ID A0A1V9G2R4_9BACT Unreviewed; 1121 AA.
AC A0A1V9G2R4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN ORFNames=A3860_19360 {ECO:0000313|EMBL:OQP64911.1};
OS Niastella vici.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=1703345 {ECO:0000313|EMBL:OQP64911.1, ECO:0000313|Proteomes:UP000192796};
RN [1] {ECO:0000313|EMBL:OQP64911.1, ECO:0000313|Proteomes:UP000192796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ57 {ECO:0000313|EMBL:OQP64911.1,
RC ECO:0000313|Proteomes:UP000192796};
RA Chen L., Wang D., Yang S., Wang G.;
RT "Niastella vici sp. nov., isolated from farmland soil.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025437, 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:OQP64911.1}.
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DR EMBL; LVYD01000041; OQP64911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9G2R4; -.
DR STRING; 1703345.A3860_19360; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000192796; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 2.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000192796}.
FT DOMAIN 39..127
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 178..662
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 718..822
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 830..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 124656 MW; F3845AE3C1B4F85F CRC64;
MPSKKSKGLQ FNRRFTKDGI SVFDQFEYDY RTSVIRNPTG EVVFEMNNVE VPKHWSQIAT
DILAQKYFRK AGVPQADGSM GRETSVKQVA HRLANCWKVW GEKYGYFASE QDATIFYEEL
VHCILNQSCT PNSPQWFNTG LFESYGIKGK PQGHYYVDAV DGQLKKSTSA YERPQPHACF
ILSVEDDLVN DGGIMDLWMR EARIFKYGSG VGTNFSHIRG EGEKLSGGGT SSGLMSFLKI
GDRAAGAIKS GGTTRRAAKM VCLDLDHPEI MEFINWKVEE EKKVGALIAA GYPSDYEGEA
YKTVSGQNSN NSIRIPNEFF NKLNNNEDWE LKARTDGKVM KRIPAREVWN QVAYAAWRCA
DPGTQYDTTI NEWHTSPKGG RINASNPCSE YMFLDNTACN LASANLRRFY NETNNTFDVE
GFEYVCRLWT VVLEVSVLMA QFPSKEVAQL SYDYRTLGLG YANLGSMLMV MGIPYDSEEA
RGIAGALTAI MTGVAYKTSA ELASILGPFA RYEENREDML RVMRNHRLAA YDADEYEKLH
IKPQGIKARY CPDYLLKAAT KAWDEAVQLG EKYGYRNAQV TVIAPTGTIG LVMDCDTTGV
EPDFALVKFK KLSGGGYFKI INQSVPTALK NLGYQTREIE SIVKYAVGAG TFVGAPHINH
QTLSEKGFIA EEIRKLDAAV ASAFEIGFVF NVYTLGEECL QRLGFKPEQY FNFEWSLLEA
LGFTDEQVEA ANDYICGTMT IEGAPFLKAE HLPVFDCANK CGKKGQRYIH AHGHIRMMAA
AQPFLSGAIS KTINLPNEAT VDEIADAYMM SWQLGLKACA LYRDGSKLSQ PLSNKSDKKK
KVEEETTDKT PAAEPQESNI VDLGKLTITE LLGEVQKRVQ ASPDTRLKRE LARIVERRTL
PAKRRGYTQK AKINGQAIFL RTGEYGDGTV GEIFIDMAKE GATMRSMLNC FAISISIGLQ
YGVPLEEFVE KFVFTRFDPA GMVDHPNIKS TTSIVDFIFR ALAYEYLGRT DLVHVLDRPE
VMNTGTDDWD EIPTSLEYEK KTPPLSDVRI VPGKPAKAPD VEPLKPVKAT VKKAEAGMDA
INAAAKSMQS DAPACNTCGH ITIRSGTCYK CLNCGNSMGC S
//
