ID E6N494_CALS0 Unreviewed; 191 AA.
AC E6N494;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=CSUB_C0078 {ECO:0000313|EMBL:BAJ49942.1}, HGMM_F25E12C34
GN {ECO:0000313|EMBL:BAJ47113.1};
OS Caldiarchaeum subterraneum.
OC Archaea; Nitrososphaerota; Candidatus Caldarchaeales;
OC Candidatus Caldarchaeaceae; Candidatus Caldarchaeum.
OX NCBI_TaxID=311458 {ECO:0000313|EMBL:BAJ47113.1, ECO:0000313|Proteomes:UP000008120};
RN [1] {ECO:0000313|EMBL:BAJ47113.1, ECO:0000313|Proteomes:UP000008120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT "Genetic and functional properties of uncultivated thermophilic
RT crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT genome fragments.";
RL Environ. Microbiol. 7:1967-1984(2005).
RN [2] {ECO:0000313|EMBL:BAJ47113.1, ECO:0000313|Proteomes:UP000008120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21169198; DOI=10.1093/nar/gkq1228;
RA Nunoura T., Takaki Y., Kakuta J., Nishi S., Sugahara J., Kazama H.,
RA Chee G., Hattori M., Kanai A., Atomi H., Takai K., Takami H.;
RT "Insights into the evolution of Archaea and eukaryotic protein modifier
RT systems revealed by the genome of a novel archaeal group.";
RL Nucleic Acids Res. 39:3204-3223(2011).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00039}.
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DR EMBL; AP011827; BAJ47113.1; -; Genomic_DNA.
DR EMBL; BA000048; BAJ49942.1; -; Genomic_DNA.
DR AlphaFoldDB; E6N494; -.
DR STRING; 311458.CSUB_C0078; -.
DR KEGG; csu:CSUB_C0078; -.
DR BioCyc; CCAL311458:G131R-78-MONOMER; -.
DR Proteomes; UP000008120; Chromosome.
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:UP000008120};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00039}.
FT REGION 102..112
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
SQ SEQUENCE 191 AA; 21493 MW; 3BC622458DFC063B CRC64;
MIIWVTGTPG VGKTTTGRML AKRLGIGFID LPEFVSANNL YTERLGDGTM VVDPRRLERH
LSRNVKEDTV IAGHITVRVR GHETRCIVLR LNPLQLRKRL EERGYSVEKV AENVEAEFLG
VVYLDAIRVF GKNRVSQIDV TGKEASDVVN RCVDVLEGRD AGDDVEWMSR LDEDILSQLL
RYLSTAKTRG L
//
