AC   MF_04026;
DC   Protein; auto
TR   HAMAP; MF_04026; -; 1; level=0
XX
Names: HSV_RIR1
XX
ID   RIR1
DE   RecName: Full=Ribonucleoside-diphosphate reductase large subunit;
DE            Short=R1;
DE            EC=1.17.4.1;
DE   AltName: Full=Ribonucleotide reductase large subunit;
GN   Name=RIR1;
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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   -!- 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.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC       chain family.
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DR   PROSITE; PS00089; RIBORED_LARGE; 1; trigger=no
DR   Pfam; PF02867; Ribonuc_red_lgC; 1; trigger=no
DR   Pfam; PF00317; Ribonuc_red_lgN; 1; trigger=no
DR   PRINTS; PR01183; RIBORDTASEM1; 1; trigger=no
DR   NCBIfam; TIGR02506; NrdE_NrdA; 1; trigger=no
XX
KW   ATP-binding
KW   Disulfide bond
KW   Early protein
KW   Nucleotide-binding
KW   Oxidoreductase
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GO   GO:0005524; F:ATP binding
GO   GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO   GO:0016032; P:viral process
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FT   From: RIR1_HHV11 (P08543)
FT   BINDING         581..582
FT                   /ligand="substrate"
FT   Condition: S-C
FT   BINDING         791..795
FT                   /ligand="substrate"
FT   Condition: N-L-C-[TA]-E
FT   BINDING         968..972
FT                   /ligand="substrate"
FT   Condition: P-T-x-x-[SCT]
FT   ACT_SITE        791
FT                   /note="Proton acceptor"
FT   Condition: N
FT   ACT_SITE        793
FT                   /note="Cysteine radical intermediate"
FT   Condition: C
FT   ACT_SITE        795
FT                   /note="Proton acceptor"
FT   Condition: E
FT   BINDING         566
FT                   /ligand="substrate"
FT   Condition: T
FT   BINDING         612
FT                   /ligand="substrate"
FT   Condition: G
FT   SITE            582
FT                   /note="Important for hydrogen atom transfer"
FT   Condition: C
FT   SITE            808
FT                   /note="Important for hydrogen atom transfer"
FT   Condition: C
FT   SITE            1111
FT                   /note="Important for electron transfer"
FT   Condition: Y
FT   SITE            1112
FT                   /note="Important for electron transfer"
FT   Condition: Y
FT   SITE            1132
FT                   /note="Interacts with thioredoxin/glutaredoxin"
FT   Condition: C
FT   SITE            1135
FT                   /note="Interacts with thioredoxin/glutaredoxin"
FT   Condition: C
FT   DISULFID        582..808
FT                   /note="Redox-active"
FT   Condition: C-x*-C
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Size: 767-1144;
Related: None;
Template: P08543;
Scope:
 Viruses; Alphaherpesvirinae
 Viruses; Gammaherpesvirinae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.8 2023/10/16
//