ID A0A1S2K5W8_9ACTN Unreviewed; 960 AA.
AC A0A1S2K5W8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=BJP40_24245 {ECO:0000313|EMBL:OII63504.1};
OS Streptomyces sp. CC53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII63504.1, ECO:0000313|Proteomes:UP000179639};
RN [1] {ECO:0000313|EMBL:OII63504.1, ECO:0000313|Proteomes:UP000179639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC53 {ECO:0000313|EMBL:OII63504.1,
RC ECO:0000313|Proteomes:UP000179639};
RA Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT transport.";
RL Submitted (OCT-2016) 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:OII63504.1}.
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DR EMBL; MKXB01000137; OII63504.1; -; Genomic_DNA.
DR RefSeq; WP_071280477.1; NZ_MKXB01000137.1.
DR AlphaFoldDB; A0A1S2K5W8; -.
DR STRING; 1906740.BJP40_24245; -.
DR Proteomes; UP000179639; 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:UP000179639}.
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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 104546 MW; 43791B922FC02A3E CRC64;
MTETASGSAR GSRSKGTKAS KGMRVERVHT TPGVHPYDEV VWERRDVVMT NWRDGSVNFE
QRGVEFPDFW SVNAVNIVTS KYFRGAVGTP QRETGLKQLI DRIVKTYRKA GEDHGYFASP
ADAEIFEHEL AYALLHQIFS FNSPVWFNVG TPQPQQVSAC FILSVDDSME SILDWYKEEG
MIFKGGSGAG LNLSRIRSSK ELLSSGGNAS GPVSFMRGAD ASAGTIKSGG ATRRAAKMVI
LDVDHPDVED FIQTKVKEEE KIRALRDAGF DMDLGGDDIT SVQYQNANNS VRVNDEFMKA
VETGGQFGLR ARMTGEVIEE IDAKSLFRKM AEAAWACADP GIQYDDTINH WHTCPESGRI
NGSNPCSEYM HLDNTSCNLA SLNLMKFLKD DGKGNQSFDA ERFQKVVELV ITAMDISICF
ADFPTQKIGE NTRAFRQLGI GYANLGALLM ATGHAYDSDG GRALAGAITS LMTGTAYRRS
AELAAVVGPY DGYARNAEAH QRVMKQHADA NGTAVRMDDL DTPVWAAATE AWQDVIRLGE
KNGFRNSQAS VLAPTGTIGL AMSCDTTGVE PDLALVKFKK LVGGGSMQIV NGTVPQALRR
LGYQEEQIEA IVAHIAEHGN VIDAPGLKQE HYEVFDCAMG ERAISPMGHV RMMAAIQPWI
SGAISKTVNM PESATVEEVE EIYFEAWKLG IKALAIYRDN CKVGQPLSAK KKEEEKKAEP
EAAVVPTKVE KVVEYRPVRK RLPKGRPGIT TSFTVGGAEG YMTANSYPDD GLGEVFLKMS
KQGSTLAGMM DAFSIAVSVG LQYGVPLETY VSKFTNMRFE PAGMTDDPDV RMAQSIVDYI
FRRLALDFLP FETRSALGIH SAEERQRHLE TGSYEPVDED VDVEGLAQSA PRATEAPKPA
APEAKAEVPA PQQAHTSAEL VEMQLGIQAD APLCFSCGTK MQRAGSCYIC EGCGSTSGCS
//
