ID E0SQE2_IGNAA Unreviewed; 193 AA.
AC E0SQE2;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=Igag_0243 {ECO:0000313|EMBL:ADM27092.1};
OS Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignisphaera.
OX NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM27092.1, ECO:0000313|Proteomes:UP000001304};
RN [1] {ECO:0000313|EMBL:ADM27092.1, ECO:0000313|Proteomes:UP000001304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC {ECO:0000313|Proteomes:UP000001304};
RX PubMed=21304693; DOI=10.4056/sigs.1072907;
RA Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL Stand. Genomic Sci. 3:66-75(2010).
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; CP002098; ADM27092.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SQE2; -.
DR STRING; 583356.Igag_0243; -.
DR KEGG; iag:Igag_0243; -.
DR HOGENOM; CLU_079096_0_0_2; -.
DR BioCyc; IAGG583356:GHAH-255-MONOMER; -.
DR Proteomes; UP000001304; 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:ADM27092.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW Reference proteome {ECO:0000313|Proteomes:UP000001304};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00039, ECO:0000313|EMBL:ADM27092.1}.
FT REGION 31..54
FT /note="NMP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT REGION 107..117
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
SQ SEQUENCE 193 AA; 21914 MW; 1A9529683AE1B270 CRC64;
MKSIGISGTP GTGKSSTAKI LSQYLGIPVI DLSKYVIENN LILFYDSERQ TNVIDEDRVR
HELLKLYNSN GAMIIDSHYA EITPKEILEV VFVIRRDPEE LMNILLKRGW SLNKVIENVE
AELLSICTLN AIDELGEDLV IEINATSRNS EEIALEIIEI LFGEKSAYYG HTIDWLSILP
QEKLLKIIEL LKR
//
