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Database: UniProt
Entry: A0A0W1FK92_9SPHN
LinkDB: A0A0W1FK92_9SPHN
Original site: A0A0W1FK92_9SPHN 
ID   A0A0W1FK92_9SPHN        Unreviewed;       650 AA.
AC   A0A0W1FK92;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=ATE62_04705 {ECO:0000313|EMBL:KTE43020.1};
OS   Sphingopyxis sp. HIX.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759074 {ECO:0000313|EMBL:KTE43020.1, ECO:0000313|Proteomes:UP000053691};
RN   [1] {ECO:0000313|Proteomes:UP000053691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIX {ECO:0000313|Proteomes:UP000053691};
RA   Gomez-Alvarez V., Revetta R.P.;
RL   Submitted (NOV-2015) 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   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160, 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}.
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:KTE43020.1}.
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DR   EMBL; LNSB01000006; KTE43020.1; -; Genomic_DNA.
DR   RefSeq; WP_058810563.1; NZ_LNSB01000006.1.
DR   AlphaFoldDB; A0A0W1FK92; -.
DR   STRING; 1759074.ATE62_04705; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000053691; Unassembled WGS sequence.
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:UniProtKB-UniPathway.
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}.
FT   DOMAIN          68..133
FT                   /note="Ribonucleotide reductase large subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00317"
FT   DOMAIN          137..456
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
FT   DOMAIN          465..611
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   650 AA;  72114 MW;  BD819BE200E37ECD CRC64;
     MDFRETDRVE TSDVATMELA KNETPVAPES VGESKDDSAP AAKLNDVGEP KVHARRFAIE
     TVRDRDALLT DFGKETLEDR YLLPGESYQD LFARVADAYA DDQDHAQRLY DYISKLWFMP
     ATPVLSNGGT GRGLPISCYL NSVDDSLEGI VGTWNENVWL ASRGGGIGTY WGAVRGIGEP
     VGLNGKTSGI IPFVRVMDSL TLAISQGSLR RGSAACYLDI SHPEIEEFLE VRKPSGDFNR
     KALNLHHGVL ITDEFMEAVR DGAEFNLRSP KDNSVRGSVD ARGLFQKLVE TRLATGEPYI
     IFIDQVNRMM PKHHRDLGLK VTTSNLCSEI TLPTGRDHLG NDRTAVCCLS SLNLETWDEW
     NGDKRFIEDV MRMLDNVLQD YIDRAPPEMA RAKYSASRER SVGLGVMGFH SFLQARGLPF
     EGAMAKSSNL RVFKHIRAQV DAASMLLANE RGPCPDAADQ GVMERFSCKM AIAPTASISI
     ICGGTSACIE PIPANIYTHK TLSGSFSIRN PHLEALLVDK AKNSDAIWNS ILERGGSVQH
     LDFLSQDEKD CFKTSFEIDQ RWLLELAADR TPYIDQAASL NLFIPADVEK WDLLMLHYRA
     WELGIKSLYY LRSKSVQRAG FAGGVEADNT AEAPKFELQT TDYDECLACQ
//
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