ID A0A285EFW6_9ACTN Unreviewed; 956 AA.
AC A0A285EFW6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN06893097_108233 {ECO:0000313|EMBL:SNX97867.1};
OS Geodermatophilus sabuli.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1564158 {ECO:0000313|EMBL:SNX97867.1, ECO:0000313|Proteomes:UP000219514};
RN [1] {ECO:0000313|EMBL:SNX97867.1, ECO:0000313|Proteomes:UP000219514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46844 {ECO:0000313|EMBL:SNX97867.1,
RC ECO:0000313|Proteomes:UP000219514};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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|ARBA:ARBA00025437, 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; OBDO01000008; SNX97867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285EFW6; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000219514; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide 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 CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 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|ARBA:ARBA00022634,
KW 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:UP000219514}.
FT DOMAIN 56..139
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 160..695
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 103668 MW; 7B4A7CC743FAC641 CRC64;
MTETEDRLSG RTRRATKAPT RGKGLKIKRV FTTAGVHPYD EVTWERRDVV MTNWRDGSIN
FEQRGVEFPA EWSINATNIV TTKYFRGAVG TPQRESSLRQ LIDRVVLTYG QAGREHGYFA
TEGDAEIFEH ELTWMLLHQY FSFNSPVWFN VGTSAPQQVS ACFILAVDDT MDSILNWYRE
EGLIFKGGSG AGLNLSRIRS SKELLSSGGT ASGPVSFMRG ADASAGTIKS GGATRRAAKM
VVLDIDHPDI EEFIETKARE EDKIRALRDA GYDMDLGGKD ITSVQYQNAN NSVRVSDEFM
RAVEDGTEFG LRARLDGTVI ETVDAKSLFR KVTQAAWECA DPGIQYDDTI NDWHTNPETG
RINASNPCSE YMSLDNSSCN LASLNLMKFL KDDGTFDSKN FVKAVELVIT AMDISICFAD
FPTDPIGETT RAYRQLGIGY ANLGALLMAT GHAYDSRGGQ TLAAAITSLM TGTAYRRSAE
LAGIVGAYEG YARNADAHAR VMRKHAAAND AIRPVGADDA DVLKAATAQW QECLEIGSDS
GWRNAQASVL APTGTIGFMM DCDTTGIEPD FSLVKFKKLV GGGSMQIVNQ TVPRALKSLG
YQDEQIEAIV EYIAEHGHVV DAPSLRPEHY EVFDCAMGER AISPMGHVRM MAAVQPFISG
AISKTVNMPE SATIEDVENI YFQGWKLGLK ALAIYRDNCK VGQPLSGGKG KNDGTKDEAK
VEAAAPAALA HPVRKRLPKK RTSVTTSFSV AGAEGYMTAG MYDDGSLGEV FLKLGKQGST
LAGVMDAFSI SLSIALQHGV PLETYIQKFT NMRFEPAGMT DDPDIRIAQS VMDYIFRRLA
LDHLPVDKRA NLGIFSAEER AAQVSGYDTS ASTATVAEED EVDLEALRGS APTEAPTKPE
AKAEKPVKEA HSSAELLELV TGTATDAPLC MTCGTKMRPA GSCYVCEGCG STSGCS
//
