ID A0A193LIB6_9GAMM Unreviewed; 715 AA.
AC A0A193LIB6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-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=BA177_14470 {ECO:0000313|EMBL:ANO52236.1};
OS Woeseia oceani.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Woeseiaceae;
OC Woeseia.
OX NCBI_TaxID=1548547 {ECO:0000313|EMBL:ANO52236.1, ECO:0000313|Proteomes:UP000092695};
RN [1] {ECO:0000313|EMBL:ANO52236.1, ECO:0000313|Proteomes:UP000092695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XK5 {ECO:0000313|EMBL:ANO52236.1,
RC ECO:0000313|Proteomes:UP000092695};
RA Mu D., Du Z.;
RT "Complete genome sequence of a deep-branching marine Gamma Proteobacterium
RT Woeseia oceani type strain XK5.";
RL Submitted (JUN-2016) 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; CP016268; ANO52236.1; -; Genomic_DNA.
DR RefSeq; WP_068617363.1; NZ_CP016268.1.
DR AlphaFoldDB; A0A193LIB6; -.
DR STRING; 1548547.BA177_14470; -.
DR KEGG; woc:BA177_14470; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000092695; Chromosome.
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:UP000092695}.
FT DOMAIN 16..91
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 102..650
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 715 AA; 80124 MW; F0DE19D15AA25D06 CRC64;
MKSAVNLNAE TVADIEFQPA SLDIWQAKYR LSAKDGAPID QTIDDTYIRV ARALADVEAE
PLREEWFEKF LWALRSGAIP AGRITSNAGA KEHKPATSTI NCTVSGTVAD SMDNILNKVH
EAGLTLKAGC GIGYEFSTLR PKGAYVSGAG AYTSGPLSFM DIYDKMCFTV SSAGGRRGAQ
MGTFDVGHPD VMDFILAKRE DGRLRQFNLS LLITDEFMQA VKADTEWKLA FPVTRKEMDQ
DGLDVNDASQ FVWREWPEPQ NYVRNADGLV ACKIYRTMPA RRVWDVIMAS TYDFAEPGFV
LIDRVNEMNN NWFTETIRAT NPCGEQPLPP YGSCLLGSVN LTKFVLDPFT EKARFDWTEF
RKVVKVFTRM LDNVVEINGL PLARQRDEIT RKRRHGMGFL GLGSTITMLR MKYGEENSVS
FTEEVSKQLA IAGWETALEL AREKGPAPIM NEEFTVTQEM LSKRPEMVAD GLKVGDKVPG
RVLHARYSRY MQRIAKESPE LVEQLAETGA RFTHHSSIAP TGTISLSLAN NASNGIEPSF
AHHYFRNVIR QGKKTKEKVD VLSFELLSYR ALINEKAAPN SEDSEAALPD YFVTAEDITP
KAHVDIQAAA QSWIDSSISK TANVPTDYPY EDFKDIYMYA YEQGLKGCTT FRFNPEAFQG
VLVKERDLKN TVYTFTLEDG KEVELQGDEE IEYDGEVHTA ANLFDALKEG YYGKF
//
