ID A0A1A8TG95_9GAMM Unreviewed; 754 AA.
AC A0A1A8TG95;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:SBS30972.1};
GN ORFNames=MSP8886_01988 {ECO:0000313|EMBL:SBS30972.1};
OS Marinomonas spartinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1792290 {ECO:0000313|EMBL:SBS30972.1, ECO:0000313|Proteomes:UP000092544};
RN [1] {ECO:0000313|EMBL:SBS30972.1, ECO:0000313|Proteomes:UP000092544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8886 {ECO:0000313|EMBL:SBS30972.1,
RC ECO:0000313|Proteomes:UP000092544};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FLOB01000003; SBS30972.1; -; Genomic_DNA.
DR RefSeq; WP_067015726.1; NZ_FLOB01000003.1.
DR AlphaFoldDB; A0A1A8TG95; -.
DR STRING; 1792290.MSP8886_01988; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000092544; 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; 1.10.1650.20; -; 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:UP000092544}.
FT DOMAIN 4..94
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 754 AA; 84832 MW; 882CDE347F9A7562 CRC64;
MSTLTVTKRN GKTENINLEK IHKVITWAAE DLDNVSVSQV ELKAQIQFFN GIRTTDIHET
LIKSAADLIS ENTPDYQYLA ARLAIFHLRK KAYGNFEPPH LYDHVRNLVE QNRYDQSLLD
NYTKAEFDEL NNIIDHSRDM NFSYAAVKQL EGKYLVQNRV TGEIYESPQF IYILIAACLF
ANYDKATRLD LIGRFYDAVS KFKISLPTPI MSGIRTPTRQ FSSCVLIECG DSLDSINATS
SAIVKYVSQR AGIGINAGAI RALGSPIRGG EAFHTGCIPF YKHFQTAVKS CSQGGVRGGA
ATVFYPIWHL EVESLLVLKN NRGVEENRVR HLDYGVQFNR LMYQRLIKGG NITLFSPSDV
PGLYDAFFAD QEEFDRLYTM YEQDPSIRKQ TVKASDLFTL FASERASTGR IYLQNVDHCN
THSPFDPAVA PVKQSNLCLE IALPTKPLNR VDDPEGEIAL CTLSAFNLGA LDNLDELEEL
SELIVRALDA LLDYQNYPIP AAQRATEMRR TLGVGVINYA YYLAKNGVRY SDGSANDLTH
KTFEAIQYYL LKASNKLSKE FGPCLAFDET TYAKGILPID TYKKEIDNIV SNELTYNWET
LRKDIVEHGL RNSTLSALMP SETSSQISNA TNGIEPPRGF VSVKASKDGI LKQVVPEFER
LKEQYELLWS IPSNDGYLQL VGIMQKFIDQ SISANTNYDP QKFESQKVPM KVILKDLLTA
YKLGVKTLYY HNTRDGADDQ QDDMDDCASG ACKI
//
