ID A0A0G9MKY3_9SPHN Unreviewed; 683 AA.
AC A0A0G9MKY3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=AAW01_07000 {ECO:0000313|EMBL:KLE31350.1}, BMF35_a0397
GN {ECO:0000313|EMBL:APE27226.1};
OS Aurantiacibacter gangjinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=502682 {ECO:0000313|EMBL:KLE31350.1, ECO:0000313|Proteomes:UP000053070};
RN [1] {ECO:0000313|EMBL:KLE31350.1, ECO:0000313|Proteomes:UP000053070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K7-2 {ECO:0000313|EMBL:KLE31350.1,
RC ECO:0000313|Proteomes:UP000053070};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacr gangjinensis K7-2.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APE27226.1, ECO:0000313|Proteomes:UP000183202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC1.15024 {ECO:0000313|EMBL:APE27226.1,
RC ECO:0000313|Proteomes:UP000183202};
RA Xu L., Wu Y.-H., Cheng H., Zhou Y.-G., Wu M., Cheng L., Xu X.-W.;
RT "Complete genome sequence of two-chromosomal Erythrobacter gangjinensis
RT CGMCC 1.15024T, isolated from seawater.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; CP018097; APE27226.1; -; Genomic_DNA.
DR EMBL; LBHC01000002; KLE31350.1; -; Genomic_DNA.
DR RefSeq; WP_047006702.1; NZ_LBHC01000002.1.
DR AlphaFoldDB; A0A0G9MKY3; -.
DR STRING; 502682.BMF35_a0397; -.
DR KEGG; egn:BMF35_a0397; -.
DR PATRIC; fig|502682.8.peg.1426; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000053070; Unassembled WGS sequence.
DR Proteomes; UP000183202; Chromosome i.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
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 Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000053070}.
FT DOMAIN 98..163
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 167..486
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 495..641
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 75300 MW; 91260E9EC542DC66 CRC64;
MEFRNSDEAA MGLEDSVEDT TETKADAANT AARSEQKAVS MDKKDAGSDA LVDEAAAGAM
AGAVAVAMKA DKDSSGDDSK KVNPRRFTIV TDEARDANLT EFGKETLTDR YLLPNESYQD
LFARVADAYA DDQDHAQRLY DYISNLWFMP ATPVLSNGGT NRGLPISCYL NSVSDSLDGI
VGTWNENVWL ASKGGGIGTY WGNVRGIGEP VGLNGKTSGI IPFVRVMDSL TLAISQGSLR
RGSAACYLDV SHPEIEEFLE IRKPSGDFNR KALNLHHGVL LTDEFMEAVR AGEKFDLKSP
KDGSVRGQVD ARSLFQKLVE TRLATGEPYI VFSDTVNRMM PKHHRDLGLK VSTSNLCSEI
TLPTGIDHLG NDRTAVCCLS SLNLEKWDEW NGDKTFIEDV MRFLDNVLQD YIDRAPEEMA
RAKYSAMRER SVGMGVMGFH SFLQSKGIGF ESPMAKVWNL KMFKHIHGKA SEASMVLAQE
RGACPDAEEM GAMERFSCKM AIAPTASISI ICGGTSACIE PIPANIYTHK TLSGSFIVKN
PYLEKVLDKK SKNSTNVWNS ILEKGGSVQH LDFLTDEEKS AFKTSFEIDQ RWLLEFAADR
SEYIDQAQSL NLFIPADVDK WDLMMLHFQA WEKGIKSLYY LRSKSVQRAG FAGGVEADNT
AEATKFELSA GESTDYDECL ACQ
//
