ID Q9HMU3_HALSA Unreviewed; 804 AA.
AC Q9HMU3;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=nrdB1 {ECO:0000313|EMBL:AAG20478.1};
GN Synonyms=nrdA1 {ECO:0000313|EMBL:DAC79235.1};
GN OrderedLocusNames=VNG_2384G {ECO:0000313|EMBL:AAG20478.1};
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX NCBI_TaxID=64091 {ECO:0000313|EMBL:AAG20478.1, ECO:0000313|Proteomes:UP000000554};
RN [1] {ECO:0000313|EMBL:AAG20478.1, ECO:0000313|Proteomes:UP000000554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1
RC {ECO:0000313|Proteomes:UP000000554}, and NRC-1
RC {ECO:0000313|EMBL:AAG20478.1};
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.W., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2] {ECO:0000313|EMBL:DAC79235.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC79235.1};
RX PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
RN [3] {ECO:0000313|EMBL:DAC79235.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC79235.1};
RX PubMed=26042526;
RA Pfeiffer F., Oesterhelt D.;
RT "A manual curation strategy to improve genome annotation: application to a
RT set of haloarchael genomes.";
RL Life 5:1427-1444(2015).
RN [4] {ECO:0000313|EMBL:DAC79235.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRC-1 {ECO:0000313|EMBL:DAC79235.1};
RA Pfeiffer F., Marchfelder A., Habermann B.H., Dyall-Smith M.;
RT "The genome of the Halobacterium salinarum type strain is closely related
RT to that of the laboratory strains NRC-1 and R1.";
RL Microbiol. Resour. Announc. 0:0-0(2019).
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}.
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DR EMBL; AE004437; AAG20478.1; -; Genomic_DNA.
DR EMBL; BK010829; DAC79235.1; -; Genomic_DNA.
DR PIR; B84389; B84389.
DR RefSeq; WP_010903780.1; NC_002607.1.
DR AlphaFoldDB; Q9HMU3; -.
DR STRING; 64091.VNG_2384G; -.
DR PaxDb; 64091-VNG_2384G; -.
DR GeneID; 68694916; -.
DR KEGG; hal:VNG_2384G; -.
DR PATRIC; fig|64091.14.peg.1846; -.
DR HOGENOM; CLU_000404_3_0_2; -.
DR OrthoDB; 6188at2157; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000554; Chromosome.
DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IBA:GO_Central.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IBA:GO_Central.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000554}.
FT DOMAIN 597..619
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
FT REGION 770..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..794
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 804 AA; 91063 MW; 38FFE992FA41FEC8 CRC64;
MTHATSATSD MVAAALDRAL TDHEDDIDSD ARDRILTEAT RNAYDDATTD ERYDALLGAL
TGRIDRHPAY KTVAGRVLRE RLERRLVDDY DPATRDAATR QAFRDGIQRG LDADLLDERM
GDYDLNRLAD AITPARDDRL DYMAMDTLRQ RYFLREPDAD PFELPQPFWM RVAMGVALRE
DPADREEYAI EFYDALSTLR FVHSTPTLFH AGTTHAQLSS CYLTTVPDDL DGIFDAYKEH
AKLSKWSGGL GNDWTPLRAA GSLIESTGVE STGTVPFLKI SNDVTAAINR SGKRRGAAAA
YLACWHLDFP AFCDLRRNTG DERRRTHDMN TAAWIPDLFM ERVRADKQWT LFSPKETGDL
YELYGSDFAE RYREYEAMAD DGDIQRFERV DATDLWRTML TRLFETGHPW LTFKDPCNVR
SPQDHAGTVR SSNLCTEITL NTSEEETAVC NLGSVNLARH LDDGDIDREQ LSETVETAMR
MLDNVVDLNF YPTENAERSN MRHRPVGLGV MGFHDALQQM RVPMASDDAL DRADALQEYV
AYHAIGASAD LAAERGTYES YEGSKWDRDV FPQDTVDRLE SERGREIPVP REERLDWSDV
RQRVATHGMR NSNTMAVAPT ATISTIAGTT PSIEPVYSNL YVKSNMSGDF TVVNDRLVAD
LEERDLWTEE LRDKLTYHDG SVQELDAVPE DVQELYRTAF EIDPRHQLRL AARRGVWIDQ
SQSVNVFFPE TDGSKLSEVY QTAWELGLKT TYYLRTLGAS QIEKTTLDMD EYDDTQFRGD
DDGEDADGDG DLPSVEDPTC EVCQ
//
