ID A0A1I2Y217_9PROT Unreviewed; 953 AA.
AC A0A1I2Y217;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN ORFNames=SAMN05216299_102163 {ECO:0000313|EMBL:SFH19780.1};
OS Nitrosospira sp. Nsp14.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=1855333 {ECO:0000313|EMBL:SFH19780.1, ECO:0000313|Proteomes:UP000198772};
RN [1] {ECO:0000313|EMBL:SFH19780.1, ECO:0000313|Proteomes:UP000198772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nsp14 {ECO:0000313|EMBL:SFH19780.1,
RC ECO:0000313|Proteomes:UP000198772};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOPV01000002; SFH19780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2Y217; -.
DR STRING; 1855333.SAMN05216299_102163; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000198772; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000198772}.
FT DOMAIN 32..132
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 147..236
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 953 AA; 106703 MW; 8353DE93E5C5E2C5 CRC64;
MQLATDHTAR PAITGYEVSS PLSGQDARYS QYKIIRRNGS VAAFEPSKIS IAMTKAFIAV
NGGQGAASAR VREVVARLTD DVVNALIRRQ PSGGTFHIED IQDQVELALM RSGEHDVARA
YVLYREDRAR KRAQHKEIAA AEAAHVLNVL EDGRKTQLDT SRLLTLIESC CEGLGDVVNG
PVILKATLKD LYDGVPMDEV RRSLVLSARA LIEKEPAYSY VTARLLLHNL RLEVLGEEAL
QQEMTDRYAE YFPQFIKRGI EAELLDERLA QFDLPRLAKA LDSSRDLKFG YLGLQNLYDR
YFLHVREHRI ELPQTFFMRV AMGLALNEID REGRAIEFYH VLSSFDFMSS TPTLFNSGTR
RSQLSSCYLT TVPDNLDGIY ESIKENALLA KYAGGLGNDW TPVRAMGARI KGTNGKSQGI
VPFLKVVSDT AVAVNQGGKR KGAVCAYLES WHLDIEEFLD LRKNTGDDRR RTHDMDTATW
VPDLFMKRVM EGGEWTLFSP SDVPDLHDKY GKEFEKAYLA YEEKAASGEL ILHKKIPAQQ
LWRKMLSMLF ETGHPWITFK DACNVRSPQN HVGVVHSSNL CTEITLNTNE HEIAVCNLGS
VNLAAHINDA GELDAGKLKR TVRTAMRMLD NVIDINFYAV PKARNSNLKH RPVGLGIMGF
QDCLHMMRIP YASNEAVEFA DHAMEAVAYH AYWASTELAE ERGRYASYRG SLWDRGILPQ
DSLDLLLEER GGYVEVDRTS TLDWEPLRER IRQYGMRNSN CLAIAPTATI SNIVGVSASI
EPSFTNLYVK ANLSGDFTTV HKYLVYDLKK LGLWDEVMLS DLKYFDGSLS RIDRVPADIR
QLYATAFEID PQWLIEAAAR RQKWIDQAQS LNIYMAGVSG KKIDETYKLA WLRGLKTTYY
LRSLAATSAE KSTIGAGSLN AVAEGNMAGM SAMVPATDVK LCAIDDPGCE SCQ
//
