ID A0A2R4ZVP7_9CREN Unreviewed; 209 AA.
AC A0A2R4ZVP7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Putative adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00039};
DE Short=AK {ECO:0000256|HAMAP-Rule:MF_00039};
DE EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00039};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00039};
GN ORFNames=ATG_17200 {ECO:0000313|EMBL:GAY26516.1};
OS Desulfurococcaceae archaeon AG1.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae.
OX NCBI_TaxID=2027460 {ECO:0000313|EMBL:GAY26516.1, ECO:0000313|Proteomes:UP000245022};
RN [1] {ECO:0000313|EMBL:GAY26516.1, ECO:0000313|Proteomes:UP000245022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1 {ECO:0000313|EMBL:GAY26516.1,
RC ECO:0000313|Proteomes:UP000245022};
RA Oinishi Y., Fujiwara S., Yumiya M., Fukuyama Y., Omae K., Takashi Y.,
RA Sako Y.;
RT "Draft Genome Sequence of Genus novel archaea, Isolated from Hot Spring in
RT Japan.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|HAMAP-Rule:MF_00039}.
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_00039};
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00039}.
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:GAY26516.1}.
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DR EMBL; BEWT01000016; GAY26516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4ZVP7; -.
DR Proteomes; UP000245022; Unassembled WGS sequence.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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_00039};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00039};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW Reference proteome {ECO:0000313|Proteomes:UP000245022};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00039}.
FT REGION 29..52
FT /note="NMP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT REGION 109..119
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 9..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
SQ SEQUENCE 209 AA; 23891 MW; 242B4CD2ACA01E25 CRC64;
MIAISGTPGV GKSTVAKIVS RILNAEVIDL SELVLKRHLY SDYDEKRKSY IVDEALVKKE
LRTLISRCGD GKEYLIVEGH YAEIVDEKDL EILVVLRIDP RELVKRLCIR GWSLEKSLEN
GEAEYLGICL SNALEEHPRE KVCEIDVTRE DPELVAKRIV DLVRSRVKCE PYIDWTISID
PRELWETATK YCARDMGKDG ETRGEEKKG
//
