DCHM_BPT4
ID DCHM_BPT4 Reviewed; 246 AA.
AC P08773;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 23-FEB-2022, entry version 127.
DE RecName: Full=Deoxycytidylate 5-hydroxymethyltransferase;
DE Short=Deoxycytidylate hydroxymethylase;
DE EC=2.1.2.8;
DE AltName: Full=dCMP hydroxymethylase;
DE Short=dCMP HMase;
GN Name=42;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W;
RX PubMed=3295783; DOI=10.1093/nar/15.9.3920;
RA Lamm N., Tomaschewski J., Rueger W.;
RT "Nucleotide sequence of the deoxycytidylate hydroxymethylase gene of
RT bacteriophage T4 (g42) and the homology of its gene product with
RT thymidylate synthase of E. coli.";
RL Nucleic Acids Res. 15:3920-3920(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3350013; DOI=10.1111/j.1432-1033.1988.tb13925.x;
RA Lamm N., Wang Y., Mathews C.K., Rueger W.;
RT "Deoxycytidylate hydroxymethylase gene of bacteriophage T4. Nucleotide
RT sequence determination and over-expression of the gene.";
RL Eur. J. Biochem. 172:553-563(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-186 AND 225-246.
RX PubMed=2832395; DOI=10.1128/jb.170.4.1994-1998.1988;
RA Thylen C.;
RT "Expression and DNA sequence of the cloned bacteriophage T4 dCMP
RT hydroxymethylase gene.";
RL J. Bacteriol. 170:1994-1998(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 226-246.
RX PubMed=2999696; DOI=10.1093/nar/13.21.7551;
RA Tomaschewski J., Gram H., Crabb J.W., Rueger W.;
RT "T4-induced alpha- and beta-glucosyltransferase: cloning of the genes and a
RT comparison of their products based on sequencing data.";
RL Nucleic Acids Res. 13:7551-7568(1985).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dCMP + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + 5-hydroxymethyl-dCMP;
CC Xref=Rhea:RHEA:11280, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57566, ChEBI:CHEBI:57962; EC=2.1.2.8;
CC -!- SIMILARITY: Belongs to the thymidylate synthase family. {ECO:0000305}.
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DR EMBL; Y00148; CAA68342.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42467.1; -; Genomic_DNA.
DR EMBL; M22767; AAA88468.1; -; Genomic_DNA.
DR EMBL; M22766; AAA88467.1; -; Genomic_DNA.
DR EMBL; M37159; AAA21709.1; -; Genomic_DNA.
DR EMBL; X03139; CAA26907.1; -; Genomic_DNA.
DR PIR; JS0786; SZBPT4.
DR RefSeq; NP_049659.1; NC_000866.4.
DR PDB; 1B49; X-ray; 2.30 A; A/C=1-246.
DR PDB; 1B5D; X-ray; 2.20 A; A/B=1-246.
DR PDB; 1B5E; X-ray; 1.60 A; A/B=1-246.
DR PDB; 6A9A; X-ray; 1.90 A; A=1-246.
DR PDB; 6A9B; X-ray; 2.01 A; A=1-246.
DR PDB; 6L18; X-ray; 1.90 A; A=1-246.
DR PDBsum; 1B49; -.
DR PDBsum; 1B5D; -.
DR PDBsum; 1B5E; -.
DR PDBsum; 6A9A; -.
DR PDBsum; 6A9B; -.
DR PDBsum; 6L18; -.
DR SMR; P08773; -.
DR DrugBank; DB03798; 2'-Deoxycytidine-5'-Monophosphate.
DR GeneID; 1258746; -.
DR KEGG; vg:1258746; -.
DR BRENDA; 2.1.2.8; 732.
DR EvolutionaryTrace; P08773; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0047153; F:deoxycytidylate 5-hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.572.10; -; 1.
DR InterPro; IPR014619; Deoxycytidylate_hydroxyMease.
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 PIRSF; PIRSF036750; dCMP_HMase; 1.
DR SUPFAM; SSF55831; SSF55831; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..246
FT /note="Deoxycytidylate 5-hydroxymethyltransferase"
FT /id="PRO_0000141068"
FT ACT_SITE 148
FT /evidence="ECO:0000255"
FT CONFLICT 164
FT /note="V -> L (in Ref. 4; AAA88467)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:6A9A"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:1B5E"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1B49"
FT STRAND 32..42
FT /evidence="ECO:0007829|PDB:1B5E"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1B5E"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 96..101
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1B5E"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1B5E"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:1B5E"
FT STRAND 160..171
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 174..197
FT /evidence="ECO:0007829|PDB:1B5E"
FT STRAND 204..218
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:1B5E"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:1B5E"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1B5E"
SQ SEQUENCE 246 AA; 28489 MW; 36F1C4EE23B51E8E CRC64;
MISDSMTVEE IRLHLGLALK EKDFVVDKTG VKTIEIIGAS FVADEPFIFG ALNDEYIQRE
LEWYKSKSLF VKDIPGETPK IWQQVASSKG EINSNYGWAI WSEDNYAQYD MCLAELGQNP
DSRRGIMIYT RPSMQFDYNK DGMSDFMCTN TVQYLIRDKK INAVVNMRSN DVVFGFRNDY
AWQKYVLDKL VSDLNAGDST RQYKAGSIIW NVGSLHVYSR HFYLVDHWWK TGETHISKKD
YVGKYA
