ID A0A1I2H4L0_9BACT Unreviewed; 801 AA.
AC A0A1I2H4L0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05216283_103226 {ECO:0000313|EMBL:SFF23611.1};
OS Sunxiuqinia elliptica.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Sunxiuqinia.
OX NCBI_TaxID=655355 {ECO:0000313|EMBL:SFF23611.1, ECO:0000313|Proteomes:UP000198964};
RN [1] {ECO:0000313|EMBL:SFF23611.1, ECO:0000313|Proteomes:UP000198964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9156 {ECO:0000313|EMBL:SFF23611.1,
RC ECO:0000313|Proteomes:UP000198964};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONW01000003; SFF23611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2H4L0; -.
DR STRING; 655355.SAMN05216283_103226; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000198964; 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 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.
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:UP000198964}.
FT DOMAIN 3..96
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 739..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 91217 MW; C68CD4A53F735C59 CRC64;
MQRTVIKRDG SEERFRTQEI INAIFEIIKG MAVEDDYELV FRIIKELDLK VPERVTTEEL
DVLVLKAIEH LIPKHPVYDT LATLQLLKLI NKRVGRQFSS FSQYLKFNIE TGYLKEDLVQ
FDLKTIEKAI DYDNDRLLDY FGLTTLRDRY LSKDREQEVI EKPQWFFMRV ALGIGTTEDE
VIAIYNKMSR LEYLHSTPTL FNSGTNVSQY SSCYVNVVDD SLQSITDKLT ETAFLAKYAG
GVGTDISRVR ATGSHIHSLN AKSSGVIPFI KVFDTMVNSI QQGGRRRSSQ VISIQPWHYD
IETFLELRET TGNAYFRTPS LNTKLWMPDE MMKRIEKDEP VYLFDPGECP ELVEAVGDDF
SNKYHKRIQQ AEAGELKLFK KLSGRDFYKK YLFKLAKTGH PWLTFKDAHN RHNPCPQYGI
INSSNLCTEI AIPNNPESTA VCTLASVNLA RHINADKTDF NWTQLESTIQ IIVRALDNVL
DKNYYPSEAS KRNTMDLRPL GIGMMGFAEA LVQLKIAYDS SQAVEVAQKL GQFFREKAYG
TSEQLAKEKG AFPHYEAVRK AGKAYAYPAR RNAVLLAIAP TATISIIAGT TSSIDSYFSN
LYSRDTLSGK YIVINKRLIE DLEIKGLWND EIADAIKSNN GSVQTIEALR GKIDVNLYKT
TYEVHPKRQI DLAAAFQETV DQAVSKSIYI DEQLRAEMED IYLYAWKKQL KSTYYCFIDK
VIKGEKYTSE VNKRGSRKGF GRQKLATPDS RLKNDSPDGL KTIELEARAK FGDELVDEVK
KGNQETCPTD PLLAKLCPSC E
//
