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Database: UniProt
Entry: K0SAD9_THAOC
LinkDB: K0SAD9_THAOC
Original site: K0SAD9_THAOC 
ID   K0SAD9_THAOC            Unreviewed;       181 AA.
AC   K0SAD9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=THAOC_17484 {ECO:0000313|EMBL:EJK61934.1};
OS   Thalassiosira oceanica (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK61934.1, ECO:0000313|Proteomes:UP000266841};
RN   [1] {ECO:0000313|EMBL:EJK61934.1, ECO:0000313|Proteomes:UP000266841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK61934.1,
RC   ECO:0000313|Proteomes:UP000266841};
RX   PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA   Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA   Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA   Rosenstiel P., Hippler M., Laroche J.;
RT   "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT   limitation.";
RL   Genome Biol. 13:R66-R66(2012).
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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:EJK61934.1}.
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DR   EMBL; AGNL01019300; EJK61934.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0SAD9; -.
DR   EnsemblProtists; EJK61934; EJK61934; THAOC_17484.
DR   eggNOG; KOG3347; Eukaryota.
DR   OMA; QCEIFGT; -.
DR   Proteomes; UP000266841; 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:UP000266841};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03173}.
FT   REGION          38..61
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         44
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   181 AA;  20964 MW;  ECDBA9889E1A54F3 CRC64;
     MSDTERKRPN ILITGTPGVG KTATASLIAE QIGFRHVNVG DLIKQHKCYD GRDEDLDTHI
     LDEDKLLDLM ESMFQECADE NKGIVADYHS SELFPERWFD LILVLRARTE VLFDRLSQRG
     YGEKKRDENL EAEIMQVCLD EAKESYDKEI VVEVHSNTIE EMESNVDRCK IWVEQWIKDN
     A
//
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