ID A0A1Y5TML8_9RHOB Unreviewed; 1222 AA.
AC A0A1Y5TML8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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:SLN65507.1};
GN ORFNames=AQS8620_03028 {ECO:0000313|EMBL:SLN65507.1};
OS Aquimixticola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aquimixticola.
OX NCBI_TaxID=1519096 {ECO:0000313|EMBL:SLN65507.1, ECO:0000313|Proteomes:UP000193862};
RN [1] {ECO:0000313|EMBL:SLN65507.1, ECO:0000313|Proteomes:UP000193862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8620 {ECO:0000313|EMBL:SLN65507.1,
RC ECO:0000313|Proteomes:UP000193862};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFS01000012; SLN65507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5TML8; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000193862; 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:UP000193862}.
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..746
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 802..911
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1222 AA; 132759 MW; 1CC8A8A268C346F5 CRC64;
MKIERKFTTA GQDAYAEIEF TTTSSEIRNP DGTIVFKLDD CEIPRDWSQV ASDVIAQKYF
RKAGVPAALK KVREKGVPAF LWRSVADEDV LAKLPQADRF GGESSAKQVF DRLAGAWCYW
GWKGGYFTTE ADAKAYYDEM RFMLARQMAA PNSPQWFNTG LHWAYGIDGP GQGHYYVDFK
SGELTRSASA YEHPQPHACF IQSVADDLVG DGGIMDLWVR EARLFKYGSG TGTNFSSLRG
ANEALSGGGK SSGLMGFLKI GDRAAGAIKS GGTTRRAAKM VICDMDHPDI EEFVNWKVIE
EQKVASIVAG SKMHERQLNE IFDAIGTWDG KEVDAFDPSK NAALKAAIKS AKQVCIPETY
VKRVLDYAKQ GYAKIEFPTY DTDWDSEAYA SVSGQNSNNS VRVTDAFLKA VKDDSEWELI
KRTDGTVAKT VKARDLWEQV GHAAWACADP GIQFHDTVNA WHTCPEDGQI RGSNPCSEYM
FLDDTACNLA SMNLLTFLSD GKFLSEHYMH ATRLWTLTLE ISVTMAQFPS REIAQRSYDF
RTLGLGYANI GGLLMNLGFS YDSREGRALT GALTAIMTGV SYATSAEIAG ELGAFVKFDK
NRDHMLRVIR NHRTAAYGKA TGYEGLDVKP VPLDHAGCPD IELVELAKSA WDEALTLGET
HGFRNAQVSV IAPTGTIGLV MDCDTTGIEP DFALVKFKKL AGGGYFKIIN RSVPAALEKL
GYASNEIEEI VAYAVGHGTL GNAPGITHAS LIGHGFGQAQ IDKIEAALPS AFDIRFVFNQ
WTLGAEFCTG TLGIPAAKLN DPAFDLLRHL GFSNKDIAAA NDHVCGTMTL EGAPFLKTEH
YAVFDCANAC GKKGKRYLSV ESHITMMAAA QSFISGAISK TINMPNDATV EDCKAAYELS
WSLGIKANAL YRDGSKLSQP LASALIEDDE EAEQILATGS AQEKAAVIAE KIIEKVIIKE
VARGREKLPE RRKGYTQKAI VGGHKVYLRT GEYQDGNLGE IFIDMHKEGA GFRAMMNNFA
IAVSVGLQYG VPLEEFVDAF TFTKFEPAGM VQGNDSIKNA TSILDYIFRE LAVSYLDRTD
LAHVKPTGAA FDDLGRGEEE GLSNVKTPSE AASVKSIEVL KQISSTGYLR KRMPQELVLL
QGGATVALKD VDAATALQTL VPQAKAKPAT SSAAVTTGLD ARVKAKMQGY EGDPCGECGN
YTLVRNGTCM KCNTCGGTSG CS
//
