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
//