ID M0A4Q1_9EURY Unreviewed; 816 AA.
AC M0A4Q1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=C482_18989 {ECO:0000313|EMBL:ELY93514.1};
OS Natrialba chahannaoensis JCM 10990.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=1227492 {ECO:0000313|EMBL:ELY93514.1, ECO:0000313|Proteomes:UP000011693};
RN [1] {ECO:0000313|EMBL:ELY93514.1, ECO:0000313|Proteomes:UP000011693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10990 {ECO:0000313|EMBL:ELY93514.1,
RC ECO:0000313|Proteomes:UP000011693};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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|RuleBase:RU364064};
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|RuleBase:RU364064}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406}.
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:ELY93514.1}.
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DR EMBL; AOIN01000098; ELY93514.1; -; Genomic_DNA.
DR RefSeq; WP_006169325.1; NZ_AOIN01000098.1.
DR AlphaFoldDB; M0A4Q1; -.
DR STRING; 1227492.C482_18989; -.
DR PATRIC; fig|1227492.4.peg.3772; -.
DR OrthoDB; 6188at2157; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000011693; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0071897; P:DNA 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; IPR013346; NrdE_NrdA_C.
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 InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 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; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|RuleBase:RU364064};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 599..621
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 776..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..803
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 92676 MW; A76D74B08E2FB3E3 CRC64;
MTHHSSPTQT LDIDAVLDRA LSDQPSVLSS ADRAQLVTEI EHSLYDEASL DECYQAILQA
LTARIEREPA YKQIAAAVFR QRYYRNLLGE DLTGAALDHA YRETFVTNIE RAVELDLLDE
RLLTRFDLEE LATALEIERD EHFEYMAMET LSQRYFLKTE EHGEHLELPQ AFWMRIAMGL
ALEEDDPQQR AIEFYDVLSS LEFTPSTPTL FHSGSPHPQL SSCYLTTVQD SLENIFDSYK
HHAQLSKWSG GLGNDWTNLR SAGSLIESTG VESTGVVPFL RISNDVTSAI NRSGKRRGAA
CAYLACWHLD FPAFTDLKRN TGDERRRTPD MNTAAWIPDL FMKRVDADEE WTLFSPDEVP
DLHDLSGEAF EERYREYERQ AENGDLRQYE RIDAAELWRT MLTRLFETGH PWLTFKDPCN
VRSPQDHVGT VHSSNLCTEI TLNTSADEHA VCNLGSVNLA THVSDGELDR EHLADTIETA
MRMLDNVVDL CFYPTEEAER SNMRHRPIGL GTMGFHDALM ELGIPMHSAD AVEAANRWQE
FVSYHAILNS SKLASERGAY PSYEGSKWDQ GLLPQDTVDL LEAERGREIP TDREESLEWD
VVREHVAEHG MRNSNTMAIA PTATVSTING TTPSIEPIYS NLYVKSNMSG DFTVINDKLV
SDLKARDRWD DEMVDRLKFH DGSVQEIDSI PDDLQELYRG AFEIDPRHQL RLTAHRQTWI
DQSVSHNVFF PSTDGSLLDD VYRTAWELGL KTTYYLRTLG ASQIEKSTLD MAEYGKTQHR
DDDSTGTLDD DNSETDDADS SDELCRVDDP TCEACQ
//
