AC   MF_04028;
DC   Protein; auto
TR   HAMAP; MF_04028; -; 1; level=0
XX
Names: HSV_RIR2
XX
ID   RIR2
DE   RecName: Full=Ribonucleoside-diphosphate reductase small subunit;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase small subunit;
GN   Name=RIR2;
XX
CC   -!- FUNCTION: Ribonucleoside-diphosphate reductase holoenzyme provides the
CC       precursors necessary for viral DNA synthesis. Allows virus growth in
CC       non-dividing cells, as well as reactivation from latency in infected
CC       hosts. Catalyzes the biosynthesis of deoxyribonucleotides from the
CC       corresponding ribonucleotides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC         diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC         diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- SUBUNIT: Heterotetramer composed of a homodimer of the large subunit
CC       (R1) and a homodimer of the small subunit (R2). Larger multisubunit
CC       protein complex are also active, composed of (R1)n(R2)n.
case <Feature:Transmembrane==1>
CC   -!- SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein.
end case
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC       chain family.
XX
DR   PROSITE; PS00368; RIBORED_SMALL; 1; trigger=no
DR   Pfam; PF00268; Ribonuc_red_sm; 1; trigger=no
DR   General; Transmembrane; -; 0-1; trigger=yes
XX
KW   Iron
KW   Metal-binding
KW   Oxidoreductase
case <Feature:Transmembrane==1>
KW   Host membrane
KW   Membrane
KW   Transmembrane
KW   Transmembrane helix
end case
XX
case <Feature:Transmembrane==1>
GO   GO:0033644; C:host cell membrane
GO   GO:0016020; C:membrane
end case
GO   GO:0046872; F:metal ion binding
GO   GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO   GO:0009186; P:deoxyribonucleoside diphosphate metabolic process
XX
FT   From: RIR2_EBVG (P0C701)
FT   ACT_SITE        98
FT   Condition: Y
FT   BINDING         61
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: [ED]
FT   BINDING         91
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         91
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT   Condition: H
FT   BINDING         154
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         188
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: E
FT   BINDING         191
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT   Condition: H
XX
Size: 302-343;
Related: None;
Template: P0C701;
Scope:
 Viruses; Herpesviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.10 2023/10/16
//