ID A0A162FK61_9EURY Unreviewed; 186 AA.
AC A0A162FK61;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=cmk_2 {ECO:0000313|EMBL:KZX11220.1};
GN Synonyms=adkA {ECO:0000256|HAMAP-Rule:MF_00234};
GN ORFNames=MBCUR_14920 {ECO:0000313|EMBL:KZX11220.1};
OS Methanobrevibacter curvatus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=49547 {ECO:0000313|EMBL:KZX11220.1, ECO:0000313|Proteomes:UP000077245};
RN [1] {ECO:0000313|EMBL:KZX11220.1, ECO:0000313|Proteomes:UP000077245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11111 {ECO:0000313|EMBL:KZX11220.1,
RC ECO:0000313|Proteomes:UP000077245};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter curvatus DSM 11111.";
RL Submitted (APR-2016) 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:KZX11220.1}.
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DR EMBL; LWMV01000191; KZX11220.1; -; Genomic_DNA.
DR RefSeq; WP_067092139.1; NZ_LWMV01000191.1.
DR AlphaFoldDB; A0A162FK61; -.
DR STRING; 49547.MBCUR_14920; -.
DR PATRIC; fig|49547.3.peg.1594; -.
DR OrthoDB; 26198at2157; -.
DR Proteomes; UP000077245; 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:KZX11220.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW Reference proteome {ECO:0000313|Proteomes:UP000077245};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00234, ECO:0000313|EMBL:KZX11220.1}.
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00234"
SQ SEQUENCE 186 AA; 20590 MW; D3BA223A26F593AD CRC64;
MKLIVLTGIP GSGSTTVLSK ALEEVDFLHL NYGDIMIELS REEGLAEDRD DLRKLSPEIQ
KDIQKIAAAR IKEQSLSQNV IVDTHCTIST SAGFLPGLPS WVLEELNPDT FIIVEADPDE
IILRRISDET RNRDSQRASD INLHQEINRA TAMAYATLTG ATVKILENHN GELDKVVPML
VETLSV
//
