ID A0A011QP85_9PROT Unreviewed; 961 AA.
AC A0A011QP85;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN Name=nrdZ {ECO:0000313|EMBL:EXI80694.1};
GN ORFNames=AW12_02827 {ECO:0000313|EMBL:EXI80694.1};
OS Candidatus Accumulibacter sp. BA-94.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=1454005 {ECO:0000313|EMBL:EXI80694.1, ECO:0000313|Proteomes:UP000020878};
RN [1] {ECO:0000313|EMBL:EXI80694.1, ECO:0000313|Proteomes:UP000020878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-94 {ECO:0000313|Proteomes:UP000020878};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:EXI80694.1}.
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DR EMBL; JEMZ01000199; EXI80694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011QP85; -.
DR STRING; 1454005.AW12_02827; -.
DR PATRIC; fig|1454005.3.peg.2756; -.
DR Proteomes; UP000020878; 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:UP000020878}.
FT DOMAIN 27..93
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 99..591
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 961 AA; 106326 MW; E05EF49B5CA85B49 CRC64;
MSQLTYQLPL SEIAEAPAIA PLAEQEISGE VLVEKYAKGS ETSVHDVRRR VACALAANEE
EKQRAHWEAR FLWAQENGFV PAGRINSAAG TTLAATLINC FVQPIGDSVV EIVDGKPGIY
SALAEAAETM RRGGGVGYDF SSIRPIGALV KGTQSRASGP VSYMRVFDRS CETVESAGAR
RGAQMGVLRC DHPDIEVFIH AKDHGDLSNF NVSIAVTDSF MQAVEADSEV ELTHRAEPSP
DMKRAGAFQR DDGIWVYRRV RARDLWDQVM KSTYDHAEPG ILFLDRMNKD NNLYYCEVIE
ATNPCAEQPL PPYGCCCLGS INLTLFVRSP FTIDAEFDFE AFAEVVKLST RMLDNVLDVT
AWPLERQREE AASKRRVGLG FTGLGDTLCM LRLRYDRPEA MAMGARISEF MRDTAYLASV
ELAQERGAFP LFNAELYLSG GNFASRLPAD IKSEIRKHGL RNSHLLSIAP TGTISLAFAD
NASNGIEPPF SWTYTRKKRM ADGTLKEYAV EDYAWRLYKH LGGDVEKLPD YFVTALEISA
RAHKDMVAAV APYIDTSISK TVNVPADYPY EEFQDLYFTA WKSGLKGLAT YRPNAVLGSV
LSVESQKQAE DRKQPQDFEI GDANRRLTIK TLPAPVLASL RWPNRPNMLE GNMAWTYMIE
HTHGKFALFV GQIEQDGRHW PFEAWVNGPE QPRGLGAVAK TLSMDMRAND HGWLALKLES
LARTAGDEGF EMPFPPHGER KRMPSVVAAM AQLIQFRVDR LDSFRHEGPT PVLDAMFSRK
EPKTGTDGTL SWTVDVFNPA TGEDFVLGLK EITLPDGVTR PYSVWLSGNY PRALDGLTKL
LSFDMRVIDP AWIGMKLRKL LDYPEPLGDF MAFIPGTRRQ TNYPSTVAYL AQLIIHRYAM
LGILDENGLP LQQMGILQTP VGGSAAPATA GKLCGECGNM TMIRKDGCDF CTACGAVGSC
G
//
