ID A0A059LQ79_9CHLO Unreviewed; 173 AA.
AC A0A059LQ79;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 22-FEB-2023, entry version 26.
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 ORFNames=H632_c294p1 {ECO:0000313|EMBL:KDD76260.1};
OS Helicosporidium sp. ATCC 50920.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Helicosporidium.
OX NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD76260.1, ECO:0000313|Proteomes:UP000026042};
RN [1] {ECO:0000313|EMBL:KDD76260.1, ECO:0000313|Proteomes:UP000026042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD76260.1,
RC ECO:0000313|Proteomes:UP000026042};
RX PubMed=24809511;
RA Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT "A lack of parasitic reduction in the obligate parasitic green alga
RT helicosporidium.";
RL PLoS Genet. 10:E1004355-E1004355(2014).
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}.
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:KDD76260.1}.
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DR EMBL; AYPS01000294; KDD76260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059LQ79; -.
DR STRING; 1291522.A0A059LQ79; -.
DR OrthoDB; 5472563at2759; -.
DR Proteomes; UP000026042; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_03173};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03173};
KW Reference proteome {ECO:0000313|Proteomes:UP000026042};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT REGION 35..58
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT REGION 110..120
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 15..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 41
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03173"
SQ SEQUENCE 173 AA; 19708 MW; B9C3B50583C851B3 CRC64;
MSRSQPNILI TGTPGTGKTT TAELLASAAG LEHVNVGQLV KDEGLHSGWD ERFQCHILDE
DKVCDELEDK MGRGGCVVDH HGCDFFPERW FDLVVVLQAD NSVLWERLEE REYPTHKIQE
NVQCEIMHVV VEEARESYRE DVVQVLSSNT VDEMERNVSQ LTEWVAAWRQ NNA
//
