ID A0A1N6H1V9_9SPHN Unreviewed; 683 AA.
AC A0A1N6H1V9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02745824_3097 {ECO:0000313|EMBL:SIO13791.1};
OS Parasphingorhabdus marina DSM 22363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Parasphingorhabdus.
OX NCBI_TaxID=1123272 {ECO:0000313|EMBL:SIO13791.1, ECO:0000313|Proteomes:UP000185192};
RN [1] {ECO:0000313|Proteomes:UP000185192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22363 {ECO:0000313|Proteomes:UP000185192};
RA Varghese N., Submissions S.;
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; FSQW01000002; SIO13791.1; -; Genomic_DNA.
DR RefSeq; WP_074206017.1; NZ_FSQW01000002.1.
DR AlphaFoldDB; A0A1N6H1V9; -.
DR STRING; 1123272.SAMN02745824_3097; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000185192; 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: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:UP000185192}.
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..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 75996 MW; 0ECDABF99FC3E73A CRC64;
MDFRENRDSE TGFNGGDMSE SEMGAEVLDK AVDENAGEQN AGPVKEPEVA PKGKSKKAEA
EAAAAKKNDE QEKKEERDSH SVAERRFKIA QDESRDDLLT EFGKETLVDR YLLPGESFQD
LFARVADAYA DDQDHAQRLY DYISKLWFMP ATPVLSNGGT GRGLPISCYL NSVDDSLGGI
VNTWNENVWL ASKGGGIGTY WGSVRGIGEP VGLNGKTSGI IPFVRVMDSL TLAISQGSLR
RGSAACYLDI DHPEIEEFLE IRKPSGDFNR KALNLHHGVL LTDEFMEAVR DGKEMDLKSP
KDGSVRGSVD ARSLFQKLVE TRLATGEPYI IFNDTVNRMM PKHHRDLGLK VSTSNLCSEI
TLPTGRDHLG EDRTAVCCLS SLNLEKWDEW SVDKDFIEDV MRFLDNVLQD YIDRAPEEMA
RAKYSAMRER SVGLGVMGFH SFLQARGLGF ESALAKSWNM KIFKHIHSKA SEASMMLAKE
RGPCPDAADQ GVMERFSCKM AIAPTASISI ICGGASACIE PIPANIYTHK TLSGSFVVKN
PHLEKLLQEK SKDSTNVWNS ILEQGGSVQH LDFLTQEEKD AYKTSFEIDQ RWLLELAADR
TPYIDQAQSL NLFIPADVDK WDLLMLHFRA WELGIKSLYY LRSKSVQRAG FAGGVEADNT
LDPKQVELMT AETTDYDECL ACQ
//
