ID A0A1S8FD44_9BURK Unreviewed; 968 AA.
AC A0A1S8FD44;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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 ORFNames=B0B52_18185 {ECO:0000313|EMBL:OOG37327.1};
OS Polaromonas sp. A23.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG37327.1, ECO:0000313|Proteomes:UP000218978};
RN [1] {ECO:0000313|EMBL:OOG37327.1, ECO:0000313|Proteomes:UP000218978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A23 {ECO:0000313|EMBL:OOG37327.1,
RC ECO:0000313|Proteomes:UP000218978};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-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}.
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:OOG37327.1}.
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DR EMBL; MUNO01000039; OOG37327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8FD44; -.
DR STRING; 1944133.B0B52_18185; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000218978; 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; 2.
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:UP000218978}.
FT DOMAIN 33..133
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 147..236
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 107329 MW; A6399462678C65F0 CRC64;
MQTAQHAAPA PAGMPIAPQT PATSAHASSL AHYQIIRRNG SVVPFEPNKI AVAMMKAFLA
VHGTQGAASA SVRETVDGLT QAVMRALMRS RPGGGTFHIE DVQDQVELGL MRGGHHEIAR
AYVLYREKRT QERARQPQAP VAEAPQLHVL DGGKKVTLDI GKLQALIEAS CAGLGAEIKP
DPIVQETMRN LYDGVPIDEV YKASILAART LIEKDPDYTY ATARLLLHTI RREVLGEEVT
QENMATRYAE YFPEFIAKGV ANELLDEKLQ QFDLARLGAA LKPERDLKFD YLGLQTLFDR
YFLHVRKQRI ELPQAFFMRV AMGLALDEID REARAIEFYE IMSSFDFMSS TPTLFNAGTL
RSQLSSCYLT TVADDLGGIY DAIKENALLS KFAGGLGNDW TPVRALGAHI KGTNGESQGV
VPFLKVVNDT AVAVNQGGKR KGAVCAYLET WHLDIEEFLE LRKNTGDDRR RTHDMNTANW
IPDLFMRRVM EKGSWTLFSP SDTPDLHDKF GVEFEKAYTA YEAKAERGEI KPARKLQAID
MWRKMLSMLF ETGHPWITFK DACNVRSPQQ HAGVVHSSNL CTEITLNTSD TETAVCNLGS
VNLAQHLKDG AVDHEKLKKT ITTAMRMLDN VIDINYYAVK KARDSNMRHR PVGLGIMGFQ
DCLYELRVPY ASDAAVEFAD KSMEAVCYHA YWASTELAKE RGKYTSYKGS LWDQGILPLD
TLDMLAKERG GYVEVDRSST MDWVALRKKI AKDGMRNSNC VAIAPTATIS NIIGVDACIE
PCFGNLSVKS NLSGEFTVIN HYLVRDLKRL GLWDDVMVVD LKHFDGSLRP IDRVPQDIKA
LYATAFEVDA TWLVEAASRR QKWIDQAQSL NIYMSGASGK KLDDTYKLAW LRGLKTTYYL
RTMSATHAEK STVKAGKMNA VASGNTDDTG SMNALDAAAA TAQAQMNSSP ATDIKFCAID
DPGCEACQ
//
