ID A0A127MGQ0_9SPHN Unreviewed; 669 AA.
AC A0A127MGQ0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AZE99_11130 {ECO:0000313|EMBL:AMO72331.1};
OS Sphingorhabdus sp. M41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO72331.1, ECO:0000313|Proteomes:UP000073959};
RN [1] {ECO:0000313|EMBL:AMO72331.1, ECO:0000313|Proteomes:UP000073959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:AMO72331.1,
RC ECO:0000313|Proteomes:UP000073959};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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 -!- 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; CP014545; AMO72331.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127MGQ0; -.
DR STRING; 1806885.AZE99_11130; -.
DR KEGG; sphg:AZE99_11130; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000073959; Chromosome.
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}.
FT DOMAIN 69..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..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 73999 MW; 4678F05B55FF2263 CRC64;
MGAEVLDTPK SKTENTGPTS EPEVSKKAAA EAASAKANDE KELKAERDSH SVEKRRFKIT
QDESRDDLLT DFGKETLNDR YLLPGESYQD LFARVADAYA DDQEHAQRLY DAISKLWFMP
ATPVLSNGGT GRGLPISCYL NSVDDSLGGI VNTWNENVWL ASRGGGIGTY WGSVRGIGEP
VGLNGKTSGI IPFVRVMDSL TLAISQGSLR RGSAACYLDV NHPEIEEFLE IRKPSGDFNR
KALNLHHGVL LTDEFMEAVR DGKEFDLKSP KDGSVRGTVD ARSLFQKLVE TRLATGEPYI
IFSDTVNRMM PKHHRDLGLK VSTSNLCSEI TLPTGRDHLG EDRTAVCCLS SLNLEKWDEW
SVEKGFIEDV MRFLDNVLQD YIDRAPEEMA RAKYSAMRER SVGLGVMGFH SFLQARGLGF
ESALAKSWNF KIFKHVSAKA SEASMMLAKE RGPCPDAADQ GVMERFSCKM AIAPTASISI
ICGGASACIE PIPANIYTHK TLSGSFVVKN PHLQKLLQEK SKDSNNIWNS ILEKGGSVQH
LDFLSTEEKD TYKTSFEIDQ RWLLELAADR TPYIDQAQSL NLFIPADVDK WDLLMLHFRA
WELGIKSLYY LRSKSIQRAG FAGGETMMSE PATGNISGGV EADNTLDPKT VELMTTAGTT
DYDECLACQ
//
