ID A0A031LQG8_9GAMM Unreviewed; 941 AA.
AC A0A031LQG8;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=CL42_08945 {ECO:0000313|EMBL:EZQ10061.1};
OS Acinetobacter sp. Ver3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ10061.1, ECO:0000313|Proteomes:UP000023816};
RN [1] {ECO:0000313|EMBL:EZQ10061.1, ECO:0000313|Proteomes:UP000023816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ10061.1,
RC ECO:0000313|Proteomes:UP000023816};
RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT isolated from a high altitude andean lake.";
RL Submitted (MAR-2014) 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:EZQ10061.1}.
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DR EMBL; JFYL01000027; EZQ10061.1; -; Genomic_DNA.
DR RefSeq; WP_035267250.1; NZ_JFYL01000027.1.
DR AlphaFoldDB; A0A031LQG8; -.
DR eggNOG; COG0209; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000023816; Unassembled WGS sequence.
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}.
FT DOMAIN 10..110
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 121..210
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 941 AA; 105348 MW; 08AF5971B9C2037C CRC64;
MSANTTPGQL QVIKRTGDVA TFDADKISVA IGKAFLAVEG QPSADSSRIH DRITQLTEMV
MNTFKRRLPS GGTIHIEEIQ DQVELALMRT GEQKVARAYV IYREQRAEAR KELGAHHHPT
LQITGQNGQL QPLDLSRLQA KIEKASEGLE GIDVQAIIDE TVKNLYNGVK ASDISTTMMM
ATRTRIEQEP NYTYVTARLL RDNLVATGLE FLGLSKDTLE NDALETFLKK GVELELLSPE
LLNFDLVKLA AAIKPERSNQ FTYLGLQTLF DRYFIHSDGV RFELPQLFFM RVSMGLSLNE
DNREDRAIEF YNLLSSFDYM ASTPTLFNSG TLRPQLSSCY LTTIDDDLFD IYGAMRDNAM
LSKWAGGLGN DWTPVRALNS YIKGTNGKSQ GVVPFLKVAN DTAVAVNQGG KRKGAVCAYL
ETWHLDIEEF LELRKNTGDD RRRTHDMNTA NWVPDLFMQR VFEDAEWTLF TPSETPDLHD
LTGAEFAERY AYYESIAKET DMLHKKVRAK DLWRKMLSML FETGHPWITF KDVCNLRSPQ
QHVGVVHSSN LCTEITLNTS KDEIAVCNLG SINLVQHVRG GQLDREKLAR TIKTAVRMLD
NVIDINYYAV PQARNSNLKH RPVGMGIMGF QDALYEMKIA YGSDAAVEFA DESMEVISYY
AIQTSSDLAV ERGTYETFKG SLWDQGILPI DSLELVAKSR PERMFEVDRT QRLDWDTLRA
KVQKDGMRNS NVMAIAPTAT ISNICGVSQS IEPTFQNLYV KSNLSGEFTV INPYLVRALK
ERGLWDSVMV NDLKHFEGSV QKIARIPEEL KAIFATAFEV EARWIVDAAS RRQKWIDQAQ
SLNLYISGAN GKKLDITYKM AWLRGLKTTY YLRALGATSA EKSTINTGAL NAVKPATVAA
PVAAVAQEAK PEAAASEEGF EQAAPVPMAC SIDNPDCEAC Q
//
