ID A0A1N7G8Y0_9RHOB Unreviewed; 1232 AA.
AC A0A1N7G8Y0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05421666_1787 {ECO:0000313|EMBL:SIS08994.1};
OS Roseovarius nanhaiticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=573024 {ECO:0000313|EMBL:SIS08994.1, ECO:0000313|Proteomes:UP000186019};
RN [1] {ECO:0000313|EMBL:SIS08994.1, ECO:0000313|Proteomes:UP000186019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29590 {ECO:0000313|EMBL:SIS08994.1,
RC ECO:0000313|Proteomes:UP000186019};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTNV01000001; SIS08994.1; -; Genomic_DNA.
DR RefSeq; WP_076532760.1; NZ_FTNV01000001.1.
DR AlphaFoldDB; A0A1N7G8Y0; -.
DR STRING; 573024.SAMN05216208_0349; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000186019; 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:UP000186019}.
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..741
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 796..904
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 1232 AA; 133429 MW; BB9C584C7744D1DE CRC64;
MKIDRKFTKA GQDAYAEMDF TVTSSEIRNP NGSSVFKLDN VEVPAGWSQV ASDVIAQKYF
RKAGVPVRLK KVKEKGVPEF LWRSVPDGEN VETTGETSAK QVFDRLAGAW TYWGWKGGYF
TTEEDAQAYF DEMRVMLAGQ MGAPNSPQWF NTGLHWAYGI DGPGQGHYYV DYKTGKLTKS
SSAYEHPQPH ACFIQSVADD LVGDGGIMDL WVREARLFKY GSGTGTNFSS LRAANEPLSG
GGKSSGLMGF LKIGDRAAGA IKSGGTTRRA AKMVICDADH PDIEEFINWK VKEEQKVASI
VAGSKMHEAK LNDIFAAIRA WDGSLEDSVD PKKNAGLKDA IRGAKKCSIP ETYVKRVLDY
AKQGYESIEF PTYDTDWDSE AYASVSGQNS NNSIRVTDAF LKAVKDDADW ALLNRTDGSV
AKTIKARDLW EDVGHAAWAC ADPGIQYHDT VNAWHTCPED GEIRGSNPCS EYMFLDDTAC
NLASMNLLKF YDDGRFDAEA YMHASRLWTI TLEISVMMAQ FPSKEIAQRS YDFRTLGLGY
ANIGGLLMNM GLGYDSDEGR ALGGALSAIM TGVAYATSAE MAGELGAFAG YQRNAKHMLR
VIRNHRNAAY GKEDGYEGLE VKPVPLDIAG CPDSRLVELA MSTWDEALAL GEQHGYRNAQ
STVIAPTGTI GLVMDCDTTG IEPDFALVKF KKLAGGGYFK IINQSVPAAL EMLGYGSAQI
EEIISYAVGH GTIGNAPGIN HTSLVGHGFG PNELAKVDAA LGSAFDIRFV FNQWTLGAEF
CTNVLGIPEA KLNDPAFDLL AHLGYSKKDI DAANDHVCGT MTLEGAPHLR EEHYSVFDCA
NPCGKKGKRY LSVNSHITMM AAAQSFISGA ISKTINMAND ATIEDCQKAY ELSWSLGVKA
NALYRDGSKL SQPLASALVE DDDEAAEILE SGSNHDKAVT LAEKIVEKIV IKEVNKSHRE
KMPERRKGYT QKAVIGGHKV YLRTGEYADG QLGEIFIDMH KEGAGFRAMM NNFAIAVSVG
LQYGVPLEEF VDAFTFTKFE PSGMVQGNDS IKNATSILDY IFRELAVSYL DRTDLAHVKP
SGHSFDDLGR GEEEGVRNIS EMSEAAASKS LEVLKQISST GYLRKRLPQD LYVLNGGQAR
AASATGAASA DPVSSLQTLV PETAGAAMAT ATVTSQVSSA TMTSGAMSMD ARTKAKMQGY
EGEACGDCGN YTLVRNGTCM KCNTCGATSG CS
//
