ID A0A1Y6K571_9CHLR Unreviewed; 856 AA.
AC A0A1Y6K571;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=CFX1CAM_1760 {ECO:0000313|EMBL:SMX54825.1};
OS Brevefilum fermentans.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Brevefilum.
OX NCBI_TaxID=1986204 {ECO:0000313|EMBL:SMX54825.1, ECO:0000313|Proteomes:UP000195514};
RN [1] {ECO:0000313|Proteomes:UP000195514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kirkegaard R., Mcilroy J S.;
RL Submitted (MAY-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|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; LT859958; SMX54825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6K571; -.
DR KEGG; abat:CFX1CAM_1760; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000195514; Chromosome i.
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; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR008926; RNR_R1-su_N.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
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.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 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:UP000195514}.
FT DOMAIN 26..105
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 108..640
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 856 AA; 94925 MW; C7A51896A6266D72 CRC64;
MTDSEQIQSN ELLPTPPLPE NLPRVNLSEN AHQVISRRYR RKGENGSLIE TVEEMFWRVA
YHVAKVETVN PISVDARAQD FYHLLAEKKF FPNSPTFTGA GTPLGQLAAC FVLPISDDMG
RQEDGIFSTL RNAALIQQTG GGNGFSFSRL RPSGARVKSS AGIATGPIGF LRVYDQAFDE
VAQGGTRRGA NMGTLRVDHP DIEQFVTCKT DENAITNFNI SVGITDAFME AVKADLDWEL
RFPDETAPEY KTFNGDLDEA IANNIPIKVH KVVRARELFD KIVTQAHHNG EPGLLFIDAA
NRDNPVPHLY PLESTNPCGE QWLGPFENCC LASINLAEHL VPEHTIDWRE LQKTVETATI
FLDDVIDANA YVPAVPQLKE AAQNSRRIGL GIMGLGDLLY HVQIPYGSKE GQEFSAQVME
FIRYHAMLTS IKLAEERGSF PAIKGSLYDP ENMRWTPPKP LFPYKNNYHR PEINWETVVE
GIRKHGIRNA AQTTIAPTGT IATVAGCEGY GCEPVFALAY VRHVNDNGKD LKLNYISPNF
LKELDACNFD AKTRAQILEK ILETGSCQDV DDLPPRIRNV FVVSSDITAE EHVRMQASLQ
AFVDNSLSKT INFPSTATTE DVAQAYMLAW ELGCKGITVY VTGSRDQVVL ETKSTAKSKQ
TESSATSRQL PIWHDPVKPR QRSLKGYTNS IETPLGKTYV TINENGENQP FEVFINTAKA
GTETAAHSEA IGRLISYILR LASPVEPRKR LKAVIEQLSG IGGSRSLGFG ANRILSLPDG
IAKALDSYLY NLDKDIEESN QQDQMRDAPT LPLSNFEPNE EHKPRLKRGL CPECGHASLV
NEEGCRKCYS CGYSEC
//
