ID A9BGY0_PETMO Unreviewed; 840 AA.
AC A9BGY0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=Pmob_1872 {ECO:0000313|EMBL:ABX32561.1};
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Petrotoga.
OX NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX32561.1, ECO:0000313|Proteomes:UP000000789};
RN [1] {ECO:0000313|EMBL:ABX32561.1, ECO:0000313|Proteomes:UP000000789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) 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}.
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DR EMBL; CP000879; ABX32561.1; -; Genomic_DNA.
DR RefSeq; WP_012209658.1; NC_010003.1.
DR AlphaFoldDB; A9BGY0; -.
DR STRING; 403833.Pmob_1872; -.
DR KEGG; pmo:Pmob_1872; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_2_0_0; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000789; 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 InterPro; IPR008926; RNR_R1-su_N.
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.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 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 11..92
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 124..631
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 840 AA; 94547 MW; B124FD218782ADA6 CRC64;
MRVLNKWIQK EPSKNAITIL KDRYFLKDGE GNYLESTWDE VAKRIARHVA AAEVNYTNDI
EEIKNAEEHF YQLIKSRIFL PNSPTIFNAG KTMDRQLFKK DIEETTLEDY KTIFDSRTKH
NMLSACFVIP MDDSMSAIFD AVKNAALIMK YGGGVGYDFS VLRPKGSSIA GTGGKSSGPI
SFMHVFNTAA STIEQGGARR AAQMAVLRYD HPDVFDFINS KKDNKGNNVL NYFNISVNID
NPKEFKKMLE EDGDLTLEHP ASSIRKTIKA NDLMNKMVEN AWKTGDPGML FLGRHNQYYA
MSEHTPVTAT NPCGEEPLPP FGSCNLGSID VAKLVEDMDL GNPNSPDISE FQEIVYWAVR
FLDDVIESNI YPLKEIEEIS KKQRFIGLGM MGLADALYKK ELPYNSEQAR KFMAKLTAEL
AYFSHVASTE LAKERGNFPD FQRSKYPNGF IPFPMLDDEI DEDIKVWNEK IRQHFQGEAT
KYKRNVQTNT IAPTGSISNL ADTSSGIEPN FLLSYVRYMT NKEGDRVPLS YINPILMEKI
GTNMTEELKA EIIEKGSIQN IDSIPNEIKK IFVTSMDIPP KDHLLAQHVI QSYLDASCSK
TINMPKSSTI EDVKAIYLQA LELNLKGLTI YRDGSLETQV LTSSSQEEKE TSETQGKSVT
FFVLDEKHKL RARPRKETLR SVTRKFKHDT GTVYVTVSFD DAGEAVEIFL SDGTETAEVI
GRLSSIALRA GVSTDEIVEQ LKKVKGTYCK GLAQEISKAL NDFNQLWGSK IEDYEVIRTG
TPKTREEVEK FVYANDLKYD KGYYIDSEGN AYCPSCLSKN TLVNESGCVT CTTCGWSKCS
//
