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Database: UniProt
Entry: A0A0G0USC7_9BACT
LinkDB: A0A0G0USC7_9BACT
Original site: A0A0G0USC7_9BACT 
ID   A0A0G0USC7_9BACT        Unreviewed;       186 AA.
AC   A0A0G0USC7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=Adenylate kinase {ECO:0000256|RuleBase:RU003331};
DE            EC=2.7.4.3 {ECO:0000256|RuleBase:RU003331};
GN   ORFNames=UT90_C0012G0007 {ECO:0000313|EMBL:KKR53202.1};
OS   Parcubacteria group bacterium GW2011_GWA1_40_21.
OC   Bacteria.
OX   NCBI_TaxID=1618784 {ECO:0000313|EMBL:KKR53202.1, ECO:0000313|Proteomes:UP000034712};
RN   [1] {ECO:0000313|EMBL:KKR53202.1, ECO:0000313|Proteomes:UP000034712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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|RuleBase:RU003331};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|RuleBase:RU003331}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003331}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC       {ECO:0000256|RuleBase:RU003330}.
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:KKR53202.1}.
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DR   EMBL; LBYO01000012; KKR53202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0USC7; -.
DR   STRING; 1618784.UT90_C0012G0007; -.
DR   Proteomes; UP000034712; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359:SF148; ADENYLATE KINASE 9; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU003331};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003330};
KW   Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003331};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
SQ   SEQUENCE   186 AA;  21858 MW;  586B753D8BC1732D CRC64;
     MSGCGKGTQA KLLGEYLKKV DPKREVFFLE TGAEFRRFIQ GEGYTQRLSK KIYDEGGSQP
     EFLSVYMWSH LIAENFKEDE HLIVDGTPRR FHEAGALDSA FDFYSREKPY FIFLNIGKEW
     ATERLTGRGR IDDNHDDIKA RLNWYETDVV PAINFYRNNP KYNFLEINGE QTIEKVHQDI
     WDKLPF
//
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