ID A0A0G1VI55_9BACT Unreviewed; 196 AA.
AC A0A0G1VI55;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Adenylate kinase {ECO:0000256|RuleBase:RU003331};
DE EC=2.7.4.3 {ECO:0000256|RuleBase:RU003331};
GN ORFNames=UX94_C0018G0008 {ECO:0000313|EMBL:KKU69730.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_21.
OC Bacteria.
OX NCBI_TaxID=1618843 {ECO:0000313|EMBL:KKU69730.1, ECO:0000313|Proteomes:UP000034472};
RN [1] {ECO:0000313|EMBL:KKU69730.1, ECO:0000313|Proteomes:UP000034472}
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|ARBA:ARBA00000582,
CC ECO:0000256|RuleBase:RU003331};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245,
CC ECO:0000256|RuleBase:RU003331}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC 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:KKU69730.1}.
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DR EMBL; LCOC01000018; KKU69730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1VI55; -.
DR STRING; 1618843.UX94_C0018G0008; -.
DR PATRIC; fig|1618843.3.peg.565; -.
DR Proteomes; UP000034472; 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:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP 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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003331};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 196 AA; 22871 MW; 9281F93E0E7F609D CRC64;
MQNHAFIFYG ISGSGKGTQA KLLIEYLQKN DPSREVIYIE TGARIRSFIA DTSGHTRDMV
KNILDKGGLL PEFIPIWLWS NLLVTKFTGK EHLVLDGVSR WPHESPIVDA ALKFYGFEEL
NVILINVSRE WARSRLKERK RYDDDEAEIN RRFDWYEKNT KPAVDYFRDK PSVSIIEING
EQEIEAVHRE IIRKVF
//