ID B8NQF0_ASPFN Unreviewed; 153 AA.
AC B8NQF0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Nucleoside diphosphate kinase {ECO:0000256|ARBA:ARBA00017632, ECO:0000256|RuleBase:RU004013};
DE EC=2.7.4.6 {ECO:0000256|ARBA:ARBA00012966, ECO:0000256|RuleBase:RU004013};
GN ORFNames=AFLA_006300 {ECO:0000313|EMBL:EED47988.1}, G4B84_006862
GN {ECO:0000313|EMBL:QMW31481.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED47988.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED47988.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED47988.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0007829|PDB:6K3H}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS).
RX PubMed=31243100; DOI=10.1074/jbc.ra119.007505;
RA Wang Y., Wang S., Nie X., Yang K., Xu P., Wang X., Liu M., Yang Y.,
RA Chen Z., Wang S.;
RT "Molecular and structural basis of nucleoside diphosphate kinase-mediated
RT regulation of spore and sclerotia development in the fungus <i>Aspergillus
RT flavus</i>.";
RL J. Biol. Chem. 294:12415-12431(2019).
RN [3] {ECO:0007829|PDB:6JOH}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RA Wang Y., Wang S.H.;
RT "Molecular and structural basis of Nucleoside Diphosphate Kinase regulating
RT the spores and sclerotia development in Aspergillus flavus.";
RL Submitted (MAR-2019) to the PDB data bank.
RN [4] {ECO:0000313|EMBL:QMW31481.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW31481.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000082,
CC ECO:0000256|RuleBase:RU004013};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000937};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000256|ARBA:ARBA00008142,
CC ECO:0000256|RuleBase:RU004011}.
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DR EMBL; EQ963482; EED47988.1; -; Genomic_DNA.
DR EMBL; CP059869; QMW31481.1; -; Genomic_DNA.
DR RefSeq; XP_002382830.1; XM_002382789.1.
DR PDB; 6JOH; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-153.
DR PDB; 6K3H; X-ray; 2.18 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-153.
DR PDBsum; 6JOH; -.
DR PDBsum; 6K3H; -.
DR AlphaFoldDB; B8NQF0; -.
DR SMR; B8NQF0; -.
DR STRING; 332952.B8NQF0; -.
DR EnsemblFungi; EED47988; EED47988; AFLA_006300.
DR VEuPathDB; FungiDB:AFLA_011985; -.
DR eggNOG; KOG0888; Eukaryota.
DR HOGENOM; CLU_060216_6_3_1; -.
DR OMA; QHYGEHK; -.
DR OrthoDB; 3075753at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR CDD; cd04413; NDPk_I; 1.
DR Gene3D; 3.30.70.141; Nucleoside diphosphate kinase-like domain; 1.
DR HAMAP; MF_00451; NDP_kinase; 1.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR PANTHER; PTHR11349; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR PANTHER; PTHR11349:SF91; NUCLEOSIDE DIPHOSPHATE KINASE; 1.
DR Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; Nucleoside diphosphate kinase, NDK; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6JOH, ECO:0007829|PDB:6K3H};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004013};
KW Kinase {ECO:0000256|RuleBase:RU004013, ECO:0000313|EMBL:EED47988.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004013};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004013}.
FT DOMAIN 3..140
FT /note="Nucleoside diphosphate kinase-like"
FT /evidence="ECO:0000259|SMART:SM00562"
SQ SEQUENCE 153 AA; 17010 MW; 72F7BEE651A66AD7 CRC64;
MSDEQTFIAI KPDGVQRGLV GPIISRFENR GFKLAALKLC SPSKEHLEQH YADLSSKPFF
PGLVSYMLSG PIVAMVWEGR EVVKTGRTIL GATNPLASAP GTIRGDFAID VGRNVCHGSD
SVENAKKEIA LWFKPEELQK YKHSQFDWIY EKA
//
