ID F8GLT5_NITSI Unreviewed; 954 AA.
AC F8GLT5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=Nit79A3_2121 {ECO:0000313|EMBL:AEJ01909.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01909.1};
RN [1] {ECO:0000313|EMBL:AEJ01909.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01909.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-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|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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002876; AEJ01909.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GLT5; -.
DR STRING; 261292.Nit79A3_2121; -.
DR KEGG; nii:Nit79A3_2121; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
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 32..132
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 148..237
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 954 AA; 106648 MW; FCFD7D70F9BBFF7D CRC64;
MQLTTEHTNL KPVSGSQSFA DSSNQNSRFS QYRVIRRNGA VVAFEPGKIT VAMTKAFIAV
DGGQGAASVR VREVVAGLTN DVVGALLRRQ PDSGTFHIED IQDQVELALM RSGEHDVARA
YVLYREDRAR ERAKLKQKSA AEVAAETLYV VDNGQRVPLD MARLSALIES SCSGLGNTVD
ASLILKATIK DLYDGVPLDE VRKSVILSAR VLIEKDPAYS YVTARLLLNN MRYEVLGEEV
SQQMMQAQYK DYFPAFIKRG IEADLLDERL AQFDLTRLAE VLDAARDLQF DYLGLQTLYD
RYFLHIKENR IELPQAFFMR VAMGLALNEI DREARAIEFY HVLSSFDFMS STPTLFNSGT
CRSQLSSCYL TTVPDDLDGI YEAIKENALL AKYAGGLGND WTAVRAMGAR IKGTNGKSQG
VVPFLKVVSD TAVAVNQGGK RKGAVCAYLE CWHLDIEEFL ELRKNTGDDR RRTHDMNTAT
WIPDLFMKRV MDGSDWTLFS PSDVPDLHEK FGQQFEQAYL AYEAKIERGE LELYKKIPAV
QLWRKMLSML FETGHPWITF KDPCNIRSPQ NHIGVVHSSN LCTEITLNTN DKEIAVCNLG
SVNLVAHLKD GALDLDKLKR TVSIAMRMLD NVIDINFYAV AKARNANLKH RPVGLGIMGF
QDCLHQLGIP YSSDAAVEFA DRSMEAVAYQ AYWASTELAE ERGCYSSYKG SLWDRGILPH
DTLEILRKER GGFVEADLST TLDWDALRQR IKNHGMRNSN CLAIAPTATI SNIIGVSASI
EPTYQNLYVK SNLSGEFTIT NRSLVDDLKK LNLWDEVMIA DLKYFDGAIS KIDRIPESIR
TLYATAFEME PCWLIEAGAR RQKWIDQSQS LNIYMAGVSG KKLDDTYKLA WLRGLKTTYY
LRSMGATAAE KSTVRAGSLN AVPADGGMAK VAMEVSAVEI KYCAIDDESC ESCQ
//
