ID A0A1D6HXQ0_MAIZE Unreviewed; 179 AA.
AC A0A1D6HXQ0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Adenylate kinase isoenzyme 6 homolog {ECO:0000256|HAMAP-Rule:MF_03173};
DE Short=AK6 {ECO:0000256|HAMAP-Rule:MF_03173};
DE EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03173};
DE AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000256|HAMAP-Rule:MF_03173};
DE Short=AK/ATPase {ECO:0000256|HAMAP-Rule:MF_03173};
GN Name=103632249 {ECO:0000313|EnsemblPlants:Zm00001eb305840_P001};
GN ORFNames=ZEAMMB73_Zm00001d019481 {ECO:0000313|EMBL:ONM52995.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EnsemblPlants:Zm00001eb305840_P001, ECO:0000313|Proteomes:UP000007305};
RN [1] {ECO:0000313|EMBL:ONM52995.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb305840_P001,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM52995.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:Zm00001eb305840_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb305840_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC catalyzes the reversible transfer of the terminal phosphate group
CC between nucleoside triphosphates and monophosphates. Has also ATPase
CC activity. {ECO:0000256|HAMAP-Rule:MF_03173}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000582, ECO:0000256|HAMAP-
CC Rule:MF_03173};
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03173}.
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DR EMBL; CM007650; ONM52995.1; -; Genomic_DNA.
DR RefSeq; XP_008652287.1; XM_008654065.1.
DR AlphaFoldDB; A0A1D6HXQ0; -.
DR SMR; A0A1D6HXQ0; -.
DR IntAct; A0A1D6HXQ0; 22.
DR STRING; 4577.A0A1D6HXQ0; -.
DR PaxDb; 4577-GRMZM2G032699_P02; -.
DR EnsemblPlants; Zm00001eb305840_T001; Zm00001eb305840_P001; Zm00001eb305840.
DR GeneID; 103632249; -.
DR Gramene; Zm00001eb305840_T001; Zm00001eb305840_P001; Zm00001eb305840.
DR KEGG; zma:103632249; -.
DR eggNOG; KOG3347; Eukaryota.
DR InParanoid; A0A1D6HXQ0; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 5472563at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; A0A1D6HXQ0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595:SF0; ADENYLATE KINASE ISOENZYME 6; 1.
DR PANTHER; PTHR12595; POS9-ACTIVATING FACTOR FAP7-RELATED; 1.
DR Pfam; PF13238; AAA_18; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_03173, ECO:0000313|EMBL:ONM52995.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D6HXQ0};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..66
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT REGION 118..128
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 23..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 49
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 179 AA; 19921 MW; C5882FE4BB69DC91 CRC64;
MAVGSGGGSR RARPNVLVTG TPGTGKTTTC SLLADAAGLR HVNIGDLVRE KSLHDGWDAD
LECHVINEDL VCDELEDMME EGGILVDYHG CDFFPERWFD LVVVLQTDNS ILHDRLTGRG
YMGSKLANNI ECEIFQVLLE EARESYREDI VMPLRSDNVE DISRNVGALT DWVNNWRPS
//
