ID F8X151_9BACT Unreviewed; 847 AA.
AC F8X151;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=HMPREF9456_01960 {ECO:0000313|EMBL:EGK03323.1};
OS Dysgonomonas mossii DSM 22836.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=742767 {ECO:0000313|EMBL:EGK03323.1, ECO:0000313|Proteomes:UP000006420};
RN [1] {ECO:0000313|EMBL:EGK03323.1, ECO:0000313|Proteomes:UP000006420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22836 {ECO:0000313|EMBL:EGK03323.1,
RC ECO:0000313|Proteomes:UP000006420};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Dysgonomonas mossii DSM 22836.";
RL Submitted (APR-2011) 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|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:EGK03323.1}.
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DR EMBL; ADLW01000007; EGK03323.1; -; Genomic_DNA.
DR RefSeq; WP_006843330.1; NZ_GL892006.1.
DR AlphaFoldDB; F8X151; -.
DR STRING; 742767.HMPREF9456_01960; -.
DR GeneID; 78082602; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_2_10; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000006420; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006420}.
FT DOMAIN 22..86
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 104..636
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 847 AA; 96173 MW; D93FA78F86622D6F CRC64;
MAQKVYTFDE AYRAALDYFN GDELAAKVWV NKYALKDATG NIYEQSPEDM HWRLANEIGR
IESKYKNGLT TQELYDLFDQ FKYIVPQGSP MTGIGNDYQI ASLSNCFVIG MEGSSDSYGA
IIRVDEEQVQ LMKRRGGVGH DLSHIRPKGS PVKNSALTST GLVPFMERYS NSTREVAQDG
RRGALMLSVS IKHPDSESFI DAKMIEGKVT GANVSVRIDD AFMQAVVDGT PYTQQYPIDS
DNPTTVKDTD ATELWKKIVH NAWKSAEPGV LFWDTIIRES VPDCYADLGF KTISTNPCGE
IPLCPYDSCR LLAINLYSYV VNPFKEDAYF DFELFKKHVG LAQRIMDDII DLETEKIDKI
LNKIEIDPEN EEVKWPERHL WEKIRKKTLQ GRRTGVGITA EGDMIAAMGL RYGTEEATTF
AEEVHRTLAV AAYRASVELA KERGAFEIFD IERERNNPFI NRLAEVDPKL YKDMEKYGRR
NIACLTVAPT GTTSLMTQST SGIEPVFLPV YKRRRKVNPN DKEVRVDFVD ENGDSWEEYV
VFHHKFVTWM ESKGYPAAKR YTNEEIDKMI AESPYYKATS NDVDWLQKVK MQGRIQKWVD
HSISVTINLP SDVSEDLVNQ LYIEAWKSGC KGCTVYRDGS RAGVLIANDS KKEEEDCGDC
YERPQIVMER PRELAADVIK FQNNKEKWIA FIGLLDGRPY EIFTGLSDDD EGLVLPKNIN
QGVIIKTMND EGQRSYDFQF KNKRGYKTTI EGLNGKFNPE FWNYAKLISG VLRYGMPIDQ
VVKLVQGLEL NSETINTWKN GVERALKKYL PNETEAKGQK CPVCGLETLV YQEGCMKCTN
CGASKCG
//
