ID A0A1W1I4C9_9BACT Unreviewed; 813 AA.
AC A0A1W1I4C9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:SLM47860.1};
GN ORFNames=NSJP_1688 {ECO:0000313|EMBL:SLM47860.1};
OS Nitrospira japonica.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1325564 {ECO:0000313|EMBL:SLM47860.1, ECO:0000313|Proteomes:UP000192042};
RN [1] {ECO:0000313|EMBL:SLM47860.1, ECO:0000313|Proteomes:UP000192042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Genome sequencing of Nitrospira japonica strain NJ11
RC {ECO:0000313|EMBL:SLM47860.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; LT828648; SLM47860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1I4C9; -.
DR STRING; 1325564.NSJP_1688; -.
DR KEGG; nja:NSJP_1688; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000192042; Chromosome i.
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:UP000192042}.
FT DOMAIN 34..123
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 90558 MW; FF728C0249FB964D CRC64;
MPSEPTESIE SLAVSDSPLS PHGGNDEVSS QHTMRVKKRN GSTEPVDVMK IVRAVERCCG
GLSDIDPLRI ATKTISGLYD GATTRELDRL SIQTAAALIV EEPQYARLAA RLLATYIDKE
VRNQEIHAFS QSVAAGYRLG LVNERLQHFV SQNSRKLNDA LDPKRDREFE YFGLRTVYDR
YLLKHPATRQ VIETPQQFFL RIACALSETV SDALELYRLL SSLEYLPSSP TLFNAGTKHE
QLSSCFLLDS PDDHLEHIYQ RYTDVAMLSK FSGGIGLAYH RVRSRGSLIE STNGHSNGII
PWLKTLDASV AAVNQGGKRK GACCVYLEPW HADVEEFLEL RDNTGDEASR THNLNLANWI
PDLFMRRVEA DADWSLFDPK TVPELPDLYG EEFERAYVRA EEAGLAVKAI KARELYARMM
RTLAQTGNGW MTFKDKSNRA CNQTALPGRT VHLSNLCTEI LEVTSRDETA VCNLGSINLA
RHTAAGSDGA VSFDFEKMGR TVRCAVYQLD RVIDLNYYPI TAARSSNLRW RPVGLGVMGL
QDVLFQMRLS FDAPEARALS ARIAEDIYYH ALSASVDLAI TKGRHPAFED TRAARGELQF
DAWGIEPSDP ARWSALRTRI ATHGLRNSLL VAIAPTATIA SIAGCYECIE PQVSNLFKRE
TLSGDFLQVN RYLVADLKRL GLWNSETRAR LKLAEGSAQG LNELPSDLRT LYRTAWEIPM
RSLIDMAADR GAFIDQSQSL NLFIENPNIG QLSSMYFYGW KKGLKTTYYL RSRPATRIAK
ATVDAAPQKS PGERGTDAVA CSLENPGSCE ACQ
//
