ID A0A0G1LHK9_9BACT Unreviewed; 782 AA.
AC A0A0G1LHK9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, 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};
DE Flags: Fragment;
GN ORFNames=UW62_C0001G0001 {ECO:0000313|EMBL:KKT68237.1};
OS Candidatus Collierbacteria bacterium GW2011_GWB1_44_35.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1618383 {ECO:0000313|EMBL:KKT68237.1, ECO:0000313|Proteomes:UP000034604};
RN [1] {ECO:0000313|EMBL:KKT68237.1, ECO:0000313|Proteomes:UP000034604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT68237.1}.
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DR EMBL; LCJA01000001; KKT68237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1LHK9; -.
DR PATRIC; fig|1618383.3.peg.1; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000034604; 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 InterPro; IPR008926; RNR_R1-su_N.
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}.
FT DOMAIN 49..129
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 133..605
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 782
FT /evidence="ECO:0000313|EMBL:KKT68237.1"
SQ SEQUENCE 782 AA; 86053 MW; 419E894B48C755FD CRC64;
MVVSQSIYKS MSTKRESEEE NYEQVMKGIN SKLGSMPKMP DDLPTGDWSE QAVKVLKERY
LDKDGDGVLT ETPDELVWRV AWAIAAAEVR WGADKEQVME MAKRFYSLLG SRKFLPNSPT
LMNAGKENGL QYSGCFVLPV EDSIDGIFES LKNQAIIHQS GGGTGFSFSR LRQKGSMVRK
SRGVASGPVS FMKVYNEATQ QIKQGGTRRG ANMGILRVDH PDVREFITCK IDGGITNFNI
SVAATDKFMK AVVDDTDYDI IEPHTGRVIR QENAREIFDL ICECAWKSGD PGMVFIDKIN
DGPANPVPSM GPVESTNPCG EQPLYPYDSC NLGSIFLNYF VKESGGKQEI DWEGLKETVR
LSVRFLDDVI EVNPYPLKQI WDTVRSIRRI GLGIGGWADM LYLLGIAYNS EEALVLARKV
MKTINDTAHE ESEFLAEERG AFPLWKESIF KDGKKIRNSA ITTIAPTGTI GIIANTSGGC
EPVFALAYKH MVKDESLNRE MFFVDPAFKE VAVREGFWSD DLGSAVAESG NVHGLSLVPE
KWQKILVTSH EITPEWHVKM QSAWQEFTDN AVSKTINLPN EATVDDVARS YLMSYELGCK
GITIYRDGSK SIQVLNVGTK ETNIKDTEVD EVMTTEEVVE TMADLRIRPI KLQGNTYRVH
TPVGAAFVVI NADEMGNPFE VFINVGKAGT HVMADAEAMG RLISLALRVP SKFPPKALAE
AVIDQLSGIG GAESVGFGGN RVRSLADGVA KVLKDYLKGN GGGLEAAHEE EVVGSVGQQQ
AL
//
