ID A0A2A2HBA6_9EURY Unreviewed; 185 AA.
AC A0A2A2HBA6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:PWL07836.1};
GN Synonyms=adkA {ECO:0000256|HAMAP-Rule:MF_00234};
GN ORFNames=ASJ82_04250 {ECO:0000313|EMBL:PAV06648.1}, MSCUN_13680
GN {ECO:0000313|EMBL:PWL07836.1};
OS Methanosphaera cuniculi.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=1077256 {ECO:0000313|EMBL:PAV06648.1, ECO:0000313|Proteomes:UP000217528};
RN [1] {ECO:0000313|EMBL:PWL07836.1, ECO:0000313|Proteomes:UP000246004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4103 {ECO:0000313|EMBL:PWL07836.1,
RC ECO:0000313|Proteomes:UP000246004};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanosphaera cuniculi DSM 4103.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PAV06648.1, ECO:0000313|Proteomes:UP000217528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1R-7 {ECO:0000313|EMBL:PAV06648.1,
RC ECO:0000313|Proteomes:UP000217528};
RX PubMed=28826405; DOI=10.1186/s12864-017-4036-4;
RA Gilmore S.P., Henske J.K., Sexton J.A., Solomon K.V., Seppala S., Yoo J.I.,
RA Huyett L.M., Pressman A., Cogan J.Z., Kivenson V., Peng X., Tan Y.,
RA Valentine D.L., O'Malley M.A.;
RT "Genomic analysis of methanogenic archaea reveals a shift towards energy
RT conservation.";
RL BMC Genomics 18:639-639(2017).
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:PAV06648.1}.
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DR EMBL; LMVN01000027; PAV06648.1; -; Genomic_DNA.
DR EMBL; LWMS01000044; PWL07836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2HBA6; -.
DR OrthoDB; 26198at2157; -.
DR Proteomes; UP000217528; Unassembled WGS sequence.
DR Proteomes; UP000246004; 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:PAV06648.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00234};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00234, ECO:0000313|EMBL:PAV06648.1}.
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00234"
SQ SEQUENCE 185 AA; 20799 MW; C9B2C7CB7F27A1BC CRC64;
MNIVVLAGIP GTGSTTVLNK VLEEVDYVNI NYGNIMFDIA SEKGLVESRD DMRKLDPEIQ
KDVQKKAAER IHEMAQDDDV IIDTHCTIKT PKGFLPGLPI WVLEELQPTQ FILIEAEPSE
IMFRRLNDDT RVRDIEYTDE IDLHQQMSRA TAMSYAVQTG CTVAMVQNND DGLEDAVSEI
VDILS
//
