ID A0A258H2I5_9PROT Unreviewed; 621 AA.
AC A0A258H2I5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=B7Y90_03970 {ECO:0000313|EMBL:OYX50482.1};
OS Alphaproteobacteria bacterium 32-64-14.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1970492 {ECO:0000313|EMBL:OYX50482.1, ECO:0000313|Proteomes:UP000215897};
RN [1] {ECO:0000313|EMBL:OYX50482.1, ECO:0000313|Proteomes:UP000215897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32-64-14 {ECO:0000313|EMBL:OYX50482.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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}.
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:OYX50482.1}.
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DR EMBL; NCEM01000008; OYX50482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258H2I5; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000215897; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
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.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 42..107
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 111..430
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 439..584
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 69137 MW; 4066D9562A9B7CD7 CRC64;
MSMSAEAVLT EDKTAARRGK PKAQSGLRVV EGVKTDPSRD ALLTDFGKKT LDDRYVLPGE
SYQDMFARVA LAYSDDVVHA QRIYDYISRL WFMPATPVLS NGGADRGLPI SCFLNGVSDS
LDGIVETWNE NVWLASNGGG IGTYWGEVRS IGEKVGQNGQ TSGIIPFIRV MDSLTLAISQ
GSLRRGSAAC YLDVFHPEIE EFLEIRKAAG DFNRKSLNLH HGINITDEFM EAVRQDAPFQ
LKSPKTGEVM KEISARKLWQ KILELRMATG EPYLLFTDTT NNAMPAHQKQ LGFKVRQSNL
CSEIMLHTGP DHLGVDRTAV CCLSSVNAEK FLEWKSNENF LDDIFRFLDN VLEDFIKRAP
PEMHRAVYSA KRERSVGLGL MGFHSFLQSQ GVAMESSTAK SWNNVMFKHL RRGADAASVK
LAKERGACPD AEDMGVMARF SHKLAIAPTA SISIICGGTS AGIEPIPANI YTHKTLSGSF
SVKNPFLEQV LEKTGNNTPG IWASILENEG SVQHLDCLTG QEKLVFRTAF EIDQRWIIEL
AADRTPYICQ GQSLNLFLPA DIDKWDLHML HWTAWEKGLK SLYYCRSKSI QRAGFAGSDR
EKVEMDMGRG RTDYDECLAC Q
//
