ID Q5L9C8_BACFN Unreviewed; 882 AA.
AC Q5L9C8;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=BF9343_3519 {ECO:0000313|EMBL:CAH09300.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH09300.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH09300.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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}.
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DR EMBL; CR626927; CAH09300.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5L9C8; -.
DR PaxDb; 272559-BF9343_3519; -.
DR KEGG; bfs:BF9343_3519; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_2_10; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
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 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 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:UP000006731}.
FT DOMAIN 139..671
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 882 AA; 100247 MW; 0FFD65F57AC58F5F CRC64;
MIYQKTFIAL QARLLMISKL LHIYLLIKKS KTHCIVEKQI YSYEEAFEES LRYFQGDELA
ARVWVNKYAV KDSFGNIYEK SPKDMHWRLA NEVARIEAKY PNALSSEQLF ELFDHFKYIV
PQGSPMTGIG NDYQVASLSN CFVIGIDGSA DSYGAIIKID EEQVQLMKRR GGVGHDLSHI
RPKGSPVKNS ALTSTGLVPF MERYSNSTRE VAQDGRRGAL MLSVSIKHPD SEAFIDAKMT
EGKVTGANVS VKLDDAFMSA AVEGRKYTQQ YPIDSDHPTT VKEIEASNLW KKIVHNAWKS
AEPGVLFWDT IIRESVPDCY ADLGYKTVST NPCGEIPLCP YDSCRLLAIN LYSYVVNPFT
KDAYFDFDLF HKHVALAQRI MDDIIDLELE KIERIIEKID QDPENEEVKH TERGLWEKIY
KKSGQGRRTG VGITAEGDML AALGMRYGTE EATEFSEKVH KAVALGAYRS SVDMAKERGA
FDVYDSEREK NNPFINRLRE ADPALYEDMK KYGRRNIACL TIAPTGTTSL MTQTTSGIEP
VFLPVYKRRR KVNPNDTNVR VDFVDETGDA FEEYIVFHHK FVTWMEANGY DPAKRYTQEE
IDELVAKSPY YKATSNDVDW LMKVRMQGKI QKWVDHSISV TINLPNDVDE ELVNRLYVEA
WKSGCKGCTV YRDGSRSGVL ISAKSDKDKK EELPPCKPPT VVEVRPTVLE ADVVRFQNNK
EKWVALVGLL DGRPYEIFTG LQDDDEGIII PKSVNTGRII KNVDENGNKR YDFQFENKRG
YKMTIEGLSE KFNKEYWNYA KLISGVLRWR MPIEQVIKLV GSLQLDSENI NTWKNGVERA
LKKYVQDGTE AKGKKCPNCG NETLVYQEGC LICTTCGASR CG
//
