ID A0A1D2IAB8_9ACTN Unreviewed; 966 AA.
AC A0A1D2IAB8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, 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 Name=nrdJ {ECO:0000313|EMBL:ODA71436.1};
GN ORFNames=APS67_004403 {ECO:0000313|EMBL:ODA71436.1};
OS Streptomyces sp. AVP053U2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1737066 {ECO:0000313|EMBL:ODA71436.1, ECO:0000313|Proteomes:UP000054731};
RN [1] {ECO:0000313|EMBL:ODA71436.1, ECO:0000313|Proteomes:UP000054731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AVP053U2 {ECO:0000313|EMBL:ODA71436.1,
RC ECO:0000313|Proteomes:UP000054731};
RA Olsen C.W., Carey S., Hinshaw L., Karasin A.I.;
RL Submitted (JUN-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:ODA71436.1}.
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DR EMBL; LMTQ02000026; ODA71436.1; -; Genomic_DNA.
DR RefSeq; WP_062191152.1; NZ_LMTQ02000026.1.
DR AlphaFoldDB; A0A1D2IAB8; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000054731; 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:UP000054731}.
FT DOMAIN 55..138
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 159..698
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 105211 MW; B7E4D35FCD1BD9ED CRC64;
MTETASGPTR SSRTKGSGKA GKGLRVERIH TSPGVHPYDE VAWERRDVVM TNWRDGSVNF
EQYGVEFPDF WSVNAVNIVT SKYFRGAVGT PQRETGLKQL IDRIVKTYRK AGEDHKYFAS
PADAEIFEHE LAYALLHQIF SFNSPVWFNV GTPQPQQVSA CFILSVDDSM ESILDWYKEE
GMIFKGGSGA GLNLSRIRSS KELLSSGGNA SGPVSFMRGA DASAGTIKSG GATRRAAKMV
ILDVDHPDIE DFIQTKVKEE EKIRALRDAG FDMDLGGDDI TSVQYQNANN SVRVNDTFMK
AVQDGGTFGL TSRMTGEVIE EVEAKALFRK MAEAAWACAD PGIQYDDTIN HWHTCPESGR
INGSNPCSEY MHLDNTSCNL ASLNLMKFLE DDSKGNQSFD AERFSKVVEL VITAMDISIC
FADFPTRKIG ENTRAFRQLG IGYANLGALL MATGHAYDSD GGRALAGAIT SLMTGTSYRR
SAELAAVVGP YDGYARNAQP HLRVMKQHSD ENAKAVRMDD LDTPVWAAAT EAWQDVLSLG
EKNGFRNSQA SVIAPTGTIG LAMSCDTTGL EPDLALVKFK KLVGGGSMQI VNGTVPQALR
RLGYQEEQIE AVVAHIAEHG NVIDAPGLKH EHYEVFDCAM GERSISAMGH VRMMAAIQPW
ISGALSKTVN LPESATVEDV EEVYFEAWKM GVKALAIYRD NCKVGQPLSA KTKEKEKAEI
TERTEDTIRA AVEKVVEYRP VRKRLPKGRP GITTSFTVGG AEGYMTANSY PDDGLGEVFL
KMSKQGSTLA GMMDAFSIAV SVGLQYGVPL ETYVSKFTNM RFEPAGMTDD PDVRMAQSIV
DYIFRRLALD FLPFETRSAL GIHSAEERQR HLETGSYEPT DDEVDVEGLA QSAPRAAQEL
KAVSTPKAGA EAAKPAPQQA HTSAELVEMQ LGIQADAPLC FSCGTKMQRA GSCYICEGCG
STSGCS
//
