ID A0A095US20_9GAMM Unreviewed; 960 AA.
AC A0A095US20;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=Y5S_01228 {ECO:0000313|EMBL:KGD65335.1};
OS Alcanivorax nanhaiticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177154 {ECO:0000313|EMBL:KGD65335.1, ECO:0000313|Proteomes:UP000029444};
RN [1] {ECO:0000313|EMBL:KGD65335.1, ECO:0000313|Proteomes:UP000029444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19-m-6 {ECO:0000313|EMBL:KGD65335.1,
RC ECO:0000313|Proteomes:UP000029444};
RA Lai Q., Shao Z.;
RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax sp. 19-m-6.";
RL Submitted (SEP-2012) 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 -!- PATHWAY: Genetic information processing; DNA replication.
CC {ECO:0000256|ARBA:ARBA00005160, 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:KGD65335.1}.
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DR EMBL; ARXV01000004; KGD65335.1; -; Genomic_DNA.
DR RefSeq; WP_035231355.1; NZ_ARXV01000004.1.
DR AlphaFoldDB; A0A095US20; -.
DR STRING; 1177154.Y5S_01228; -.
DR PATRIC; fig|1177154.3.peg.1251; -.
DR eggNOG; COG0209; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000029444; 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:UniProtKB-UniPathway.
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; 2.
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}.
FT DOMAIN 34..134
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 150..239
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 107401 MW; 3A07C8808FE4CDA7 CRC64;
MQTDMSQNPQ NPAAKAGDDA GQDQNIASTA PGQLRVIKRN GKVVSYDDDK ITVAISKAFL
AVEGGTAAAS SRIHETVARL TEQVSATFKR RMPSGGTIHI EEIQDQVELA LMRNGEHKVA
RDYVLYRDRQ AQKRAEQASQ FPEPTHKVEM SVTMEDGSKA PLDMGRLEHL IRTACEGLED
VHADKIITET VKNLYDGVSI NDVNTSMVMT ARTLIEVEPN YSQVTARLLM DKIRAEALQY
LGVAERANQE EMNALYGEAL AAYISKGIEL ELLSPALGEY DIARLGAAIQ GDRDLQFTYL
GLQTLYDRYF IHHNDTRIEL PQCFFMRVAM GLAIEEENKE ERAIEFYNLL SSFDYMSSTP
TLFNAGTLRP QLSSCYLTTV PDDLHGIYGA IQDNAMLSKF AGGLGNDWTP VRALGSYIKG
TNGKSQGVVP FLKVVNDTAV AVNQGGKRKG AVCAYLETWH MDIEEFLELR KNTGDDRRRT
HDMNSANWIP DLFMKRVLNE EDWTLFSPND TPDLHDLYGE AFEKAYTAYE EQTRNGEIKL
FKRLPAATLW RKMLSMLFET GHPWFTFKDP CNLRSPQQHV GVVHSSNLCT EITLNTNKDE
IAVCNLGSVN LAQHVDENGL DTDKLQRTIN TAVRMLDNVI DINYYSVPQA ENSNMKHRPV
GLGIMGFQDA LYKQGISYAS EGAVQFADTS MEAVSYYAIQ ASAKLAEERG AYQTFDGSLW
SQGILPIDSI DILVNQRGED YCKVDRSQTL DWDSVREMAK KGMRNSNVMA IAPTATIANI
TGVSQSIEPT YQNLYVKSNL SGEFTVVNPY LVHALKERGL WDNVMVNDLK YYDGSAQPIE
RIPADLKEQF RTAFEVETRW IVEAASRRQK WIDQAQSLNL YIAEANGKKL DVTYKMAWLL
GLKTTYYLRA IGATQAEKST INDGKLNRVS SKVEEPAEFS QAAEVPQACS IDNPDCEACQ
//