ID A0A2A9F7A3_9PSEU Unreviewed; 936 AA.
AC A0A2A9F7A3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=ATK36_1344 {ECO:0000313|EMBL:PFG46370.1};
OS Amycolatopsis sulphurea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=76022 {ECO:0000313|EMBL:PFG46370.1, ECO:0000313|Proteomes:UP000243542};
RN [1] {ECO:0000313|EMBL:PFG46370.1, ECO:0000313|Proteomes:UP000243542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46092 {ECO:0000313|EMBL:PFG46370.1,
RC ECO:0000313|Proteomes:UP000243542};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-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}.
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:PFG46370.1}.
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DR EMBL; PDJK01000002; PFG46370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9F7A3; -.
DR Proteomes; UP000243542; 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:UP000243542}.
FT DOMAIN 54..137
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 158..693
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 936 AA; 101763 MW; AF48AFDB58962AAF CRC64;
MTETVGAGAD AGRSNAKKAA GGLRVQRVFT TAGVHPYDEV AWEKRDVVMT NWRDGSVNFE
QRGVEFPEFW SVNATNIVTS KYFRGAVGSA ERESSLKQLI DRVVRTYVKA AAEFDYFAGP
ADLEVFEHEL TWMLLHQVFS FNSPVWFNVG TPSKQQVSAC FILAVDDTME SILNWYREEG
LIFKGGSGAG LNLSRIRSAK ELLTSGGTAS GPVSFMRGAD ASAGTIKSGG ATRRAAKMVV
LDVDHPDIEE FIATKAREEE KIKVLRDAGF DMDLSGADIS SVQYQNANNS VRVSDEFMQA
VENGTDFGLR ARLTGEVIER TDAKKLFRSM ARAAWECADP GLQYDGTIND WHTCPESGRI
TASNPCSEYM HLDNSSCNLA SLNLLKFVSA DGTFDAPLFA KAVEFVITAM DISICFADFP
TEPIAETTRK FRQLGIGYAN LGALLMALGH AYDSEGGRAL AGAITSLMTG VSYRRSAELA
EVVGPYEGYA RNAEAHQRVM RKHAAASELI RTYHENDKAV RALASQEWQR GIELGGRHGW
RNAQASVLAP TGTIGFMMDC DTTGIEPDFS LVKFKKLVGG GSMQIVNQTV PRALRALGYQ
DEQVEAIVEY VAQHGHVVGA PGLRSEHYEV FDCAVGERSI APMGHVRMMA AVQPFLSGAI
SKTVNMPEAA TVEDVEEIYF QGWKLGLKAL AIYRDNCKVG QPLSTAKTTE TEAEPEKLVE
YRPVRRRLPK KRPSQTVSFT VGGAEGYLHA GSYPDDGLGE IFVKLGKQGS TLAGVMDAFS
MSISVGLQHG IPLEFYVSKF SNLRFEPAGM TDDPDIRIAT SVMDYLFRRL ALDYLPYEKR
AQLGIFTAAE RSAEVEQNYG GSMDLEALRT SVDSTPSVAP GEARLEPGSA HSTAELMELH
LGKAADAPLC MTCGTKMRPA GSCYACEGCG ATSGCS
//
