLNGR
     KSNIFQMVAE TFWVMSGSGN IKEFLEFFLP RAPQYSDDGI NWHGAYGPRM YAHNQLQSAI
     DLLIKDKDTR RAYVMIADPT LDSAPAIEAA YGVGHSPKDV PCNREIHINI IEDKLCMKVI
     QRSGDMLFGT GSINPFEFTF LQELLSEATG YALGDYQWDV TDAHYYKAFE DQVNDVLRSE
     QTFWPNDGKP LGTRFTSATK MQEFFAGVVR VWVKQINRLI DLGDAHYAIN DLFADYGVLP
     EGRLRDYAKM VTFYIAAKQG EIEGDFKALL TNIPTNTDLG QAILTSPFRK FGVVLGD