ID C3NHP8_SULIN Unreviewed; 838 AA.
AC C3NHP8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Vitamin B12-dependent ribonucleotide reductase {ECO:0000256|RuleBase:RU364064};
DE EC=1.17.4.1 {ECO:0000256|RuleBase:RU364064};
GN OrderedLocusNames=YN1551_1570 {ECO:0000313|EMBL:ACP48658.1};
OS Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=419942 {ECO:0000313|EMBL:ACP48658.1, ECO:0000313|Proteomes:UP000006818};
RN [1] {ECO:0000313|EMBL:ACP48658.1, ECO:0000313|Proteomes:UP000006818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.N.15.51 / Yellowstone #2 {ECO:0000313|Proteomes:UP000006818};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001404; ACP48658.1; -; Genomic_DNA.
DR RefSeq; WP_012717503.1; NC_012623.1.
DR AlphaFoldDB; C3NHP8; -.
DR GeneID; 7809163; -.
DR KEGG; sin:YN1551_1570; -.
DR HOGENOM; CLU_000404_2_3_2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000006818; Chromosome.
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; cd02888; RNR_II_dimer; 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 NCBIfam; TIGR02506; NrdE_NrdA; 1.
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; 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; 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};
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|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 13..99
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 838 AA; 94916 MW; 432373248BA0A107 CRC64;
MEQLLYSTSL RKIKVIKRDG RVDEFKLEKI LSKLSSVPDE VTDGIVNDVQ ANVKDNAIDT
RAIADIVERN LIENSLKYPF LMELAKRYVL ARIYNHVFGK GKWKDFNEKD LLLSYNALKV
LEARYLLKDP NTLRYIETPQ MLFRRVARFL ASVERKYGKS EAEVKQLEEK FYEMISSLKF
VPNSPTLMNS ETRLGILSAC FVIPVKDAMT TPEGDGIYDA LRATALVHQQ GGGTGFDFSE
LRPKGDVVAS TAGVASGPVS FMKVFDASTD VIKQGGKRRG ANMGVMHAWH ADIEDFIRAK
TGQLKDVQLQ NFNISVGAYD YFMEAVVKGE SVPLINPRKT KIAGRDHEYY ITKARGYMNE
EWIQEVIISE LEEKGGVVSL DESKVITVDE ALIIASKEGA VVRYVNAKSL FDEIVKGAWD
SGDPGLLFID TINRRHPVWY LGKINATNPC GEEPLLPWES CNLGSINLEK FIIERNGKVE
IDWDGLAEII SYGVRFLDNV IDANRYPLKQ IEDATKRTRK VGLGVMGLAR MFIKLGIAYD
SVDAIYLSYQ LAKFIFYHAY KASIEVAKEK GPFPTYDSKL YRDIWESALD FNSLLQIAEV
ADKPSDYVKK LTSVVDKLDF DLLKDERLKY GLRNSTVVSI APTGTISIIA GTSSSIEPLF
ALAFVRNVAV GKFIEIDPLF LEYLRKYELD DPEVIQKIAE SGIIDDNVFM PRSLRKLFRT
AHEVPPIYHV LHQAAWQQWN DSGTSKTINL RSEEPPETVE KVYLLAWKLG IKGITVYRDK
SKQQQVIYFG VKKEREEYEK KKEEEGKKTQ LLPSSLRMEK KFVEVSETYA GGCKTCEL
//
