ID G8C2Y7_9MOLU Unreviewed; 708 AA.
AC G8C2Y7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 Name=nrdE {ECO:0000313|EMBL:CCE66685.1};
GN ORFNames=MHM_01670 {ECO:0000313|EMBL:CCE66685.1};
OS Candidatus Mycoplasma haematominutum 'Birmingham 1'.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1116213 {ECO:0000313|EMBL:CCE66685.1};
RN [1] {ECO:0000313|EMBL:CCE66685.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Birmingham 1 {ECO:0000313|EMBL:CCE66685.1};
RA Barker E.N., Darby A.C., Helps C.R., Peters I.R., Hughes M.A.,
RA Radford A.D., Novacco M., Boretti F., Hofmann-Lehmann R., Tasker S.;
RT "Complete genome sequence of Candidatus Mycoplasma haemominutum.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCE66685.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Birmingham 1 {ECO:0000313|EMBL:CCE66685.1};
RA Barker E.;
RL Submitted (NOV-2011) 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; HE613254; CCE66685.1; -; Genomic_DNA.
DR RefSeq; WP_015511550.1; NC_021007.1.
DR AlphaFoldDB; G8C2Y7; -.
DR KEGG; mhb:MHM_01670; -.
DR PATRIC; fig|1116213.3.peg.178; -.
DR HOGENOM; CLU_000404_4_1_14; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
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 566..588
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 708 AA; 80823 MW; 09F1AE11F9C83807 CRC64;
MNKPKKIVSQ AFYDSLILNN QVTMMGEDGF YCLEKDELAI KEYQKYISET ERYSQKKRGH
QRIKWLIEEE YYLPELVQKY SEAQINKLSE TVYNTPFKWK SYISISKFFE SFAMRSNCGK
YILESYEDRV IVASLFLGNG DFELASKIAN LIIRQIFQPA TPTFSNAGKK RSGELVSCFL
LEVEDSINSI NYVISTSMQL SKIGGGVAIN LSKLRGRGAS IKKIDSTASG VLPVLKILEN
VFDYADQLGM RRGSGAAYLN IFHYDLIDFI DCKKINADEK SRIQTLSIGL IVPDKFLELA
KDNKDFFIFE PNTIYQKYGV FLSDLNFDEW YEKLANDTEI LKKQLSARAI LTKIAQTQFE
SGYPYVIFID NANRQNPLKA LGKIKMSNLC TEIFQIQESS HITDYGEEDL IRNDVSCNLA
SLNLVNVIED GNLEEIIEVS MRALSAVSDL TSIKNAPSVR KANEEYKSVG LGILNFTGFL
IKHNIEYGSP ESLEFADVFF AAVNYYSLLA SSKIAKERKI IFKDFEKSDY ASGKFFELYC
EQEFLPKSEK IRQLVSHLKL PTRGDWIKLR EKVKNDGLYN SYRLAIAPTQ SISYLQGATA
SIQPIISPIE TRMYGSSITY FPMPFLSKDN QHLFCSAYHI DQKKLIDMSA TIQTHIDQGI
STILYVTNNS TTRDLVKLYL YAHHKGLKSL YYVRTKNLQP EECELCQA
//
