ID A0A1F7TIP6_9BACT Unreviewed; 1193 AA.
AC A0A1F7TIP6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=A3J27_03090 {ECO:0000313|EMBL:OGL65851.1};
OS Candidatus Tectomicrobia bacterium RIFCSPLOWO2_12_FULL_69_37.
OC Bacteria; Nitrospinae/Tectomicrobia group; Candidatus Tectomicrobia.
OX NCBI_TaxID=1802343 {ECO:0000313|EMBL:OGL65851.1, ECO:0000313|Proteomes:UP000176745};
RN [1] {ECO:0000313|EMBL:OGL65851.1, ECO:0000313|Proteomes:UP000176745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGL65851.1}.
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DR EMBL; MGDP01000074; OGL65851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7TIP6; -.
DR Proteomes; UP000176745; 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; -; 3.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR029072; YebC-like.
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; 2.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF75625; YebC-like; 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}.
FT DOMAIN 31..147
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 198..754
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 822..915
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1193 AA; 131514 MW; 07580DDF81409B38 CRC64;
MKIARYFTRA GDDLYAGIQF VPRTSRIVNP DGSVVFEAKD ILVPETWSQV AVDILAQKYF
RKAGVPARLA RVAEDGVPEW LQPSLPDEPA LAVLPEGQRF TGETDARQIF HRMAGCWTYW
GWKHGYFGGE EDARAFYAEL VHMLAAQMGA PNSPQWFNAG LHWAYGIAGP SQGHFYCDPA
TGEVQRSPNA YERPQPHACF IQSVRDDLVN EGGIMDLWTR EARIFKYGSG TGTNFGTLRA
EGESLSGGGR SSGLMSFLKI GDRAAGAIKS GGTTRRAAKM VTLDVDHPDI EEFVNWKVRE
EQKVAALVSG SRMCRRHMNA ILAACRPEGK ADLNGGLLRP DKNPELRKAI LEARRAGVPD
NYIFRAIQLA QQGKAEIDVE EFDTNWEGEA YTTVSGQNSN NSVRITDGFM KAAEKGEPWK
LIRRTDRKVA REVPAKKLWD DIGYAAWCCA DPGLQFDTTI NDWHTCAADG RINASNPCSE
YMFLDDTACN LASLNLVRFL NLESGHFRVD DFRHAVRVWT VVLEISVLMA QFPSVAIAQR
SYEYRTLGLG YANLGTLLML LGIPYDSPEG EAWCGGITSV MTGCSYAASA EMAGELGPFP
RYHANREHML RVLRNHRRAA YSTPVQEYEM LSKAPAGIAP DRCPAYLLAA AREAWDEALA
LGYRSGFRNA QATVIAPTGT IGLVMDCDTT GIEPDFALVK FKKLAGGGYF KIINQSVPAA
LRRLGYGEEQ IRDIVAYCRG RGTLTSAPHI NPESLKAKGF TEKAIEKVEA ALEGAFELPF
AFNKHVLGEE FCRERLGLTE EQLAGWSLNL LGAMGFTPAQ IREANDYVCG KMTIEGAPHL
REEHLPVFDC ASKCGRDGRR YISPMAHVRM MAAAQPFISG AISKTINMPT EAAIQDIQDL
YHESWRLMAK AIAIYRDGSK LSQPLSGQHG ADLFEGIGEE AAEAESAPLR LAQQIVRRYV
IHKTGRRKLP TRRAGYTQKA IVGGHKVYLR TGEYEDGAIG EIFIDMHKEG AAFRSLMNCF
AIAISLGLQH GVPLDEFVDA FVFTRFEPSG VVEGNRTIKM STSIIDYIFR ELAITYLGRH
ELAQVMPEDL RSDTLGRPKD EIPDFDAEEA EEQVQTVLPF PRTETPRSEH LHLHRKAEQA
AAPGAAPRRG GVAEEAKFKG YVGEACGECG SFAVVRNGTC LKCLDCGATS GCS
//
