ID A0A1E5ADD5_9RHOB Unreviewed; 1214 AA.
AC A0A1E5ADD5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=AB838_13460 {ECO:0000313|EMBL:OED48004.1};
OS Rhodobacteraceae bacterium (ex Bugula neritina AB1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1868286 {ECO:0000313|EMBL:OED48004.1, ECO:0000313|Proteomes:UP000094333};
RN [1] {ECO:0000313|EMBL:OED48004.1, ECO:0000313|Proteomes:UP000094333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB1-7 {ECO:0000313|EMBL:OED48004.1};
RX PubMed=27681823; DOI=10.1038/srep34362;
RA Miller I.J., Weyna T.R., Vanee N., Fong S., Lim-Fong G.E.;
RT "Single sample resolution of rare microbial dark matter in a marine
RT invertebrate metagenome.";
RL Sci. Rep. 6:34362-34362(2016).
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:OED48004.1}.
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DR EMBL; MDLF01000074; OED48004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5ADD5; -.
DR STRING; 1868286.AB838_13460; -.
DR Proteomes; UP000094333; 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 PRINTS; PR01183; RIBORDTASEM1.
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}.
FT DOMAIN 31..139
FT /note="Ribonucleotide reductase class II vitamin B12-
FT dependent N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08471"
FT DOMAIN 190..741
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 794..903
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1214 AA; 132008 MW; 1CD0AE45114EAAB9 CRC64;
MKIERKFTKP GQDAYADLAF VSATSEIRNP DGTIVFRLDN IEIPASWSQV ASDVIAQKYF
RKAGVPSRLK KVREKGVPDF LWRSVPDKGA ELGGETSSKQ VFDRLAGAWA YWGWKGGYFS
SEEDARAYYD EMRFMLATQR SAPNSPQWFN TGLHWAYGID GPAQGHHYVD YKTGVLTKSD
SAYEHPQPHA CFIQSVSDDL VKDGGIMDLW VREARLFKYG SGTGTNFSHL RAEGEPLSGG
GKSSGLMGFL KIGDRAAGAI KSGGTTRRAA KMVIVDADHP DIEQFIEWKV IEEQKVASIV
AGSKMHEKML NGIFEAIRSW DGAEAVAYDP SVNEGLKKAV REAKKVAIPE TYIKRVLDYA
KQGHTSIEFP TYDTDWDSEA YSSVSGQNSN NSIRVTNSFL HAVEKDADWE LINRTDGKVA
KVVKARDLWE KVGHAAWACA DPGIQFHDTV NDWHTCPEDG EIRGSNPCSE YMFLDDTACN
LASLNLLSFL KDGQFQADEY MHSCRLWTLT LEISVMMAQF PSQEIAQRSY DFRTLGLGYA
NIGGLLMNMG YGYDSDEGRA LCGALTALMT GVAYATSAEI AAELGAFPGY AKNADHMLRV
IRNHRNAAKG EAEGYEALAV KPVPLDIANC PDALLTDLAA SAWDEALELG EKHGYRNAQT
TVIAPTGTIG LVMDCDTTGI EPDFALVKFK KLAGGGYFKI INRSVPSALE GLGYSSSQIE
EIVSYAVGHG SIGNAPGINH TSLAGHGFGP NELAKVDAAL EAAFDIRFVF NQWTLGEDFC
TGVLGIPATK LNDPTFDLLR HLGFTKKDIE AANDHVCGTM TLEGAPHLQK EHYAIFDCAN
PCGKKGKRFL SVGSHITMMA AAQSFISGAI SKTINMPNDA TIEDCQKAYE LSWSLGVKAN
ALYRDGSKLS QPLAAALVED DDEAAEVLES GSNQEKAVVL AEKIVEKVVI KEVIKSHRTK
MPQRRKGYTQ KAVVGGHKVY LRTGEYEDGN LGEIFIDMHK EGAGFRAMMN NFAIAVSVGL
QYGVPLEEFV DAFTFTKFEP AGMVQGNDSI KSATSILDYV FRELAVSYLD RTDLAHVKPE
GATFDDLGRG EEEGVSNLTE LSETAATRSL EVLKQISSTG YLRKRLPQDL VVLQGGQTDA
GVLGTGTDPV AALQTLVPET SEALAQSTGG MDARTKAKMQ GYEGEACGEC GNYTLVRNGT
CMKCNTCGGT SGCS
//
