ID D5BG33_ZUNPS Unreviewed; 850 AA.
AC D5BG33;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=ZPR_2826 {ECO:0000313|EMBL:ADF53146.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF53146.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF53146.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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|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; CP001650; ADF53146.1; -; Genomic_DNA.
DR RefSeq; WP_013072243.1; NC_014041.1.
DR AlphaFoldDB; D5BG33; -.
DR STRING; 655815.ZPR_2826; -.
DR KEGG; zpr:ZPR_2826; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_2_10; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000001654; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd02888; RNR_II_dimer; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013344; RNR_NrdJ/NrdZ.
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; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 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 Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
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 29..94
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 111..643
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 850 AA; 95984 MW; 97F74DCD4E0196CC CRC64;
MPVQTTPKAS KTYTQDEAFK ASLAYFKGDD LAARVWVNKY ALKDSDGNIY EQTPNDMHRR
IAKEIARVEQ RYPNPMTEDE VFDLIKDFKY IVPQGSPMAG IGNPYQIASL SNCFVIGNEG
SSDSYGGVMK IDQEQVQLMK RRGGVGHDLS HIRPKGSPVK NSALTSTGIV PFMERYSNST
REVAQDGRRG ALMLSVSINH PDSEDFIDAK MEQGKVTGAN VSVRIDDDFM KAVKNKTAYT
QKYPVFSDAP KFSKEIEAEK LWKKIVHNAW KSAEPGILFW DTVINESVPD CYADLGYKTV
STNPCGEIPL CPYDSCRLLA INLFSYVEDP FTTKAKFNYT LFKKHISAAQ RIMDDIIDLE
LEKIDAILQK IDADPENEDV KGVERNLWLN IKKKAEEGRR TGIGITAEGD MLAGLGIKYG
SEEGVAFSTE IHKNIALAAY RASVETAKER GAFGIFDSDR EKENPFILRL KEADEKLYYD
MLEYGRRNIA LLTIAPTGTT SLMTQTTSGI EPVFLPVYKR RRKVNPNDKD VRVDFVDEVG
DSWEEYVVFH HRFKEWMKIN GHDIDKNYSN TDLDELVKAS PYYQATSNDV DWLSKVRMQG
AVQKWVDHSI SVTINLPNDV SEDLVGRLYL EAWQAGCKGV TVYRDGSRSG VLISNDEKKE
EEKEGNGIFP TKRPQVLEAD VVRFQNSKDK WIAFIGLIDG RPYEIFTGFS DDEDGILIPR
WVNEGLIIKN RNEDGTSRYD FQYKNKRGYK TTIEGLSHKF NPEFWNYAKL ISSTLRHGMP
IDNVVNLVNS LQLDSESINT WKNGVARALK RFIADGTVAK KEKCTNCNSS NLIYQEGCLT
CKDCGSSKCG
//
