ID A0A125MGA2_BACSE Unreviewed; 845 AA.
AC A0A125MGA2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=nrdZ_1 {ECO:0000313|EMBL:KWR56593.1};
GN ORFNames=AA415_00902 {ECO:0000313|EMBL:KWR56593.1};
OS Bacteroides stercoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=46506 {ECO:0000313|EMBL:KWR56593.1, ECO:0000313|Proteomes:UP000056419};
RN [1] {ECO:0000313|EMBL:KWR56593.1, ECO:0000313|Proteomes:UP000056419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL09T03C01 {ECO:0000313|EMBL:KWR56593.1,
RC ECO:0000313|Proteomes:UP000056419};
RX PubMed=26768901; DOI=10.1186/s12864-016-2377-z;
RA Coyne M.J., Roelofs K.G., Comstock L.E.;
RT "Type VI secretion systems of human gut Bacteroidales segregate into three
RT genetic architectures, two of which are contained on mobile genetic
RT elements.";
RL BMC Genomics 17:58-58(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|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:KWR56593.1}.
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DR EMBL; LRGC01000003; KWR56593.1; -; Genomic_DNA.
DR RefSeq; WP_060385393.1; NZ_LRGC01000003.1.
DR AlphaFoldDB; A0A125MGA2; -.
DR STRING; 46506.AA415_00902; -.
DR PATRIC; fig|46506.5.peg.974; -.
DR Proteomes; UP000056419; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
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; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 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 Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
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:UP000056419}.
FT DOMAIN 22..86
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 104..636
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 845 AA; 95752 MW; 36124A0BA4522059 CRC64;
MEKKVYSYDE AYEESLRYFQ GDELAARVWV NKYAVKDSFG NIYEKSPEDM HWRIANEVAR
IEAKYPNALT SEELFGLLDH FKYIVPQGSP MTGIGNNYQV ASLSNCFVIG VDGEADSYGA
IFKIDEEQVQ LMKRRGGVGH DLSHIRPKGS PVKNSALTST GLVPFMERYS NSTREVAQDG
RRGALMLSVS IKHPDSEAFI DAKMTEGKVT GANVSVKLTD AFMQAAIDGK PFVQQYPIDA
DEPLFKKEIS ATDLWKKIVH NAWKSAEPGV LFWDTILRES VPDCYADLGY RTVSTNPCGE
IPLCPYDSCR LLAINLYSYV VNPFKPDAYF DFDLFKKHVA LAQRIMDDII DLELEKIERI
MAKIDSDPEN EDVKHTESVL WQKIYKKSGQ GRRTGVGITA EGDMLAALGL RYGTEEATEF
AEKVHQTVAL SAYRSSVEMA KERGAFEVYD SEREKSNPFI NRLREADPEL YEEMKKYGRR
NIACLTIAPT GTTSLMTQTT SGIEPVFLPV YKRRRKVNPN DANVHVDFVD ETGDAFEEYI
VFHPKFVTWM QAQGYDPAKH YTQDEVDALV QKSPYYKATS NDVDWLMKVK MQGRIQKWVD
HSISVTINLP NDVDEELVNR LYVEAWKSGC KGCTVYRDGS RSGVLISTKK DKKEELPPCK
PPTVVETRPK VLEADVVRFQ NNKEKWVAFV GLLDGYPYEI FTGLQDDDEG IILPKNVSTG
HIIKNVDENG NKRYDFQFEN KRGYKVTIEG LSEKFNKEYW NYAKLISGVL RYRMPIEQVM
KLVSSLQLDS ENINTWKNGV ERALKKYVTD GTAAKGQKCP NCGNETLVYQ EGCLICTTCG
TSRCG
//
