ID J9YZZ8_9PROT Unreviewed; 912 AA.
AC J9YZZ8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=HIMB59_00005020 {ECO:0000313|EMBL:AFS48702.1};
OS alpha proteobacterium HIMB59.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=744985 {ECO:0000313|EMBL:AFS48702.1, ECO:0000313|Proteomes:UP000006097};
RN [1] {ECO:0000313|EMBL:AFS48702.1, ECO:0000313|Proteomes:UP000006097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB59 {ECO:0000313|EMBL:AFS48702.1,
RC ECO:0000313|Proteomes:UP000006097};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
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:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; CP003801; AFS48702.1; -; Genomic_DNA.
DR AlphaFoldDB; J9YZZ8; -.
DR STRING; 744985.HIMB59_00005020; -.
DR KEGG; apc:HIMB59_00005020; -.
DR PATRIC; fig|744985.3.peg.500; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_5; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000006097; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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: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; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 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; 2.
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};
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00492};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000006097}.
FT DOMAIN 30..128
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 145..233
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 912 AA; 103123 MW; 486B9E198D07A083 CRC64;
METNSAENTE NSTKNTVINK QNEEVNLLSL SVVRRDGSIT PFKSDKIANA IRKAFLAQTD
VRDNTKIDQT VNDITETVTA ALTRRIANGD MIHIEDIQDQ VELALMRGEH HKVARAYVLY
REQRAKQRYK TAKLNEQVGA KVSTMAVTKR DGHKEDISLE KITNRISVLS NGLEIDPITI
AQKAIQGLYD GITTNEIDTY LAETAAALTV EHPDYSYLAG RIKANALHKE TPGFIIATKN
LFEDGLLREE YYQKAMAHAE DIEKIIDYDR DYLFDYFALT TLFRAYLLQF NNKTIERPQD
LWMRVALCVS GDKFDFYQVK KTYDSLSQGL YTHATPTLFN SGLKMQQLSS CFLIGMEDDS
IEGIFNTVKD CALISKTAGG IGLHAHNIRA GGSRIKSTNG KSNGLIPFLK IFNETARSVD
QGGGKRKGSF AVYLEPWHAD IEAFLELRKN TGAEEFRARD LFYALWIPDL FMQRVEEDGE
WTLMSEHECP GLSNTYGSEF VELYTKYEKE MPDLKRVKAR ALMSKIIEAQ IETGQPYMLY
KDSINNKSNQ KNIGVIKSSN LCAEIVEYSE KDETAVCNLA SIALPKFVTE DGKYDYQNLY
QIAKLATKNL DQVIDINFYP TDKTQNSNSR HRPIGLGIQG LADVYFKMNL AYDSVQAQII
NKQIFETIYF GALEASMELA ADKGAYSTFQ GSPLSQGQFQ FDLWGVKPSN MWDWKGLMEK
IQKHGVRNSL TTACMPTAST GIILGNTETF QVQTSNIYKR QTLSGEFLLV NRYLVKELMA
RGLWSKELRD QIILENGSVQ NIEGFPEDLK EVYKTVWETS QKTVIDMAAE RAPFIDQTQS
MNLWLATPTF GKVNSMHMYA WKKGLKTGMY YLRSRSAVDA VKVTVSSEKK AKETYVKEAQ
SNEPEDCLTC SA
//
