ID A0A1Z8ULY9_9PROT Unreviewed; 629 AA.
AC A0A1Z8ULY9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CBC12_09075 {ECO:0000313|EMBL:OUU47943.1};
OS Candidatus Puniceispirillum sp. TMED52.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC Puniceispirillum.
OX NCBI_TaxID=1986639 {ECO:0000313|EMBL:OUU47943.1, ECO:0000313|Proteomes:UP000195809};
RN [1] {ECO:0000313|EMBL:OUU47943.1, ECO:0000313|Proteomes:UP000195809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED52 {ECO:0000313|EMBL:OUU47943.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-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:OUU47943.1}.
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; NHDF01000111; OUU47943.1; -; Genomic_DNA.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000195809; 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 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 26..96
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 100..439
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 444..599
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 629 AA; 71052 MW; ABBD535CA6C42184 CRC64;
MTSTTSKIGK QDYLGIQIDY DRDDLLNTFS LETLKDRYFW ENETHAQEAF ARASVYSATY
QGHTDYNLAQ RLYDYASKGW FGFSTPILSN GGTTRGLPIS CFLNYVPDSR RGLSDHYDEN
IWLASGGGGL GGYWGAVRSN GVSTSNGSQS TGSIPFMHVV DSQMLAFNQG ITRRGSYAAY
MDITHPEVEE FIAMRKTTGG DLNRKCLNLH NGITITDEFL EAVXNDDQWR LIDPKSKQAI
KTVSARDLWW QLIHTRAETG EPYIVNLDRC NEALPQSQKD MGLEVRQSNL CSEITLPTSE
ERTAVCCLSS VNLEYFDEWK DNELFISDLI TMLDNVIEHF IDNATHGEHA WHFDDTFEEF
SKYVHPDKKG FTKAAYSAYR ERAIGLGAMG FHSYLQRNGI PFEGMYAASF NNRAFKHIKD
RATSASSVLA SERTEAPDMV GRNLRNSHLL AIAPNASSSI ICGGTSPSIE PTRANVFTHK
TLTGSYKVKN KYLEELLEKK GINNEQTWKD IAAAEGSVKD LEELTEEEKE VFKTAPELNQ
IWVIEHAYQR QKYVCQAQSV NLFFEPPPAT APQEVHDEYL AYVNHVHWTG ANKLKSMYYL
RTTAARNTEN VNIKIPRINL EEECLSCEG
//
