ID U2CWL8_CLOSY Unreviewed; 764 AA.
AC U2CWL8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=CLOSYM_04751 {ECO:0000313|EMBL:ERI73632.1};
OS [Clostridium] symbiosum ATCC 14940.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=411472 {ECO:0000313|EMBL:ERI73632.1, ECO:0000313|Proteomes:UP000016491};
RN [1] {ECO:0000313|EMBL:ERI73632.1, ECO:0000313|Proteomes:UP000016491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14940 {ECO:0000313|EMBL:ERI73632.1,
RC ECO:0000313|Proteomes:UP000016491};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (JUL-2013) 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:ERI73632.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWSU01000380; ERI73632.1; -; Genomic_DNA.
DR RefSeq; WP_021642066.1; NZ_KE992902.1.
DR AlphaFoldDB; U2CWL8; -.
DR PATRIC; fig|411472.5.peg.4453; -.
DR HOGENOM; CLU_000404_3_0_9; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000016491; 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}.
FT DOMAIN 622..644
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 764 AA; 87188 MW; 891E5B01F7694498 CRC64;
MDNLKDTGAG KTAGSQVSLQ SLEHLTREVP ELAPALEEIE ARWPKEEYSP ELLAHKFSAF
VKKNMEPEEA LSLLIQAAAE LTRKEAPDWE YIAAYLLLVR FRINLREEDK KHGIGSFYDR
IRYLTRENLY GSYIMEYYSR EELEEAGGLI DEKRDLLFNY AGLDLLLSRY VIRSRQNIPL
ESPQEMFLGI SLHLAMKEQK DRMKWVKRFY DMLSTLKVTM ATPTLSNARK PYHQLSSCFI
DTVPDSLDGI YRSIDSFAKV SKFGGGMGLY FGKVRASGSS IRGFKGAAGG VIRWIKLAND
TAVAVDQLGV RQGAVAVYLD VWHKDLPEFL ALRTNNGDDR MKAHDVFPAV CYPDLFWRLA
DEAIDSDWYL MCPHEILAAT GYALEDYYGQ EWEKRYWDCV KDERIPKRVL PIKDIIRLIL
KSAVETGTPF TFNRDTVNRA NPNRHRGMIY CSNLCTEIAQ NMSPVEALEQ RIETVDGETV
VVTVTKPGDF VVCNLASLSL GKINVSDRSE LTFLVRCAVR ALDNVIDLNF FPVPYAKINN
LRYRPVGLGV SGYHHMLAKN GISWESEEHL AIADRVFEWI NYAAIEASCD YAEEKGCYEY
FPGSGWQTGS YFEMRGYCSD EWRRLREKAA AVGLRNGWLI AAAPTSSTSM ISGTTAGLDP
IMNRFYLEEK KNGLVPRVAP ELTPSTYWRY KNAHYIDQKW SLRAAGIRQR HIDQAQSINL
YITNNYTLRQ VLELYLLAWK SGVKTIYYIR SKSLEIEECE VCSS
//
