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
//