ID A0A1I0VFE3_9RHOB Unreviewed; 1212 AA.
AC A0A1I0VFE3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05421688_0567 {ECO:0000313|EMBL:SFA74767.1};
OS Poseidonocella pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Poseidonocella.
OX NCBI_TaxID=871651 {ECO:0000313|EMBL:SFA74767.1, ECO:0000313|Proteomes:UP000198796};
RN [1] {ECO:0000313|EMBL:SFA74767.1, ECO:0000313|Proteomes:UP000198796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29316 {ECO:0000313|EMBL:SFA74767.1,
RC ECO:0000313|Proteomes:UP000198796};
RA de Groot N.N.;
RL Submitted (OCT-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|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}.
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DR EMBL; FOJU01000001; SFA74767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VFE3; -.
DR STRING; 871651.SAMN05421688_0567; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000198796; 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:UP000198796}.
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 798..904
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1212 AA; 131638 MW; A732C9AC5BD5896A CRC64;
MKIERKFTKA GNDAYADLEF VTTTSEIRNP DGTVVFRLDE VEVPASWSQV ASDVIAQKYF
RKAGVPVKLK RVREAGVPEF LWRSVPASKT TATTGETSSK QVFDRLAGAW AYWGWKGGYF
SSEEDARAYY DEMRVMLATQ TAAPNSPQWF NTGLHWAYGI DGPGQGHYYV DYKTGELTRS
TSAYEHPQPH ACFIQSVKDD LVGDGGIMDL WVREARLFKY GSGTGTNFSS LRAEGESLSG
GGKSSGLMGF LKIGDRAAGA IKSGGTTRRA AKMVIVDADH PDIEEYINWK VKEEQKVASI
VAGSKMHEAK LNEIFGAIRA WDGATEDAVD PTKNVQLKDA IRGAKQVAIP ETYVKRVLDY
ARQGYASIEF PTYDTDWDSE AYASVSGQNS NNSVRVTDAF LEAVQADSDW ELIRRTDGSV
AKTIKARDLW EQIGHAAWAC ADPGIQYHDT VNAWHTCPED GAIRGSNPCS EYMFLDDTAC
NLASMNLLTF YKDGKFQVEE YVHAARLWTL TLEISVLMAQ FPSKEIAQRS YDFRTLGLGY
ANIGGLLMSM GLGYDSDEGR ALCGALTAVM TGVAYATSAE IAGELGPFPG YARNADHMLR
VIRNHRTAAY GRTDGYEGLA IKPVALDHEN CPDASLLDVA TSCWDEALKL GERNGFRNAQ
ATVIAPTGTI GLVMDCDTTG IEPDFALVKF KKLAGGGYFK IINQSVPAAL EKLGYSTSQS
EEIVAYAVGH GTLGNAPGIN HTALVGHGFG QGEIERIEAA LGSAFDIRFV FNQWTLGEDF
CTEVLGIPAE KLADPTFDML RHLGFSKREI DAANDHVCGT MTLEGAPHLD PAHYHVFDCA
NPCGKVGKRY LGVNAHIDMM AGAQSFISGA ISKTINMAND ATIEDCQAAY ERSWRKGIKA
NALYRDGSKL SQPLAASLVE DDDDAAEILE RGSAQEKAAV LAEKIVEKVI VKEIVRSHRE
KMPERRKGYT QKAIVGGHKV YLRTGEYSDG SLGEIFIDMH KEGAGFRAMM NNFAIAVSVG
LQYGVPLEEF VDAFTFTKFE PAGMVQGNDS IKNATSILDY IFRELAVSYL DRTDLAHVKP
EGASFDAIGL GEAEGKRPAT ETDAAANRSL AVLKQISSTG YLRKRLPQDL VVLQGGATGP
RAEMLRTGTE DAAVTVASEV HTTTTTSVAS AVTRAKMQGY EGEACGDCGN YTLVRNGTCM
KCNTCGSTSG CS
//
