ID A0A0Q9AV65_9ACTN Unreviewed; 966 AA.
AC A0A0Q9AV65;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=ASE41_11755 {ECO:0000313|EMBL:KRD22605.1};
OS Streptomyces sp. Root264.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD22605.1, ECO:0000313|Proteomes:UP000051177};
RN [1] {ECO:0000313|EMBL:KRD22605.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD22605.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD22605.1, ECO:0000313|Proteomes:UP000051177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root264 {ECO:0000313|EMBL:KRD22605.1,
RC ECO:0000313|Proteomes:UP000051177};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRD22605.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMIZ01000005; KRD22605.1; -; Genomic_DNA.
DR RefSeq; WP_057575374.1; NZ_LMIZ01000005.1.
DR AlphaFoldDB; A0A0Q9AV65; -.
DR STRING; 1736503.ASE41_11755; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000051177; 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:UP000051177}.
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..697
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 105432 MW; 1A7E1897D1D54F74 CRC64;
MTETASGPAR GSRAKGSKTT KGLRIERVHT TPGVHPYDEV VWERRDVVMT NWRDGSVNFE
QRGVEFPDFW SVNAVNIVTS KYFRGAVGTP QRETGLRQLI DRIVKTYRKA GEDHSYFASP
ADAEIFEHEL AYALLHQIFS FNSPVWFNVG TPQPQQVSAC FILAVDDSME SILDWYKEEG
MIFKGGSGAG LNLSRIRSSK ELLSSGGNAS GPVSFMRGAD ASAGTIKSGG ATRRAAKMVV
LDVDHPDVED FIATKVKEEE KIRALRDAGF DMDLGGDDIT SVQYQNANNS VRVNDEFMTA
VENGTEFGLR ARMTGEIIEK VDAKALFRKL AEAAWACADP GIQYDGVINN WHTCPESGRI
TASNPCSEYM HLDNTSCNLA SLNLMKFLKD DSKGHQSFDA DRFQKVVELV ITAMDISICF
ADFPTQKIGE NTRAFRQLGI GYANLGALLM ATGHAYDSDG GRSLAGAITS LMTGTAYRRS
SELAAVVGPY DGYARNSDAH NRVMKQHSDA NATAVRMDDL DTPVWAAATE AWQDVLRLGE
KNGFRNSQAS VLAPTGTIGL AMSCDTTGVE PDLALVKFKK LVGGGSMQIV NGTVPQALRR
LGYQEEQIEA IVAHIAENGN VIDAPGLAHE HYEVFDCAMG ERAISPMGHV RMMAAIQPWI
SGAISKTVNM PETATVEEVE EIYFEAWKLG VKALAIYRDN CKVGQPLSAK TKEKEKTEVT
EKTEETIRAA VEKVIEYRPV RKRLPKGRPG ITTSFTVGGA EGYMTANSYP DDGLGEVFLK
MSKQGSTLAG MMDAFSIAVS VGLQYGVPLE TYVSKFTNMR FEPAGMTDDP DVRMAQSIVD
YIFRRLALDF LPFETRSALG IHSAEERQRH LETGSYEPTF EEENVDVEGL AQSAPRQTDL
KAVATPKAEV EAVEPAPKQV HTSAELVEMQ LGIQADAPLC FSCGTKMQRA GSCYICEGCG
STSGCS
//
