ID N9NKG1_9GAMM Unreviewed; 946 AA.
AC N9NKG1; N8WC86;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=F892_00736 {ECO:0000313|EMBL:ENX21504.1}, F971_01527
GN {ECO:0000313|EMBL:ENU92544.1};
OS Acinetobacter vivianii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1776742 {ECO:0000313|EMBL:ENX21504.1, ECO:0000313|Proteomes:UP000013173};
RN [1] {ECO:0000313|EMBL:ENX21504.1, ECO:0000313|Proteomes:UP000013173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 2168 {ECO:0000313|EMBL:ENX21504.1,
RC ECO:0000313|Proteomes:UP000013173};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 2168.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ENU92544.1, ECO:0000313|Proteomes:UP000013049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 758 {ECO:0000313|EMBL:ENU92544.1,
RC ECO:0000313|Proteomes:UP000013049};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 758.";
RL Submitted (FEB-2013) 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:ENX21504.1}.
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DR EMBL; APPC01000016; ENU92544.1; -; Genomic_DNA.
DR EMBL; APRW01000009; ENX21504.1; -; Genomic_DNA.
DR RefSeq; WP_004770761.1; NZ_KB850134.1.
DR AlphaFoldDB; N9NKG1; -.
DR PATRIC; fig|1217706.3.peg.698; -.
DR PATRIC; fig|1217712.3.peg.1463; -.
DR eggNOG; COG0209; Bacteria.
DR HOGENOM; CLU_000404_3_0_6; -.
DR OrthoDB; 9762933at2; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000013049; Unassembled WGS sequence.
DR Proteomes; UP000013173; 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; 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}.
FT DOMAIN 11..111
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
FT DOMAIN 122..211
FT /note="ATP-cone"
FT /evidence="ECO:0000259|PROSITE:PS51161"
SQ SEQUENCE 946 AA; 105397 MW; 443CAF40812A1054 CRC64;
MSIITSTPGQ LQVIKRTGEI APFNAEKISV AIGKAFLAVE GQQGTDSSRI HDRITQLTEM
VMNTFNRRLP SGGTIHIEEI QDQVELALMR TGEQKVARAY VIYRDQRASA RQQTGANHHP
TLQITDSNGQ LQPLDLDALT ATIQTASEGL EGIDVQAIVD ETVKNLYNGV KESDIATTMM
MATRTRIEQE PNYTYVTARL LSNELVSTGL EFLGLPSDTP EGNALETFLK KGIELDLLSA
DLLDFDLEKL AAAIKPERSN QFTYLGLQTL FDRYFIHSNG VRFELPQLFF MRVSMGLALN
EEHKEDRAIE FYDLLSSFDY MASTPTLFNS GTLRPQLSSC YLTTIGDDLY DIYGAMRDNA
MLSKWAGGLG NDWTPVRALN SYIKGTNGKS QGVVPFLKVA NDTAVAVNQG GKRKGAVCAY
LETWHLDVEE FLELRKNTGD DRRRTHDMNT ANWVPDLFMQ RVFEDAEWTL FTPSETPDLH
DLTGAEFAER YAHYEAVAKE QNMLHKKVRA KDLWRKMLSM LFETGHPWIT FKDVCNLRSP
QQHVGVVHSS NLCTEITLNT NQDEIAVCNL GSINLVQHVQ GGVLDREKLA RTVKTAVRML
DNVIDINYYA VPQAKNSNMK HRPVGMGIMG FQDALYEMNL AYGSDAAVDF ADESMEVISY
YAIETSSNLA IERGAYSTFK GSLWDQGILP IDSLEIVAKS RPERMFEVDR TQRLDWDTLR
AKVQKDGMRN SNVMAIAPTA TISNICGVSQ SIEPTFQNLY VKSNLSGEFT VINPYLVRAL
KERGLWDTVM VNDLKHFEGS VQKIARIPDE LKAIFATAFE VDTRWIVDAA SRRQKWIDQA
QSLNLYIAGA NGKKLDITYK MAWLRGLKTT YYLRALGATS AEKSTINTGA LNAVKPASVE
APVVAAAPAA VAEKKPETPV EEDGFTTAAP VPMACSIDNP DCEACQ
//
