ID C9MP84_9BACT Unreviewed; 840 AA.
AC C9MP84;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=HMPREF0973_01422 {ECO:0000313|EMBL:EEX18887.1};
OS Prevotella veroralis F0319.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX18887.1, ECO:0000313|Proteomes:UP000003327};
RN [1] {ECO:0000313|EMBL:EEX18887.1, ECO:0000313|Proteomes:UP000003327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0319 {ECO:0000313|EMBL:EEX18887.1,
RC ECO:0000313|Proteomes:UP000003327};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX18887.1}.
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DR EMBL; ACVA01000031; EEX18887.1; -; Genomic_DNA.
DR RefSeq; WP_004383088.1; NZ_GG698713.1.
DR AlphaFoldDB; C9MP84; -.
DR STRING; 649761.HMPREF0973_01422; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_10; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000003327; 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; PF03477; ATP-cone; 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:UP000003327}.
FT DOMAIN 1..92
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 840 AA; 96615 MW; 67F3EE6E8A61E3BC CRC64;
MDIIKRNGES ERYNNNKIAI AIKKSFISTG KPIKDEEIAA MVAEVEQIII DNPDQRTVEE
IQNQVEKHLM MHGHYDEAKN FILFRYQRNE QRKAINDIAR MADDTELTTV LQDVAREYRE
RVYSMVTLQE KFANLCKPSM SHKEAIDTLI KAAVELTTPE APAWEMISAR ILSYRAEQKI
KKQEDEIGID GFYNKLKYMT SEGLYGEYIL QNYTEEEINE AATFIKEERN KLLNYSGLDL
LLKRYVIKNY AGKAIERVQE MYLGIALHLA MPEQKENRLM WVHRIYDMLS KLEVTMATPT
LSNARKPNHQ LSSCFIDTVP DSLDGIYRSL DNFSQVSKFG GGMGMYFGKV RATGGNIRGF
KGVAGGVIRW MRLVNDTAVA VDQLGMRQGA VAVYLDVWHK DLPEFLQLRT NNGDDRMKAH
DIFPAVCYPD LFWKMADENL DQNWYLFCPN EIMRIKGYCL EDCYGEEWER KYLDCVNDQR
LTRRVISIKD IIRLVLRSAV ETGTPFTFNR DTVNRANPNH HKGMIYCSNL CTEIAQNMAP
IETVSKTIET KDGETIVVTT TKPGEFVVCN LASLSLGRLP LEDEEQMREK VATIVRALDN
VISLNFYPVP YAEITNQKYR SIGLGISGYH HALAKRRIKW ESEEHLQFMD KVFETINRSA
ILASSNLAKE KGSYQYFEGS DWQTGLYFDK RGYDSDEWKE VRKTVALQGM RNAYLLAVAP
TSSTSIIAGT TAGLDPIMKR FFLEEKKGSM LPRVAPELSD ETYWMYKSAY LINQKWSIKA
SGVRQRHIDQ AQSMNLYITN DFTMRQVLDL YLLAWKSGVK TIYYVRSKSL EVEECESCAS
//
