ID A0A0M0GQX8_9BACI Unreviewed; 745 AA.
AC A0A0M0GQX8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AF331_07755 {ECO:0000313|EMBL:KON92330.1};
OS Rossellomorea marisflavi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=189381 {ECO:0000313|EMBL:KON92330.1, ECO:0000313|Proteomes:UP000037405};
RN [1] {ECO:0000313|Proteomes:UP000037405}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11544 {ECO:0000313|Proteomes:UP000037405};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Fjat-14235 jcm11544.";
RL Submitted (JUL-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}.
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:KON92330.1}.
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DR EMBL; LGUE01000001; KON92330.1; -; Genomic_DNA.
DR RefSeq; WP_053427505.1; NZ_LGUE01000001.1.
DR AlphaFoldDB; A0A0M0GQX8; -.
DR STRING; 189381.GCA_900166615_02721; -.
DR GeneID; 42291830; -.
DR PATRIC; fig|189381.12.peg.1711; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000037405; 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; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037405}.
FT DOMAIN 602..624
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 745 AA; 84735 MW; 6C725B32064867F6 CRC64;
MTSTINGTTA SHRAERLLNG LRESHESLNW EEYTQKVSLY TEDQPGVEEK QLLQFLILSA
VERISSNEPD WTYVAASLYL KNLYAISANA RGMEPYKGLH ELIGTLTKKN LYSPTLLNAY
SKEEMDHLEG LIRPERDELF TYIGIVTLSE RYLTKDHAGV LYELPQERFM IIAMTLLMNE
PKEHRLMLVE EAYWALSNLY MTVATPTFAN AGKSYGQLSS CFIDTVEDDL RSIYDSNTDV
STLSKNGGGL GIYMGKVRSR GSDIKGFKGV SSGVIPWMKQ LNNTAVSVDQ LGQRQGAIAV
YLDVWHKDIF SFLDTRLNNG DERLRTHDLF TGVCLPDLFM EQVENRGDWY LFDPHEVKTI
MGYALEDHFD EEKGSGSFRE KYWECVNEPA LSKEVIPAID IFKRIMISQL ETGTPYMFYR
DSVNRQNANS HKGMIYCSNL CTEIAQNMSP TVMEEEVVKD GKIITYKNPG DYVVCNLASV
SLARTVRDGQ MERVVTIGVR LLDNVIDLND IPVLQAQLTN ARYRGIGLGT FGWHHLLALE
GIKWESDEAV SYCDHLYEDI AFYTIKASQE LAVEKGAYPY FPGSAWDTGA YFTNKGYEGE
RWLDLKDKVA SKGIRNGYLM AVAPNSSTSI IAGSTASIDP LFRLEYSEEK KDYKIPVTAP
DLSPKTTWYY KTAYHVDQHW SIRQNKARQH HIDQGISFNL YVRNDIKAIE LLNLHMDAWK
SNLKTTYYVR STSVANFEEC ESCHS
//
