NDK_ASPFU
ID NDK_ASPFU Reviewed; 153 AA.
AC Q7Z8P9; Q4WEM0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Nucleoside diphosphate kinase;
DE Short=NDK;
DE Short=NDP kinase;
DE EC=2.7.4.6;
GN Name=ndk1; ORFNames=AFUA_5G03490;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shankar J., Kamal N., Madan T., Basir S.F., Sarma P.U.;
RT "Aspergillus fumigatus (NDK) is a putative nucleoside diphosphate kinase.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC than ATP. The ATP gamma phosphate is transferred to the NDP beta
CC phosphate via a ping-pong mechanism, using a phosphorylated active-site
CC intermediate.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; AY324230; AAP85295.1; -; Genomic_DNA.
DR EMBL; AAHF01000011; EAL85957.1; -; Genomic_DNA.
DR RefSeq; XP_747995.1; XM_742902.1.
DR PDB; 6AGY; X-ray; 1.80 A; A=1-153.
DR PDB; 6XP4; X-ray; 2.00 A; A/B/C/D/E/F=1-153.
DR PDB; 6XP7; X-ray; 2.20 A; A/B/C=1-153.
DR PDB; 6XPS; X-ray; 1.64 A; A/B/C=1-153.
DR PDB; 6XPT; X-ray; 2.30 A; A/B/C/E/G/H=1-153.
DR PDB; 6XPU; X-ray; 1.90 A; A/B/C=1-153.
DR PDB; 6XPV; X-ray; 2.30 A; A/B/C/E/G/H=1-153.
DR PDB; 6XPW; X-ray; 1.90 A; A/B/C/E/G/H=1-153.
DR PDBsum; 6AGY; -.
DR PDBsum; 6XP4; -.
DR PDBsum; 6XP7; -.
DR PDBsum; 6XPS; -.
DR PDBsum; 6XPT; -.
DR PDBsum; 6XPU; -.
DR PDBsum; 6XPV; -.
DR PDBsum; 6XPW; -.
DR AlphaFoldDB; Q7Z8P9; -.
DR SMR; Q7Z8P9; -.
DR STRING; 746128.CADAFUBP00005090; -.
DR SwissPalm; Q7Z8P9; -.
DR PRIDE; Q7Z8P9; -.
DR EnsemblFungi; EAL85957; EAL85957; AFUA_5G03490.
DR GeneID; 3505356; -.
DR KEGG; afm:AFUA_5G03490; -.
DR VEuPathDB; FungiDB:Afu5g03490; -.
DR eggNOG; KOG0888; Eukaryota.
DR HOGENOM; CLU_060216_6_3_1; -.
DR InParanoid; Q7Z8P9; -.
DR OMA; KIVAMKM; -.
DR OrthoDB; 1334716at2759; -.
DR BRENDA; 2.7.4.6; 508.
DR Proteomes; UP000002530; Chromosome 5.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.70.141; -; 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 Pfam; PF00334; NDK; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00562; NDK; 1.
DR SUPFAM; SSF54919; SSF54919; 1.
DR PROSITE; PS00469; NDP_KINASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..153
FT /note="Nucleoside diphosphate kinase"
FT /id="PRO_0000137148"
FT ACT_SITE 117
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:6XPS"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 60..67
FT /evidence="ECO:0007829|PDB:6XPS"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6XPS"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6XPS"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6XPS"
SQ SEQUENCE 153 AA; 16932 MW; 5432887C72096447 CRC64;
MSNEQTFIAI KPDGVQRGLI GPIISRFENR GFKLVAMKLV SPPQSQLEQH YADLSDKPFF
KGLVSYMLSG PICAMVWEGR DVVKTGRTIL GATNPLASAP GTIRGDFAID VGRNVCHGSD
SVENAKKEIA LWFKPEELIS WKSATFDWVY EKA
