ID U2FI04_9BURK Unreviewed; 946 AA.
AC U2FI04;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=L810_0447 {ECO:0000313|EMBL:ERJ36511.1};
OS Burkholderia sp. AU4i.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1335308 {ECO:0000313|EMBL:ERJ36511.1, ECO:0000313|Proteomes:UP000016616};
RN [1] {ECO:0000313|EMBL:ERJ36511.1, ECO:0000313|Proteomes:UP000016616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU4i {ECO:0000313|EMBL:ERJ36511.1,
RC ECO:0000313|Proteomes:UP000016616};
RA Devi U., Khatri I., Kumar N., Kumar L., Singh D., Sharma D.,
RA Subramanian S., Saini A.K.;
RT "Genome Assembly of Burkholderia vietnamiensis AU4i.";
RL Submitted (MAY-2013) 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|RuleBase:RU364064};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase class-2
CC family. {ECO:0000256|RuleBase:RU364064}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406}.
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:ERJ36511.1}.
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DR EMBL; ASSI01000107; ERJ36511.1; -; Genomic_DNA.
DR RefSeq; WP_021161023.1; NZ_ASSI01000107.1.
DR AlphaFoldDB; U2FI04; -.
DR PATRIC; fig|1335308.3.peg.5152; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000016616; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR005144; ATP-cone_dom.
DR InterPro; IPR013346; NrdE_NrdA_C.
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 InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR02504; NrdJ_Z; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF03477; ATP-cone; 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.
DR PROSITE; PS51161; ATP_CONE; 2.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00492}; Cobalamin {ECO:0000256|RuleBase:RU364064};
KW Cobalt {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, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364064}.
FT DOMAIN 10..115
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 128..218
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 946 AA; 105341 MW; 01466D1F8E79621B CRC64;
MKREDLIGAH MVIRRNGETV PFDRAKIANA IAKAFLYDAH GNLYRAGVSS LSAAQRVKVE
ELTNAVCAAL NRRGESAAFR IEDIQDQVEL SLMRSGEHEV ARGYVLYREM AAQKRTPAPT
LGQYDHIKSY RQRDGAVVPF DAAFWIAIVE SVVFGLESVS AKDLFDEAVR NLYNEAKETE
IENALVLSAR TKIEVEPQHA KAAARLVLAF QLGHDVFGKP VTLDEVAAGY GEAFIRGIED
GVKAELLTED MSKGFDLGRL ASAIRPERDG LLDYLGMQTL YDRYLLHVNE RRIELPQAFL
MRVAMGLARG EIERETRAIE FYEVLSTFDY MSSTPTLFNT GSRRSQLSSC YLTTISDDLE
GIYDGLKENA LLSKFAGGLG NDWTNVRAMG AWIKGTNGKS QGVVPFLKVV NDTAVAVNQG
GKRKGAVCAY LESWHLDIEE FLDLRKNTGD DRRRTHDMNT ANWIPDLFMK RVMEGSDWTL
FSPNDVPDLH DLYGAKFEER YVQYEAQADA GVIKLYKRRP AVELWRKMLG MLFETGHPWI
TFKDPCNIRS PQQHVGVVHS SNLCTEITLN TSDVEIAVCN LGSVNLVNHV KDGQIDHEKL
RRTVRIAMRM LDNVIDMNYY AVAKARSANL KHRPVGLGLM GYQDALYILG IPFGSEAAVE
FSDRSMEALA YYAYEASSDL AAERGAYSSF KGSLWSKGVL PFDSLKLLAE ARGEQYLEVD
QSITMDWDGL REKILKQGMR NSNCIAIAPT ATISNIVGVS ACIEPQFQNL YVKSNLSGEF
TLVNEYLIAE LKKLGIWDEL MLADLKYYEG SVQRIDRIPE EIKARYATAF EIDPKWLVEG
AARRQKWIDQ AQSLNIYIAG ASGKKLDEVY KLAWVRGLKT TYYLRTMAAT SVEKSTVASG
TLNAVTPSAP AAVAPQVAAA PALEADGPVC TMRPGDPGFD ECEACQ
//
