ID A0A0G1DJU8_9BACT Unreviewed; 782 AA.
AC A0A0G1DJU8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=UV73_C0004G0004 {ECO:0000313|EMBL:KKS97862.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_43_14.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618443 {ECO:0000313|EMBL:KKS97862.1, ECO:0000313|Proteomes:UP000034894};
RN [1] {ECO:0000313|EMBL:KKS97862.1, ECO:0000313|Proteomes:UP000034894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC deoxyribonucleotides. May function to provide a pool of
CC deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC and/or for immediate growth after restoration of oxygen.
CC {ECO:0000256|RuleBase:RU364064}.
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 Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922,
CC ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKS97862.1}.
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DR EMBL; LCFP01000004; KKS97862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1DJU8; -.
DR STRING; 1618443.UV73_C0004G0004; -.
DR PATRIC; fig|1618443.3.peg.658; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034894; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634,
KW ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 8..78
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 85..566
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 578..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 87346 MW; 7CA1ABFFC7E5DB61 CRC64;
MKLTGIREQV FLDRYSLKDE KGKPVEKTPE SMWKRVAKGV AQVENKEVRK YWEKKFIEVM
DDFKLVPGGR ILSGAGTGYR VTFYNCFVIP SPKDSRDGIL DTLKQMVEIM ARGGGVGINL
SSLRPRGARV RKVNGFSSGP CNWAELFSVA TKDIIQQGGT RRGALMLMLW DWHPDIEEFI
TVKRDLSRIN GANLSVCVSD KFMEAVKKDA DWQLVFPDIS DPEYDSKWDG YLDDWVKAGK
KVKVFKTVKA RKIWDMISEA AWASAEPGLV FMERYNKWNN NWYFNKINCV NPCGEEGLPA
WGVCNLTSIN LSALVQGGKI DYQELADIAK VGVRFQDDII DADSYIFPQI EETQKNGERR
IGLGTMGLGD ALIKMKIRYG SDASVKIIDK IYSTIRNAAY EASTEIAKEK GAFPKFDAKK
YLKGYFIKQL PEPVKAKIKK WGIRNSVLLQ QAPTGSTSLL AGVTSGIEPV YEFSFIRRDR
LGEHRLFHPL FDEWKKEHPN DPIPDYFVSA NDLIPEDHVK VQAAIQKYVD ASISKTVNAP
NSHTVKDVQK LYRMAYDLGC KGITYMREGS RPGVLERVTD KKQETDQKQQ EGSLPAGNGK
SIPEITPRPM VVKGATYQID TPVGAAFVTI NTDMDNEPLE IFINVGKAGS DVTAMAEAVG
RLGSLVLRMQ SSVPASERAR QIFNQLIGIG GSKSLGFGDK RVRSLPDAVA KILAMHFDYK
VKNGNGLTHK EVLPEQQPLA VLTQQALPVE KSEYDLCPSC GEAALAYEES CKKCYSCGYS
EC
//
