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
//