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Database: UniProt
Entry: A0A095US20_9GAMM
LinkDB: A0A095US20_9GAMM
Original site: A0A095US20_9GAMM 
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
//
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