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Database: UniProt
Entry: A0A0B3SUN4_9RHOB
LinkDB: A0A0B3SUN4_9RHOB
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ID   A0A0B3SUN4_9RHOB        Unreviewed;      1219 AA.
AC   A0A0B3SUN4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=OA50_01393 {ECO:0000313|EMBL:KHQ54164.1};
OS   Mameliella alba.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Mameliella.
OX   NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ54164.1, ECO:0000313|Proteomes:UP000030960};
RN   [1] {ECO:0000313|EMBL:KHQ54164.1, ECO:0000313|Proteomes:UP000030960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ54164.1,
RC   ECO:0000313|Proteomes:UP000030960};
RA   Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT   "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT   culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL   Submitted (OCT-2014) 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:KHQ54164.1}.
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DR   EMBL; JSUQ01000004; KHQ54164.1; -; Genomic_DNA.
DR   RefSeq; WP_043138987.1; NZ_QAEF01000005.1.
DR   AlphaFoldDB; A0A0B3SUN4; -.
DR   STRING; 561184.SAMN05216376_101442; -.
DR   PATRIC; fig|1515334.3.peg.1395; -.
DR   OrthoDB; 9762933at2; -.
DR   Proteomes; UP000030960; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030960}.
FT   DOMAIN          31..140
FT                   /note="Ribonucleotide reductase class II vitamin B12-
FT                   dependent N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08471"
FT   DOMAIN          191..740
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
FT   DOMAIN          800..904
FT                   /note="Ribonucleotide reductase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02867"
SQ   SEQUENCE   1219 AA;  132705 MW;  202F631901223C74 CRC64;
     MKIERKFTKA GQDAYAEVDF VTTKSEIRNP DGTTVFALDQ LEVPAGWSQV ASDVIAQKYF
     RKAGVPTELK RVAEEGVPEF LWRSVPASKD TPRTGETSAR QVFDRLAGAW TYWGWKGGYF
     TTEEDAQAYF DEMRFMLATQ MAAPNSPQWF NTGLHWAYGI DGPSQGHFYV DYKTGKLVKS
     KSAYEHPQPH ACFIQSVQDD LVNEGGIMDL WVREARLFKY GSGTGTNFSS LRAEGEALSG
     GGKSSGLMGF LKIGDRAAGS IKSGGTTRRA AKMVICDADH PDIEEFINWK VREEQKVASI
     VAGSKMHEKM LNGIFDAIRA WDGAEADAYD PKSNETLKAA IRAAKGAMIP ETYIKRVLDY
     ARQGYASIEF PTYDTDWDSE AYASVSGQNS NNSIRVTDAF LKAVKDDTDW ELIRRTDGKV
     AKTVKARDLW EQVGHAAWAC ADPGIQFHDT VNAWHTCPED GAIRGSNPCS EYMFLDDTAC
     NLASMNLLTF LKDGRFDAES YIHATRLWTL TLEISVLMAQ FPSKEIAQLS YDFRTLGLGY
     ANIGGLLMNM GYGYDSDEGR ALCGALTAIM TGTSYATSAE IAGELGAFPG YARNRDHMLR
     VIKNHRNAAY GASEGYDNLA VKPVPLDLVN CPDEALVHLA MSAWDEAYSL GEKHGYRNAQ
     VSVIAPTGTI GLVMDCDTTG IEPDFALVKF KKLAGGGYFK IINRSVPGAL DNLGYTSSQI
     EEIISYAVGH QTLGNAPGIN HTALVGHGFG PAQIEKVESA LASAFDIRFV FNQWTLGEEF
     CRDVLGIPAE KLVDPSFDLL RHLGFSKADI DAANDHVCGT MTLEGAPHLK EEHLKVFDCA
     NPCGKKGKRF LSVDSHITMM AAAQSFISGA ISKTINMPND ATIEDCQKAY ELSWSLGVKA
     NALYRDGSKL SQPLAAALVE DDDEAAEILE SGSQHEKAQV LAEKIVEKVV IKEVARAGRT
     KMPERRKGYT QKAIVGGHKV YLRTGEYEDG NLGEIFIDMH KEGAGFRAMM NNFAIAVSVG
     LQYGVPLEEF VDAFTFTKFE PAGMVQGNDS IKNATSILDY IFRELAVSYL DRTDLAHVKP
     EGASFDDLGR GEEEGVSNVK ELSETAASRS LEVLKQISST GYLRKRLPQE LIVLQGGQAT
     VALEAGTDPD QVLRSLVPAT AAGPKSGGSA SSAMAMTAVT KAKMQGYEGE ACGECGNYTL
     VRNGTCMKCN TCGATSGCS
//
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