ID A0A256Z815_9CREN Unreviewed; 209 AA.
AC A0A256Z815;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Adenylate kinase {ECO:0000256|ARBA:ARBA00019926, ECO:0000256|HAMAP-Rule:MF_00234};
DE Short=AK {ECO:0000256|HAMAP-Rule:MF_00234};
DE EC=2.7.4.3 {ECO:0000256|ARBA:ARBA00012955, ECO:0000256|HAMAP-Rule:MF_00234};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|ARBA:ARBA00033336, ECO:0000256|HAMAP-Rule:MF_00234};
GN Name=adkA {ECO:0000256|HAMAP-Rule:MF_00234};
GN ORFNames=B6U85_01335 {ECO:0000313|EMBL:OYT48722.1};
OS Desulfurococcales archaeon ex4484_42.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales.
OX NCBI_TaxID=2012520 {ECO:0000313|EMBL:OYT48722.1, ECO:0000313|Proteomes:UP000216823};
RN [1] {ECO:0000313|Proteomes:UP000216823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K.W., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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_00234};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00234}.
CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007088, ECO:0000256|HAMAP-Rule:MF_00234}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYT48722.1}.
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DR EMBL; NJDT01000006; OYT48722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A256Z815; -.
DR Proteomes; UP000216823; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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_00234; Adenylate_kinase_AdkA; 1.
DR InterPro; IPR023477; Adenylate_kinase_AdkA.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13207; AAA_17; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00234};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00234, ECO:0000313|EMBL:OYT48722.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00234}.
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00234"
SQ SEQUENCE 209 AA; 23462 MW; 75CF163C38D965F8 CRC64;
MVSKFNSSLK LIVMVGLPGV GKSTVINLVV KKLKEKGYNV EVINFGDFML KFMVSKGYVK
SRDEIRKLPL TIQQEAQTKS AKEIRRRFEE LSSKSEGIFI GIVDTHALIK TETGLWPGLP
KHVIEELRPH AIIVIEASPK EIVSRQLRDK TRYRADYARE ELITELLNLN RVFAISSAVL
VGASVATVMN KEGKAEEAAE EVVNIIERI
//
