NDKM_COLLI
ID NDKM_COLLI Reviewed; 181 AA.
AC P87355; O42206;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Nucleoside diphosphate kinase, mitochondrial;
DE Short=NDK;
DE Short=NDP kinase, mitochondrial;
DE EC=2.7.4.6;
DE Flags: Precursor;
GN Name=NME4;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver;
RA Mehus J.G., Milavetz B.I., Ivey M.A., Lambeth D.O.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-181, PROTEIN SEQUENCE OF 25-44, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9305928; DOI=10.1074/jbc.272.39.24604;
RA Lambeth D.O., Mehus J.G., Ivey M.A., Milavetz B.I.;
RT "Characterization and cloning of a nucleoside-diphosphate kinase targeted
RT to matrix of mitochondria in pigeon.";
RL J. Biol. Chem. 272:24604-24611(1997).
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. Through the catalyzed exchange of gamma-phosphate between
CC di- and triphosphonucleosides participates in regulation of
CC intracellular nucleotide homeostasis. Binds to anionic phospholipids,
CC predominantly to cardiolipin; the binding inhibits its phosphotransfer
CC activity. Acts as mitochondria-specific NDK coupled to respiration.
CC Promotes the redistribution of cardiolipin between the mitochondrial
CC inner membrane and outer membrane which is implicated in pro-apoptotic
CC signaling (By similarity). {ECO:0000250|UniProtKB:O00746}.
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 -!- ACTIVITY REGULATION: Feedback inhibition by ADP.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000250|UniProtKB:O00746}; Peripheral membrane protein
CC {ECO:0000305}. Mitochondrion matrix {ECO:0000269|PubMed:9305928}.
CC -!- TISSUE SPECIFICITY: Highest levels in the liver and kidney with lower
CC levels in the heart, brain and breast muscle.
CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}.
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DR EMBL; U89605; AAC78439.1; -; mRNA.
DR EMBL; AF018267; AAC78438.1; -; Genomic_DNA.
DR AlphaFoldDB; P87355; -.
DR SMR; P87355; -.
DR STRING; 8932.XP_005505701.1; -.
DR eggNOG; KOG0888; Eukaryota.
DR BRENDA; 2.7.4.6; 1579.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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:0006869; P:lipid transport; IEA:UniProtKB-KW.
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 ATP-binding; Direct protein sequencing; Kinase; Lipid transport;
KW Lipid-binding; Magnesium; Membrane; Metal-binding; Mitochondrion;
KW Nucleotide metabolism; Nucleotide-binding; Phosphoprotein; Transferase;
KW Transit peptide; Transport.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9305928"
FT CHAIN 25..181
FT /note="Nucleoside diphosphate kinase, mitochondrial"
FT /id="PRO_0000019431"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 181 AA; 20342 MW; B892F7C44C001D2C CRC64;
MFRGGTHRLR GQPGLSLPHG PRCYGSAPPE LQEKTLVLVK PDAVQRRLVG NVIQRFERRG
FKLVAMKLLQ ADQGLLDKHY QQLRQKPFYP ALLAYMTSGP LVAMVWEGYN VVRSTRAMVG
DTDSAVAAAG TIRGDFSMHV SRNVVHASDS VETAQREIGF WFQRNELVAW ESGDRDYTWG
P
