KAD6_THEVO
ID KAD6_THEVO Reviewed; 153 AA.
AC Q97B38;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Putative adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00039};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00039};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00039};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00039};
GN OrderedLocusNames=TV0621; ORFNames=TVG0613288;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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:0000255|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:0000255|HAMAP-Rule:MF_00039};
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00039}.
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DR EMBL; BA000011; BAB59763.1; -; Genomic_DNA.
DR RefSeq; WP_010916880.1; NC_002689.2.
DR AlphaFoldDB; Q97B38; -.
DR SMR; Q97B38; -.
DR STRING; 273116.14324837; -.
DR EnsemblBacteria; BAB59763; BAB59763; BAB59763.
DR GeneID; 1441728; -.
DR KEGG; tvo:TVG0613288; -.
DR eggNOG; arCOG01038; Archaea.
DR HOGENOM; CLU_079096_0_1_2; -.
DR OMA; VWEIDTT; -.
DR OrthoDB; 110798at2157; -.
DR PhylomeDB; Q97B38; -.
DR Proteomes; UP000001017; 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; -; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595; PTHR12595; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..153
FT /note="Putative adenylate kinase"
FT /id="PRO_0000153918"
FT REGION 31..47
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT REGION 94..104
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
SQ SEQUENCE 153 AA; 17439 MW; 8AF616DBD4758532 CRC64;
MGKIACITGP PGAGKSTVCS KLREYGYNCK EGNELAKEYG CLFDEEVDVE CLEEKLAEDR
FDGIICSHYS HLLGCSTVFI LEADLNDLID RMRARGYSEE KIQENIETQM SSIFYYESLE
RLPANRIFTL YNGNIDETAK RIISIIERSR NNK
