ID A0A1C8ZRX8_9CREN Unreviewed; 187 AA.
AC A0A1C8ZRX8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=BFU36_03505 {ECO:0000313|EMBL:AOL15943.1};
OS Sulfolobus sp. A20.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1891280 {ECO:0000313|EMBL:AOL15943.1, ECO:0000313|Proteomes:UP000094286};
RN [1] {ECO:0000313|Proteomes:UP000094286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A20 {ECO:0000313|Proteomes:UP000094286};
RA Dai X.;
RT "Genome sequencing of Sulfolobus sp. A20 from Costa Rica and comparative
RT analyses of central carbon, nitrogen and sulfur metabolism in various
RT Sulfolobus strains.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017006; AOL15943.1; -; Genomic_DNA.
DR RefSeq; WP_069282294.1; NZ_CP017006.1.
DR AlphaFoldDB; A0A1C8ZRX8; -.
DR STRING; 1891280.BFU36_03505; -.
DR GeneID; 28694894; -.
DR KEGG; sula:BFU36_03505; -.
DR OrthoDB; 8730at2157; -.
DR Proteomes; UP000094286; 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:AOL15943.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00039};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00039}.
FT REGION 30..53
FT /note="NMP"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT REGION 104..114
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00039"
SQ SEQUENCE 187 AA; 21660 MW; 66C810A7A3F815D6 CRC64;
MIMLITGTPG VGKSLVSSKL REIFKCEYLN VSRFVVERKL YTEFDEISQS YVIDEEKVKE
ELRKFLEKQT NVIIETIYPS LIPKADLVVV LRRNPLKLYR ELKDRGWSEL KIAENVEAEI
LGVTAEEAKQ NFENVCEIDT TNNNVEQIVN KIINKVCDRD VDWLNNSEVQ DLLINLDNII
SSHENNI
//