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Database: UniProt
Entry: A0A218NN42_9ARCH
LinkDB: A0A218NN42_9ARCH
Original site: A0A218NN42_9ARCH 
ID   A0A218NN42_9ARCH        Unreviewed;       762 AA.
AC   A0A218NN42;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE            EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN   ORFNames=Mia14_0568 {ECO:0000313|EMBL:ASI13877.1};
OS   Candidatus Mancarchaeum acidiphilum.
OC   Archaea; Candidatus Micrarchaeota; Candidatus Mancarchaeum.
OX   NCBI_TaxID=1920749 {ECO:0000313|EMBL:ASI13877.1, ECO:0000313|Proteomes:UP000197679};
RN   [1] {ECO:0000313|EMBL:ASI13877.1, ECO:0000313|Proteomes:UP000197679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mia14 {ECO:0000313|EMBL:ASI13877.1,
RC   ECO:0000313|Proteomes:UP000197679};
RX   PubMed=28680072; DOI=10.1038/s41467-017-00104-7;
RA   Golyshina O., Toshchakov S., Makarova K., Gavrilov S., Korzhenkov A.,
RA   La Cono V., Arcadi E., Nechitaylo T., Ferrer M., Kublanov I., Wolf Y.,
RA   Yakimov M., Golyshin P., Slesarev A., Kozyavkin S.;
RT   "'ARMAN' archaea depend on association with euryarchaeal host in culture
RT   and in situ.";
RL   Nat. Commun. 8:60-60(2017).
CC   -!- FUNCTION: Catalyzes the reduction of ribonucleotides to
CC       deoxyribonucleotides. May function to provide a pool of
CC       deoxyribonucleotide precursors for DNA repair during oxygen limitation
CC       and/or for immediate growth after restoration of oxygen.
CC       {ECO:0000256|RuleBase:RU364064}.
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:RU364064};
CC   -!- COFACTOR:
CC       Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC         Evidence={ECO:0000256|ARBA:ARBA00001922,
CC         ECO:0000256|RuleBase:RU364064};
CC   -!- PATHWAY: Genetic information processing; DNA replication.
CC       {ECO:0000256|ARBA:ARBA00005160}.
CC   -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC       family. {ECO:0000256|ARBA:ARBA00007405, ECO:0000256|RuleBase:RU364064}.
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DR   EMBL; CP019964; ASI13877.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A218NN42; -.
DR   KEGG; marh:Mia14_0568; -.
DR   OrthoDB; 6188at2157; -.
DR   UniPathway; UPA00326; -.
DR   Proteomes; UP000197679; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
DR   CDD; cd02888; RNR_II_dimer; 1.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR005144; ATP-cone_dom.
DR   InterPro; IPR000788; RNR_lg_C.
DR   InterPro; IPR013509; RNR_lsu_N.
DR   InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR   InterPro; IPR008926; RNR_R1-su_N.
DR   NCBIfam; TIGR02504; NrdJ_Z; 1.
DR   PANTHER; PTHR43371:SF1; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR43371; VITAMIN B12-DEPENDENT RIBONUCLEOTIDE REDUCTASE; 1.
DR   Pfam; PF03477; ATP-cone; 1.
DR   Pfam; PF02867; Ribonuc_red_lgC; 2.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   DNA synthesis {ECO:0000256|RuleBase:RU364064};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00492};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364064};
KW   Reference proteome {ECO:0000313|Proteomes:UP000197679}.
FT   DOMAIN          8..103
FT                   /note="ATP-cone"
FT                   /evidence="ECO:0000259|PROSITE:PS51161"
SQ   SEQUENCE   762 AA;  84878 MW;  C89524933FE9FB8C CRC64;
     MSANKISTKV VKRNGNVVEF DENHIFDAIL KAFKSVYPDK SASYTKEHTE EVTKSVVNAI
     SGMKKAKIKV EEIQDIVESK LMGSEPKVAK AYILYRHKHA QVRLFKSSLG IEDDDLKMPL
     NSLIVLAARY LLKNEDGSLK ETPKQLFTRV AKAVASAEKN YGKSDEEVEK IEREFYEDMT
     HFNFMPNSPT LFNAGTPLGQ LSACFVLPID DSMGGIFDSL KNTALIHQSG GGTGFSFSRI
     RPENDFVKST GGVASGPISF MKIFDAATQE IKQGGKRRGA NMGILRIDHP DILNFIVAKE
     NEGVLRNFNI SVAITDDFMR TLQSGSDYNL INPRTQKVMG KLNSNAVWNL IVTMAWKTGD
     PGLVFIDRMN STYSNPVPKY GPIESTNPCG EQPLYPYDSC NLGSINLANM VRREDGKREI
     DWSKLKHTIQ LGTRFLDDVI DANKYPIPEI DRVSRAIRRI GLGVMGWADM LIELGIRYDS
     NEALILAENV MGFITETARK ASEDLAKEKG EFPEFKNSIW YKLGYPPLRN STVTTIAPTG
     TISIISGGVS QGIEPIFSVV YMRNVHESLG SDLIEVNNEF ENYSIEEGFY SDELMKKIAG
     KNSIQEVEEI PESIRKIFVT AYDVPPEWHV KMQAAFQKHT DNAVSKTINF PSYATPQDIE
     KAYLLSYKLG CKGITVYRDK SKSVQVLELV NQQSSKQSSL AESRAKHTAG TSHEVSLDEV
     KRSAVNYQIS GDKETLCPEC GTPMIASEGC YTCPNCGYSK CE
//
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