ID K6VQ33_9MICO Unreviewed; 847 AA.
AC K6VQ33;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=nrdA {ECO:0000313|EMBL:GAB78864.1};
GN ORFNames=AUCHE_17_00760 {ECO:0000313|EMBL:GAB78864.1};
OS Austwickia chelonae NBRC 105200.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Austwickia.
OX NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB78864.1, ECO:0000313|Proteomes:UP000008495};
RN [1] {ECO:0000313|EMBL:GAB78864.1, ECO:0000313|Proteomes:UP000008495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB78864.1,
RC ECO:0000313|Proteomes:UP000008495};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL Submitted (AUG-2012) 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:GAB78864.1}.
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DR EMBL; BAGZ01000017; GAB78864.1; -; Genomic_DNA.
DR AlphaFoldDB; K6VQ33; -.
DR STRING; 100225.SAMN05421595_0075; -.
DR eggNOG; COG0209; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000008495; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; IPR005144; ATP-cone_dom.
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; PS51161; ATP_CONE; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000008495}.
FT DOMAIN 25..114
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 847 AA; 94281 MW; 9AEF03C26344F745 CRC64;
MTSTTSPPAP TRAHREDPTG DLPTVTVTAA DGTTTALDRT RIHRLLAQAT HGIPDVTAEP
VLHELRRTVY DGITQDELAT ALVLAARTLV EREPRYSQVA ARLLLDRMRT EALTHLAGTP
RQLTAEEMND EYARYFPTYL RRAVDIGRVD PELLTYDLDR IGAALDGTAD LDFGLLGLQT
VYDRYVLHED GTRFELPQAF FMRVAMGLAL REDDRETRAI EFYRMLSGFD LMTSTPTLFN
AGTTRPQLSS CFLTTVDDDL DRIFSSYRNN ALLAKYSGGL GNDWTPVRGL GAHIHGTNGR
SQGVVPFLKI ANDTTVAVNQ GGKRKGAACA YLETWHIDIE EFLDLRKNTG DDRRRTHDMN
TAHWIPDEFM RRLESDSSWT LFSPDETPDL HDLYGEDFSR RYAEYEAAAD RGEIRLHRRI
PAKDLWRRML TMLFETGHPW ITFKDPCNLR SPQQHAGVVH SSNLCTEITL NTTSDEVAVC
NLASVNLARH VTPSGLDVDK LRRTVRTAVR MLDNVIDINH YTIPETRRSN LRHRPVGLGL
MGHQDALFTL GIPYASDDAV DFADRSTETL SYFAIEASAD LAADRGTYQS YEGSLWSRGI
LPIDSLRLLA QARHDGELDI DTSSTLDWDR LRDHVQANGM RNSNVMAIAP TATISNICGV
AASIEPQFQN LFVKANMSGD FTVVNGHLVA DLKKYGLWDE EMIADLKYHD GALARIDRIP
EDLRRIYATA FDIDPRWLIA AASRRQKWID QAQSLNLYVA EPSGRALDEL YRSAWRSGLK
TTYYLRARAA TQVEKSTLRG TDGRLNAVSP AGGPAAVPAA GPVDLSAGPA VAPAACSLTD
PECEACQ
//
