ID A0A2K8NVF8_9MOLU Unreviewed; 826 AA.
AC A0A2K8NVF8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=nrdA {ECO:0000313|EMBL:ATZ17158.1};
GN ORFNames=ELUMI_v1c04340 {ECO:0000313|EMBL:ATZ17158.1};
OS Williamsoniiplasma luminosum.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Williamsoniiplasma.
OX NCBI_TaxID=214888 {ECO:0000313|EMBL:ATZ17158.1, ECO:0000313|Proteomes:UP000232063};
RN [1] {ECO:0000313|EMBL:ATZ17158.1, ECO:0000313|Proteomes:UP000232063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PIMN-1 {ECO:0000313|EMBL:ATZ17158.1,
RC ECO:0000313|Proteomes:UP000232063};
RA Lo W.-S., Gasparich G.E., Kuo C.-H.;
RT "Genome sequence of Entomoplasma luminosum PIMN-1 (ATCC 49195).";
RL Submitted (NOV-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|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; CP024963; ATZ17158.1; -; Genomic_DNA.
DR RefSeq; WP_025734366.1; NZ_CP024963.1.
DR AlphaFoldDB; A0A2K8NVF8; -.
DR KEGG; elj:ELUMI_v1c04340; -.
DR OrthoDB; 9762933at2; -.
DR Proteomes; UP000232063; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
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 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 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:UP000232063}.
FT DOMAIN 180..745
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 826 AA; 92489 MW; 9DA10E5838964328 CRC64;
MYNADQIAEL NLDIKNNFDN IFPIEDGFKL HFEGVSRMVM LDRYSQKDDT LKTLKVGDLV
ITVIKNDPNF PTRGIGQIID IIENDKYLIK IEEQYLGFVS DEFKVDPKIN NLIIKDKGSL
MKPLELYFEQ IARRVAKFLG QEEAEEIQKA FAHELESLNF IPAGRVLYGA GSNKQVTFFN
CYVMPYIHDS REGIAHHREK VAEIMSRGGG VGTNGSTLRP KGAVALSVGG SSSGAVSWLN
DLSQLTHLIE QGGSRRGAQM IMLADWHPDI VEFIISKMQN VKSLLFVKQN FTSEHIQNEV
NKKLKFKNFD ATQRKIYENV LQHSSSFDHK FVTEVTQKLL SGGEYEVVAP EFLSGANISV
AISNKFMDAI DNDQDWALKF PDNLVFTPEQ KSFYESDWEK IGNVFEWEAL GYPTKTFKTI
KARELWKLIN FCATYSAEPG IFFIDKANEM TNARGYDQRV VATNPCGEQP LAPFSVCNLG
AINLANFVDK KTGQILEDKL KKTVSTCVRL QDNIIDLTPY FLEENKKQAL GERRVGMGVM
GLHDMLIWAG VRYGSEAGNK IVDRVFEIIT TSAYRASIAL AKEKGAFPFL DDRQKFVQSG
FIKTLPGDIV DGILEFGIRN SHLITVAPTG STGTMVGGST GLEPYFAFSY FRSGRLGKFM
EVKVPLVEKW LAFHPEYQHQ NLPDIFATAM NLSPIEHANV QCIIQRWVDS SISKTVNAPK
GYLVNDVEKI YMYLYKNGAK GGTVYVDGSR DTQVLSLEKE ENLFSEEFTR SGVGVVVDDE
DFKDENTIRI GNEVGDTCPV CQLGTLIDSG GCVTCNSCNS QVKCGL
//
