ID A3TJJ4_9MICO Unreviewed; 987 AA.
AC A3TJJ4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 75.
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=JNB_00235 {ECO:0000313|EMBL:EAP98549.1};
OS Janibacter sp. HTCC2649.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=313589 {ECO:0000313|EMBL:EAP98549.1, ECO:0000313|Proteomes:UP000005063};
RN [1] {ECO:0000313|EMBL:EAP98549.1, ECO:0000313|Proteomes:UP000005063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2649 {ECO:0000313|EMBL:EAP98549.1,
RC ECO:0000313|Proteomes:UP000005063};
RX PubMed=21075932; DOI=10.1128/JB.01298-10;
RA Thrash J.C., Cho J.C., Bertagnolli A.D., Ferriera S., Johnson J.,
RA Vergin K.L., Giovannoni S.J.;
RT "Genome sequence of the Marine Janibacter Sp. Strain HTCC2649.";
RL J. Bacteriol. 193:584-585(2011).
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:EAP98549.1}.
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DR EMBL; AAMN01000002; EAP98549.1; -; Genomic_DNA.
DR RefSeq; WP_009774360.1; NZ_CH672413.1.
DR AlphaFoldDB; A3TJJ4; -.
DR STRING; 313589.JNB_00235; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_0_1_11; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000005063; 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:UP000005063}.
FT DOMAIN 50..133
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 154..689
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 864..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 106531 MW; 7652A58C6E677FE6 CRC64;
MTETAGRTGA RKATKGKGVV VERIFTTPGV HPYDAVTWEK RDVVQQNWKT GETIFEQRGV
EFPDFWSVNA STIVTTKYFR GAVGTEARET GLKQLIDRVV LTYVKAGKEH DYFSSDEDAE
LFEHELTYAL LHQVFSFNSP VWFNVGTASP QQVSACFILA VDDSMDSILN WYKEEGFIFK
GGSGAGLNLS RIRSSKELLS SGGTASGPVS FMRGADASAG TIKSGGATRR AAKMVVLDVD
HPDIVEFVET KAREEDKIRA LRDAGFDMDL GGKDIVSVQY QNANNSVRVN DEFMRAVEEG
TEFGLKSRGD GSVIETIDAR ELMGKIAKAA WECADPGIQY DDTINDWHTN PETGRITASN
PCSEYMSLDN SSCNLASLNL LKFLKDDDTF DVVKFQQVAE LVITAMDISI CFADFPTEPI
AKTTRDYRQL GIGYANLGAL LMATGHGYDS DGGRALAASI TSLLTGAAYK RSAEIAGVVG
PYAGYARNAD AHKRVMRKHA SANDSIRTMQ TMDKDIHRAA TKAWDAVVKV GEKNGYRNAQ
ASVLAPTGTI GFMMDCDTTG IEPDFSLVKF KKLVGGGSMQ IVNLTIPRAL RKLGYTEETV
EAIVEFIADK GHVIDAPGLK TEHYEIFDTA MGARSISAMG HVRMMAATQP FLSGAISKTV
NLPEDASVEE IQDVYMQGWK MGLKALAVYR DSCKVGQPLS DGGSTAKDAA TDKAAGVAAA
AAGPAQVVEK VVYRPTRERL PKRRCSQTTS FAIGGAEGYL TAGTYADGRL GEVFLKFGKQ
GSTLAGVMDA FSIAVSVGLQ YGVPLETFVE KYSNMRFEPA GMTDDQDIRM GQSLVDYVFR
RLALDHLDFE TRSFMGIHTA EERQRQLETG SYAPSTVEGD DTEALEDEIE SYSQGVGATS
PKKTAEVAPK GDSPAVDTED HSIEDKSGAG AASAREVSGD IHSSAELMEK FQGVSADAPM
CMTCGTKMRP AGSCYVCEGC GSTSGCS
//
