ID G7VFH1_9CREN Unreviewed; 196 AA.
AC G7VFH1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=P186_1558 {ECO:0000313|EMBL:AET32977.1};
OS Pyrobaculum ferrireducens.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET32977.1, ECO:0000313|Proteomes:UP000005867};
RN [1] {ECO:0000313|EMBL:AET32977.1, ECO:0000313|Proteomes:UP000005867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1860 {ECO:0000313|EMBL:AET32977.1,
RC ECO:0000313|Proteomes:UP000005867};
RX PubMed=22247528; DOI=10.1128/JB.06465-11;
RA Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT pyrobaculum able to grow with various electron acceptors.";
RL J. Bacteriol. 194:727-728(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.
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}.
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DR EMBL; CP003098; AET32977.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VFH1; -.
DR STRING; 1104324.P186_1558; -.
DR KEGG; pyr:P186_1558; -.
DR eggNOG; arCOG01038; Archaea.
DR HOGENOM; CLU_079096_0_0_2; -.
DR OrthoDB; 8730at2157; -.
DR BioCyc; PSP1104324:GJSN-1530-MONOMER; -.
DR Proteomes; UP000005867; 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:AET32977.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00039};
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 109..119
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 17..22
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 196 AA; 21856 MW; F93887AE02CBF54A CRC64;
MTCAAPRPKA LITGTPGVGK TTHCRKLAEV LSTRCVTVGE VLANTPYVVY IPELATYEIS
DLARAAEVVC RAVAPGDVVD THVVELSPDP EAVVVLRKAP DVLFRELVDR GWPLKKVLDN
VWAEMLDVVY VKARERWPWA VQIDVTKRSR DETFEAIRRC VVGGGCLDEA VDWLSYAERS
GFLEFIERLS RWGRSS
//