ID A0A2V5L9S9_9MICC Unreviewed; 706 AA.
AC A0A2V5L9S9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=CVV68_10310 {ECO:0000313|EMBL:PYI67532.1};
OS Arthrobacter livingstonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=670078 {ECO:0000313|EMBL:PYI67532.1, ECO:0000313|Proteomes:UP000247832};
RN [1] {ECO:0000313|EMBL:PYI67532.1, ECO:0000313|Proteomes:UP000247832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LI2 {ECO:0000313|EMBL:PYI67532.1,
RC ECO:0000313|Proteomes:UP000247832};
RA Liu Q., Xin Y.-H.;
RT "Genetic diversity of glacier-inhabiting Cryobacterium bacteria in China
RT and description of Cryobacterium mengkeensis sp. nov. and Arthrobacter
RT glacialis sp. nov.";
RL Submitted (MAY-2018) 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}.
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:PYI67532.1}.
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DR EMBL; QJVD01000009; PYI67532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5L9S9; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000247832; 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; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
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; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 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.
DR PROSITE; PS00089; RIBORED_LARGE; 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 558..580
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 706 AA; 80171 MW; 1D95448214B78734 CRC64;
MPAAWEGLGY HELNAMLNLY NADGEIQFDA DRAAARQYFL QHVNNNTVFF HDLEEKLDYL
VKNEYYERET LDQYTMNFIR ELYNHAYKKK FRFETFLGAF KFYTSYTLKT FDGNRFLERY
EDRVCMVALH LARGDEQLAL KMVDEIIEGR FQPATPTFLN AGKKQRGELV SCFLLRIEDN
MESIGRSINS ALQLSKRGGG VAFALTNIRE VGAPIKQIEN QSSGVIPVMK LLEDSFSYAN
QLGARQGAGA VYLHAHHPDI NRFLDTKREN ADEKVRIKTL SLGVVVPDIT FDLAKRDEDM
YLFSPYDVEK VYGVPFSDIS VTEKYYEMVD DARIKKTKIK AREFFQTLAE IQFESGYPYI
MFEDTVNRAN PIDGKIIMSN LCSEILQVSA PTSYNDDLSY ADTGKDISCN LGSLNIAKAM
DSPDFGSTIE TSIRTLTAVS DMSNITSVPS IAKGNDQSHA IGLGQMNLHG YLARERVHYG
SDEGLDFTNI YFYTVVYHCL RASNLIAMET GSTFAGFEKS KYASGEFFDK YTDAEWVPQT
ARVVELFDGI HIPTQDDWRE LKASVMEHGI YNQNLQAVPP TGSISYINNS TSSIHPVASK
IEIRKEGKLG RVYYPAPYLT NDNLEYYQDA YEIGFEKIID TYAAATQHVD QGLSLTLFFK
DTATTRDINK AQIYAWKKGI KTIYYIRLRQ LALEGTEVEG CVSCML
//
