ID L0ID61_HALRX Unreviewed; 1038 AA.
AC L0ID61;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=Halru_2113 {ECO:0000313|EMBL:AGB16704.1};
OS Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB16704.1, ECO:0000313|Proteomes:UP000010846};
RN [1] {ECO:0000313|Proteomes:UP000010846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18193 / JCM 13892 / XH-70
RC {ECO:0000313|Proteomes:UP000010846};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA Anderson I., Woyke T.;
RT "Complete sequence of Halovivax ruber XH-70.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; CP003050; AGB16704.1; -; Genomic_DNA.
DR AlphaFoldDB; L0ID61; -.
DR STRING; 797302.Halru_2113; -.
DR KEGG; hru:Halru_2113; -.
DR eggNOG; arCOG03713; Archaea.
DR eggNOG; arCOG04276; Archaea.
DR HOGENOM; CLU_000404_2_1_2; -.
DR OrthoDB; 6188at2157; -.
DR Proteomes; UP000010846; Chromosome.
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; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
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; 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.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628, ECO:0000256|RuleBase:RU364064};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|RuleBase:RU364064};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|RuleBase:RU364064};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364064};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846}.
FT DOMAIN 33..171
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 175..772
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 956..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 114787 MW; A03AD0D141D60B82 CRC64;
MSESDRAVDE ITLPVKRNEG ETLADRMTDN AYENILPARY LRKDADGELI ETQEDLFDRV
GKNIALAEAV YEANNQDVEI TVTPDQLKPD HPRRDELAAE VFGAGTTVED DVETTLTEHN
VNKFAYDTIV PELPASVREH VEDVTETFVE GMSSLSFMPN SPTLMNAGDE LQQLSACFVM
SPQDDLSNIH ETAKKAAEVF QSGGGVGYGF WQLRPYGDSV GSTGGIASGP ITFMRTYDQL
CETIAQGGTR RGAQMGIMRV SHPDVIEFIH AKNKDVSLAH CLRLNDPDDY TYTTFSEALE
EARGLIDEDG RVPKHLRNAV EGHLSNFNIS VGVTDSFMEA LQNGEEYTFT NPRTEEPHIA
TAETKEMYSR YDLGEHVEVG EPLSIPAELV WERIVEGAHE NGEPGVIYLE RVNKEHSFDV
EKHPDHRIKA TNPCGEQPLE EFEACNLGHI NLSTLADLDA PDWRVWADEH ADEYPSQDAA
IEGFLEEAID FEEFDDRIEY GTRFLENVVT MSDFPVDEIE QTVRDMRKIG LGIMGLAQLY
VQLGVRYGSD AGNEIARQLM THINHEAKWT SHELALERDS FNDWDDSKYA DPQEYREWFE
QQTGLDAEKY PDGFPIRNHN VTTIAPTGTT SMVGNTTGGC EPIYNVAYYK NVTDDVQGDE
MLVEFDDYFL RTLEDNDIDV DAVKAEAQDQ MANNEFDGVE GLETVPDAIG ELFVITADIS
AKQHAAVQCA CQAGVDSAIS KTVNAPNDSS IEDAKEVFEW VYENGGKGVT YYRDGTRSKQ
VLTTRADNAE FADEDEAAEV IVEQIRDVFG SLEAFFESED VQSVAEDELT ALLSADVDYT
EKRERPDSLQ GVSQRIDTGY GKVYVTINEE PETGQPFELF ANIGHSGGFT NSFTEALAKV
ISTALRSGVD PEEIVDELCG TRSPKVAWDK GEQIQSIPDA IGTAMRRYLA NEIDKPYPKQ
QTLGESADDV TTDADASATS VAPDEPEPDG GAAARQSADA TQDLIDAGES PECPDCGSLS
LYFSEGCKTC ESCGWSEC
//
