ID A0A0J9E2G9_9RHOB Unreviewed; 1221 AA.
AC A0A0J9E2G9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|ARBA:ARBA00014409, ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU364064};
GN ORFNames=AIOL_002014 {ECO:0000313|EMBL:KMW57056.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW57056.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW57056.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW57056.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) 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|ARBA:ARBA00025437, 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:KMW57056.1}.
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DR EMBL; LFTY01000002; KMW57056.1; -; Genomic_DNA.
DR RefSeq; WP_049642845.1; NZ_LFTY01000002.1.
DR AlphaFoldDB; A0A0J9E2G9; -.
DR STRING; 1675527.AIOL_002014; -.
DR PATRIC; fig|1675527.3.peg.2119; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000037178; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
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; -; 3.
DR InterPro; IPR013678; RNR_2_N.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
DR InterPro; IPR029072; YebC-like.
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; PF08471; Ribonuc_red_2_N; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF75625; YebC-like; 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:UP000037178}.
FT DOMAIN 31..138
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 189..738
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 814..902
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1221 AA; 132125 MW; 011DFE728C7291A3 CRC64;
MKIARKFTKA GQDAYADVEF TMTSSEIKNP DGTVVFKNDE VEVPASWSQV ASDVIAQKYF
RKAGVPAKLK KVKEKGVPEF LWRSVPAGKE MGGEQSARQV FDRLAGAWAY WGWKGGYFTT
EADAHAYFDE MRYMLATQRA APNSPQWFNT GLHWAYGIDG PAQGHFYVDY QSGELTKSTS
SYEHPQPHAC FIQGCSDDLV NDGGIMDLWV REARLFKYGS GTGTNFSHLR GEGESLSGGG
KSSGLMGFLK IGDRAAGAIK SGGTTRRAAK MVIVDADHPD IEEYINWKVK EEQKVASLVA
GSKMHEQKLN EIFAAIGQWD GAVEDAVDPA KNAALKAAVR DAKKASIPET YVKRVLDYAK
QGYSSIEFPT YDTDWDSEAY SSVSGQNSNN SVRVTDAFLK AVAEDADWEL IRRTDGKVAK
TIKARDLWEQ IGHAAWACAD PGIQYHDTVN AWHTCPEDGP IRGSNPCSEY MFLDDTACNL
ASMNLLTFFE DGKFQADDYV HATRLWTVTL EVSVMMAQFP SKEIAQLSYD FRTLGLGYAN
IGGLLMNMGL GYDSDEGRAL CGALTAIMTG VSYATSAEMA GELGPFPSYK RNEAHMLRVI
RNHRRAAYGE LDGYDGLSIK PVALDGDNCP DQDLVALARA AWDEALDLGE AHGYRNAQST
VIAPTGTIGL VMDCDTTGIE PDFALVKFKK LAGGGYFKII NRSVPAALET LGYSTSQIEE
IVAHAVGHGT LGNAPGINHT SLIGHGFGPA ELAKIEAALP SAFDIRFVFN QWTLGAEFLT
GPLGIPQEKL SDPTFDLLSH LGFSRADIDA ANDHVCGTMT LEGAPFMKDE HLSVFDCANT
CGKKGKRFLS VNSHIDMMAA AQSFISGAIS KTINMPNNAT IEEVQEAYER SWAKGVKANA
LYRDGSKLSQ PLASALVEDD DEAAEILESG STHEKAAVLA EKIVEKVIVK EIAAAREKMP
DRRRGYTQKA VVGGHKVYLR TGEYSDGSLG EIFIDMHKEG AGFRAMMNNF AIAVSVGLQY
GVPLEEFVDA FTFTKFEPAG MVQGNETIKN ATSILDYIFR ELAVSYLDRT DLAHVKPEGV
SFDDLGRGDE EGKRNFTEVP DSRGMDQVEV LKKVVSSGYL RNRAPQELVV LNGGAGQGAV
ALSGAADPVA TLQALAPETT ASTVAAAVAP PTTGAVQMDA RAKAKMQGYE GEACGDCGNY
TLVRNGTCMK CNTCGATSGC S
//
