ID A0A346Y751_9ACTN Unreviewed; 1231 AA.
AC A0A346Y751;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274};
DE AltName: Full=Ribonucleoside-diphosphate reductase NrdJ {ECO:0000256|ARBA:ARBA00033050};
GN ORFNames=DVS28_b0558 {ECO:0000313|EMBL:AXV10298.1};
OS Euzebya pacifica.
OG Plasmid pedy32-46i {ECO:0000313|Proteomes:UP000264006}.
OC Bacteria; Actinomycetota; Nitriliruptoria; Euzebyales.
OX NCBI_TaxID=1608957 {ECO:0000313|EMBL:AXV10298.1, ECO:0000313|Proteomes:UP000264006};
RN [1] {ECO:0000313|EMBL:AXV10298.1, ECO:0000313|Proteomes:UP000264006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY32-46 {ECO:0000313|EMBL:AXV10298.1,
RC ECO:0000313|Proteomes:UP000264006};
RC PLASMID=pedy32-46i {ECO:0000313|Proteomes:UP000264006};
RA Xu L., Wu Y.-H., Xu X.-W.;
RT "Complete genome sequence of Euzebya sp. DY32-46 isolated from seawater of
RT Pacific Ocean.";
RL Submitted (SEP-2018) 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}.
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 -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|ARBA:ARBA00007405}.
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DR EMBL; CP031166; AXV10298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A346Y751; -.
DR KEGG; euz:DVS28_b0558; -.
DR Proteomes; UP000264006; Plasmid pedy32-46i.
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; -; 2.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
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; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
PE 3: Inferred from homology;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plasmid {ECO:0000313|EMBL:AXV10298.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000264006}.
FT DOMAIN 68..165
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 216..705
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 780..883
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1164..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1231 AA; 130548 MW; AC06EDB0DC935CFC CRC64;
MSTLTPTDVI RPSLDELLLP TGHPDHPPVY DAKDGLRVDR RNTVAGVSPF ESTTWVSKPW
QIFDKGTVVA EGTYEVPEAM GSTAVSITAS KYARKTLVPQ YDLVTGELIR DADGQVVLGR
ETSLKMTVAR IANAFMFWGQ SGGYFASAED AAAFRDEMLY LLIHQKAANN SPVWFNVGIH
EAYGIIESAS GNVYYDPDLG EVLASPHRYF RAAVNACFIT VINDTLVDNA VGSMTEKSIF
GNIMDEARLF KDGSGAGANW SMIRAAGEPL TGGGTSSGVI SFLKVADVAA GSIKSGGYAR
RAAKMVVLDV DHPEVREFIG LKVEAERMIP FLEAGGYPVA WNDPKGAYAQ VPWQNANHTV
SVSHDFMDAV RTDRSIDLTA RKAVGEDGNP LVMDTVRARE LWDDIAEAAW ECADPGLHFN
GTMNDWATAP NDGPIRGSNP CSEYLHVDGT ACNLASLRLT GWWDPSTGFD IDGFAHASRV
YTIGLEIAVH MSHYPSATVA FNSYEHRTLG LGICDIGGLL MRSGIGYDSD EGRAVSGAIQ
ALQTAVAYET SAEMARALGP CKAYERNTAE MQRVLRNHRR AAYGTLAADR AVGDYEGLTV
TPVGIDHGVL ARTPFASLSP AAVAAGDRMV DAVAEHGARN MQTTVTAPTG TIGMFMEADT
TGPEPLYSFV AFKTLAGGGA VKLTDTAVSA GLLYLGYTPQ QVRDVEVHIA GTGTLDGDQP
VNRRILAAAG VPADVIAAVE SGLSNAMDLR SAFGPWLLTG EEAESFATAN GITSATGNWL
DELGFTTEEI DASSRAICGH HNITHAPHVS DEHKAIFLVA DAGGEDGRSL DWQGHVRMLG
ATAPFLSGAA SKTVNLPGDA TVDDIRDCHQ LAYELGVKAV AVYRDGSKYS QPLSSAGTLK
QKPTIVVDGE VKVSTAPQPT EAEAVPVAPA EPVDSYAVVA DAIRSGAAPI GHVEELRELL
DLGTESVGLS ADEFARALDT KDKHALKELL AQLGDIPEGM SPQGFYEGRS PRKFRMPSVR
ASVTEKFTIG GQDVFLTHGA YPDGTCGEFF LKLSKEGGTT EGLTSMLATV GSMALQRGVP
LKEIVDKFVG QRFEPSGIVA GHPNLKMASS ILDAVGRILA FRYLNGDGDY EKYVQVQDNP
FVTTPTAWQP GLALDGIEAA PKSRAASPAA VPGPSPVSPV AGHESLLDIG DAPDASKMLG
GKTCHDCGFD AMFPNGICDV CRHCGSSSGC S
//
