ID H3KC19_9BURK Unreviewed; 591 AA.
AC H3KC19;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=HMPREF9440_00269 {ECO:0000313|EMBL:EHY32343.1};
OS Sutterella parvirubra YIT 11816.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=762967 {ECO:0000313|EMBL:EHY32343.1, ECO:0000313|Proteomes:UP000004956};
RN [1] {ECO:0000313|EMBL:EHY32343.1, ECO:0000313|Proteomes:UP000004956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11816 {ECO:0000313|EMBL:EHY32343.1,
RC ECO:0000313|Proteomes:UP000004956};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2011) 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:EHY32343.1}.
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DR EMBL; AFBQ01000034; EHY32343.1; -; Genomic_DNA.
DR RefSeq; WP_008540688.1; NZ_JH604866.1.
DR AlphaFoldDB; H3KC19; -.
DR STRING; 762967.HMPREF9440_00269; -.
DR PATRIC; fig|762967.3.peg.226; -.
DR HOGENOM; CLU_000404_7_0_4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000004956; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004956}.
FT DOMAIN 12..77
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 82..396
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 406..550
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
SQ SEQUENCE 591 AA; 66772 MW; 6E55388003E5471A CRC64;
MSIKTDPSRD RLFGELAMMR LKESYMRPDE TSPQERLAFV AEQFATDEAH AQRIYDYASR
QWLSFSTPIL AFGRAKRGLP ISCFLTYMAD SSEGLLQTLD EVNRLSMLGG GVGIHVAIRS
ADEKSVGVMP HLKVYDAASL AYRQGSTRRG SYAAFLDVSH PDIIPFVEMR KPTGDQNMKA
LNLHHGVNIS DAFMEKVEAS MRDDSYDDTW PLVDPASGKV VTTVSARDLW QRMLEMRMHT
GEPYLVFTDT ANRALPSWLA EKGLKINGSN LCTEIFLPTS AERTAVCCLS SVNLEYFDEW
KDDQQFIPDA MEFLDNVLQY FIDHAPDQIG RAKFAAARER SVGLGAMGLH AYFQKNRIPF
DSALAKGANI RIFRHIQNEC RRADEILCKL RGPCPDAADA GVERCFSHWN AVAPNASSSL
IMGGTSPSIE PYRANIYRQD TISGAYIMKN RFLEAELEKL GLNTQETWSD LIAHDGSIQH
REDIPKEIRE VFKTAFELDQ RWLIELAADR QQFIDQGQSV NLFFPPDVSV PYLHVCHFLA
WKKGLKSLYY NRSDKLRKAD RPGTALERRR IEDDISMRAV ADNDTCLACE G
//
