ID B1L5L8_KORCO Unreviewed; 183 AA.
AC B1L5L8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
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 OrderedLocusNames=Kcr_1001 {ECO:0000313|EMBL:ACB07747.1};
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Korarchaeum.
OX NCBI_TaxID=374847 {ECO:0000313|EMBL:ACB07747.1, ECO:0000313|Proteomes:UP000001686};
RN [1] {ECO:0000313|EMBL:ACB07747.1, ECO:0000313|Proteomes:UP000001686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8 {ECO:0000313|Proteomes:UP000001686};
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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; CP000968; ACB07747.1; -; Genomic_DNA.
DR AlphaFoldDB; B1L5L8; -.
DR STRING; 374847.Kcr_1001; -.
DR EnsemblBacteria; ACB07747; ACB07747; Kcr_1001.
DR KEGG; kcr:Kcr_1001; -.
DR eggNOG; arCOG01038; Archaea.
DR HOGENOM; CLU_079096_0_0_2; -.
DR InParanoid; B1L5L8; -.
DR OrthoDB; 8730at2157; -.
DR PhylomeDB; B1L5L8; -.
DR Proteomes; UP000001686; 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, ECO:0000313|EMBL:ACB07747.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW Reference proteome {ECO:0000313|Proteomes:UP000001686};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00039}.
FT REGION 37..60
FT /note="NMP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT REGION 110..120
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
SQ SEQUENCE 183 AA; 20536 MW; 5CE5BC77F2552DDF CRC64;
MGNINISGLI VVIGTPGSGK TRVAKLIAES LGCRYLNVGE LSLEKGYVLG RDEERGSYII
DEERVREELS RIEDTIVVET ISPYAIPQDK VSLVIVVRCR PSILLERLRE RGYSKSKIRE
NLEYEAIDGP LFDAMQIADV DKIVEIDGCE GNDEEIYDAL RGIKKGVGRF NWSQDFLSIL
EEI
//
