ID   DUHM_BPSP1              Reviewed;         383 AA.
AC   P31654; B6V2J2;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Deoxyuridylate hydroxymethyltransferase;
DE            Short=Deoxyuridylate hydroxymethylase;
DE            EC=2.1.2.- {ECO:0000269|PubMed:1641983, ECO:0000269|PubMed:8527927};
DE   AltName: Full=Gp29;
DE   AltName: Full=dUMP hydroxymethylase {ECO:0000250|UniProtKB:P0DTK3};
DE            Short=dUMP-HMase {ECO:0000305};
OS   Bacillus phage SP01 (Bacteriophage SP01).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Herelleviridae; Spounavirinae; Okubovirus.
OX   NCBI_TaxID=10685;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=WT;
RX   PubMed=1641983; DOI=10.1016/0042-6822(92)90587-f;
RA   Wilhelm K., Rueger W.;
RT   "Deoxyuridylate-hydroxymethylase of bacteriophage SPO1.";
RL   Virology 189:640-646(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19285085; DOI=10.1016/j.jmb.2009.03.009;
RA   Stewart C.R., Casjens S.R., Cresawn S.G., Houtz J.M., Smith A.L.,
RA   Ford M.E., Peebles C.L., Hatfull G.F., Hendrix R.W., Huang W.M.,
RA   Pedulla M.L.;
RT   "The genome of Bacillus subtilis bacteriophage SPO1.";
RL   J. Mol. Biol. 388:48-70(2009).
RN   [3]
RP   FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX   PubMed=8527927; DOI=10.1006/prep.1995.1057;
RA   Schellenberger U., Livi L.L., Santi D.V.;
RT   "Cloning, expression, purification, and characterization of 2'-
RT   deoxyuridylate hydroxymethylase from phage SPO1.";
RL   Protein Expr. Purif. 6:423-430(1995).
RN   [4]
RP   FUNCTION.
RX   PubMed=21597187; DOI=10.1271/bbb.100921;
RA   Yee L.M., Matsumoto T., Yano K., Matsuoka S., Sadaie Y., Yoshikawa H.,
RA   Asai K.;
RT   "The genome of Bacillus subtilis phage SP10: a comparative analysis with
RT   phage SPO1.";
RL   Biosci. Biotechnol. Biochem. 75:944-952(2011).
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:8527927). As a final
CC       result of the pathway of hypermodification, hydroxymethyluracil
CC       substitutes for a subset of thymidines in the viral DNA
CC       (PubMed:8527927). These modifications probably prevent degradation of
CC       viral DNA by the host restriction-modification antiviral defense system
CC       (PubMed:8527927, PubMed:21597187). {ECO:0000269|PubMed:21597187,
CC       ECO:0000269|PubMed:8527927}.
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:1641983, ECO:0000269|PubMed:8527927};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8527927}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR   EMBL; X60728; CAA43136.1; -; Genomic_DNA.
DR   EMBL; FJ230960; ACI91041.1; -; Genomic_DNA.
DR   PIR; A42992; SZBPSP.
DR   RefSeq; YP_002300412.1; NC_011421.1.
DR   SMR; P31654; -.
DR   GeneID; 7009130; -.
DR   KEGG; vg:7009130; -.
DR   Proteomes; UP000001590; Genome.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IDA:CACAO.
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..383
FT                   /note="Deoxyuridylate hydroxymethyltransferase"
FT                   /id="PRO_0000141070"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255"
FT   CONFLICT        8
FT                   /note="K -> N (in Ref. 2; ACI91041)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301
FT                   /note="C -> S (in Ref. 2; ACI91041)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="E -> V (in Ref. 2; ACI91041)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="I -> V (in Ref. 2; ACI91041)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   383 AA;  44615 MW;  619E6D05CD8F8C4D CRC64;
     MYTFSGSKPT QLYMDILSTV IKEGDVLAPR GKRIKEIRPV MIEFKNPIRR TTFLKGRNIN
     PFFQVAESLW ILAGRSDVGF LLDYNKNMGQ FSDDGVFFNA PYGERLRFWN RSDANNFIYN
     PLDQLRDVYE KIKADPDTRQ AVAVIYNPLF DNINNDTKDR PCNLLLSFKL RNGKLDLSVY
     NRSNDLHWGT FGANLCQFST ILEAMATWLG VEVGSYYQIT DSLHVYLDDY GAKITEDIQK
     VYGVNLETDE APVVEDFEEL LDPNPRMSYT MNELNQFLNE YFGIVDSLMR DDETYMHDGD
     CAQMLLNQIR HEPDEYIKVT LLLMVAKQAL NRGMKDTVAT AMNWIPLCEI KVSALRFLYK
     SYPEYINQYD LDEKLMKYIR REE