ID A1WHZ9_VEREI Unreviewed; 968 AA.
AC A1WHZ9;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
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 OrderedLocusNames=Veis_1496 {ECO:0000313|EMBL:ABM57256.1};
OS Verminephrobacter eiseniae (strain EF01-2).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Verminephrobacter.
OX NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM57256.1, ECO:0000313|Proteomes:UP000000374};
RN [1] {ECO:0000313|Proteomes:UP000000374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL Submitted (DEC-2006) 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; CP000542; ABM57256.1; -; Genomic_DNA.
DR RefSeq; WP_011809263.1; NC_008786.1.
DR AlphaFoldDB; A1WHZ9; -.
DR STRING; 391735.Veis_1496; -.
DR GeneID; 76460118; -.
DR KEGG; vei:Veis_1496; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_4; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000000374; 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; 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; 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:UP000000374}.
FT DOMAIN 33..133
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 147..236
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 107425 MW; 578D5719A0B8F751 CRC64;
MQAALHKPAT AHTLPADVQA KPAAAPDHAL EHYQIMRRNG AVVPFQPQKI ALAMMKAFLA
VHGTQGAASA SVREVVDGLT QTVTRALMRS RPGGGTFHIE DVQDQVELGL MRGGHHEIAR
SYVLYRERRT QERSRQGSPQ QPAAALLHVL DAGVRVALDP ARLQALIESA CVGLGPDVKA
DPIVAETMRN LYDGVPMDEV CKAAILAART LIEKDPDYSY ATARLLLHTI VREVLGSDVP
QAQMALAYGD YFPRFIKKGV DNGLLDERLL QYDLQRLGAA IRAERDLKFD YLGLQTLYDR
YFLHVRKTRI ELPQVFFMRV AMGLALNEVE REARAIEFYE VLSSFDFMSS TPTLFNSGTL
RSQLSSCYLT TVPDDLDGIY ESIKENALLS KFAGGLGNDW TRVRALGSYI AGTNGESQGV
VPFLKVVNDT AVAVNQGGKR KGAVCTYLET WHLDIEEFLE LRKNTGDDRR RTHDMNTANW
IPDLFMHRVM EKGHWTLFSP SSVPDLHELF GADFEKAYVA YEEQAARGAI GPARTVQATD
LWRKMLTMLF ETGHPWITFK DACNLRSPQQ HAGVVHSSNL CTEITLNTSD SETAVCNLGS
VNLLQHLKDG QIDHDKLRQT ITVAMRMLDN VIDINYYAVR KARDSNLRHR PVGLGVMAFQ
DCLYELRIPY ASQAAVEFAD QSMEAICYYA YWASTELAKE RGKYLSYEGS LWERGQLPLD
TLDLLAQARG DYLQVDRSSR LDWDALRQKI AQDGMRNSNC VAIAPTATIS NIVGVDASIE
PSFGNLSVKS NLSGEFTVIN AGLVRDLKRL GLWDEVMIMD LKHFKGSLHP IDRVPQDIKA
LYSTAFEVDP QWLVEAASRR QKWIDQAQSL NIYMAGASGR KLDETYKLAW VRGLKTTYYL
RTQSATHVEM STVNTGQLNA VSSGPHGDAF GAAATSTPMS TAAAQAGDRP ATDIAFCALD
NPTCEACQ
//
