ID A0A0S4LI49_9BACT Unreviewed; 1178 AA.
AC A0A0S4LI49;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:CUS34834.1};
GN ORFNames=COMA2_190048 {ECO:0000313|EMBL:CUS34834.1};
OS Candidatus Nitrospira nitrificans.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742973 {ECO:0000313|EMBL:CUS34834.1, ECO:0000313|Proteomes:UP000198736};
RN [1] {ECO:0000313|Proteomes:UP000198736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Luecker S., Luecker S.;
RL Submitted (OCT-2015) 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}.
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DR EMBL; CZPZ01000011; CUS34834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4LI49; -.
DR STRING; 1742973.COMA2_190048; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000198736; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198736}.
FT DOMAIN 31..131
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 182..738
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 784..898
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1178 AA; 130708 MW; 810B624167E6B350 CRC64;
MRIDRRFTRR GQNPYEGITF VKRSSEIRNP DGSTVFKLDD IDVPEAWSQL AIDILAQKYF
RKAGVPQRDP NGQPLVGSDG KPVLGGERDA RQVFERMAGC WTHWGKSYGY FKTPEDAESF
HDEMCYMLAR QMAAPNSPQW FNTGLHYAYG LSGPAQGHYY VDPSTREVVK ATNAFEHPQP
HACFIQSIED DLVNENGIMD LWVREARLFK YGSGTGTNFS KLRGDGEGLS GGGKSSGLMS
FLKIGDRAAG AIKSGGTTRR AAKMVCLDLD HPDIEEFIDW KVIEEQKVAA MVTGSKICAQ
RLNAVLKACH TVDGEGALRL DLDQKTNPVL CEALTLARRD LVSEAYIQRM FSYAQQGFTH
FVFHEYDTNW DGKAYQTVSG QNSNNSVRIP NEFFALLEAD GDWQLKRRTN GKVCRTIKAR
ELWDRIAWAA WICADPGTQY DTTINEWHTC PEDGRINASN PCSEYMFLDD TACNLASLNL
TKFYTADGQF ELEHFRHAVR LWTIALEISV LMASFPSRSI AEKSYQFRTL GLGYANLGTV
LMRQGIPYDS PKALAICGAI TAIMTGEAYG TSAEMAAELS PFPGYANNRE HMLRVIRNHR
RAAYQVSHVD YEGLTITPAG IRPEHCPPDM LLAARRAWDH ALELGTAYGY RNAQVTVIAP
TGTIGLVMDC DTTGIEPDFA LVKFKKLAGG GYFKIINQSL PMALANLGYT DQQAQDIVRY
CVGARTLKGA PFINHDTLRQ KGFDDAALDR LEGSLGQAFE IQFVFNKFTL GEAFCVEKLG
MTEAQLNETT FNMLKTLGFT QEEIAAANDF CCGTMTVEGA PYLRAEHLAV FDCANRCGRI
GQRSIAVDAH IRMMAAAQPF ISGAISKTIN MPADATLEDV KAAYLLAWKS MVKAVALYRD
GSKLSQPLSA STDSGKAVET ATGVMGMAEK ITERVLVRYL AKRRPLPSRR SGYTQKAIVG
GHKLYLRTGE YEDGTVGEIF LDMHKEGAAF RSLMNCFAIA ISLGLQHGVP LEEFVEAFVF
TRFEPNGPVK LNDRIKMSTS IIDYIFRELA VTYLDRYDLA QVKEDDLRMD SMKKDNMDPE
CFEEEADLDA LAKSSIITEH LPIRRNGGKG NGHGNGHSVA RQVEIMRETV TLTEVQNAKE
AKVKGYEGDP CQECKQFTMV RNGTCLKCVT CGATSGCS
//
