ID A0A0M6XSA6_9RHOB Unreviewed; 1220 AA.
AC A0A0M6XSA6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
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:CTQ34046.1};
GN ORFNames=JAN5088_02838 {ECO:0000313|EMBL:CTQ34046.1};
OS Jannaschia rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ34046.1, ECO:0000313|Proteomes:UP000048908};
RN [1] {ECO:0000313|EMBL:CTQ34046.1, ECO:0000313|Proteomes:UP000048908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ34046.1,
RC ECO:0000313|Proteomes:UP000048908};
RA Noorani M.;
RL Submitted (JUL-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; CXPG01000021; CTQ34046.1; -; Genomic_DNA.
DR RefSeq; WP_055683442.1; NZ_FOOS01000003.1.
DR AlphaFoldDB; A0A0M6XSA6; -.
DR STRING; 282197.SAMN04488517_103300; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000048908; 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 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:UP000048908}.
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..749
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 808..912
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1220 AA; 132395 MW; A894EC921BA9D1D0 CRC64;
MRLERKFTEA GKDAYAALTF TTTTSEIRNP DGTVVFHLDA VEIPEGWSQV ASDVIAQKYF
RKAGVAARLK KVPEKDVPEF LWRSVPDDAA LAELPADERF GGETSSRQVF DRLAGAWAYW
GWKGGYFTTE DDARTYFDEM RVMLARQMAA PNSPQWFNTG LHWAYGIDGP AQGHHYVDPK
TGKLIRSKSS YEHPQPHACF IQSVSDDLVN DGGIMDLWVR EARLFKYGSG TGTNFSSLRA
AGENLSGGGK SSGLMGFLKI GDRAAGAIKS GGTTRRAAKM VIVDMDHPDI EQFIDWKVVE
EQKVAALVAG SKAHQAQLTK VMEAVRAWDG SLDDACDPAV NETLKSVIRG AKKHMIPEAY
ILRVLQYARQ GYDSIEFPTY DTDWDSEAYN SVSGQNSNNS VRVTNAFLHA VEKDADWELT
NRTDGRVAKT VRARDLWDKV GHAAWACADP GIQFHDTVND WHTCPADGAI RGSNPCSEYM
FLDDTACNLA SMNLLKFLNA DGSFDHDGYV HASRFWTITL EISVAMAQFP SKEIAQRSYD
FRTLGLGYAN IGGLLMNMGL GYDSREGRAL CGALTAVMTG VSYATSAEMA GELGPFPGYA
RNAAHMQRVM RNHRTAAQGR TEGYEKLAVK PVALDMEGCP DKQLTDLARK IWDEVVEAGE
KHGFRNAQST VIAPTGTIGL VMDCDTTGIE PDFALVKFKK LAGGGYFKII NQSVPAALRK
LGYGEAQIGE IIAYAVGHGS LGNAPGINHT ALIGHGFGQA ELDKIEKALP SAFDIRFVFN
QWTLGAEFCT GTLGIPAAKL ADPTFDLLRH LGFSKKDIEA ANDHVCGTMT LEGAPGLKDE
HLTVFDCANP CGKKGKRFLS VESHIHMMAA AQSFISGAIS KTINMPNSAT IGDCKAAYEL
SWSLGVKANA LYRDGSKLSQ PLAAALIEDD DEAAEVLETG TPTARGQVLA EKVIEKIIVK
ELVRSHRVKM PERRKGYTQK ATIGGHKVYV RTGEYQDGTL GEIFIDMHKE GAGFRAMMNN
FAIAVSVGLQ YGVPLEEFVD AFTFTKFEPA GMVQGNDSIK NATSILDYIF RELAVSYLDR
EDLAHVKPEG ATFDSIGEAE APAGEDGNVE ATGQSAASKS LEVIKSVTSS GYLRKRLPRD
LVALRGGADR VAAQIAGTTT MTVARSETST LSVATDLDAR TKAKMQGYEG EACGECGNYT
LVRNGTCMKC NTCGGTSGCS
//
