ID A0A0G1MDK6_9BACT Unreviewed; 356 AA.
AC A0A0G1MDK6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Adenylate kinase {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=UX07_C0003G0060 {ECO:0000313|EMBL:KKU06329.1};
OS Parcubacteria group bacterium GW2011_GWA2_45_30.
OC Bacteria.
OX NCBI_TaxID=1618834 {ECO:0000313|EMBL:KKU06329.1, ECO:0000313|Proteomes:UP000033829};
RN [1] {ECO:0000313|EMBL:KKU06329.1, ECO:0000313|Proteomes:UP000033829}
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family.
CC {ECO:0000256|ARBA:ARBA00007220}.
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:KKU06329.1}.
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DR EMBL; LCKU01000003; KKU06329.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1MDK6; -.
DR Proteomes; UP000033829; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050145; F:nucleoside monophosphate kinase activity; IEA:UniProt.
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; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR Pfam; PF13207; AAA_17; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KKU06329.1"
SQ SEQUENCE 356 AA; 40799 MW; 274FBD543044EB07 CRC64;
FSFPIFKTKV EGVGQKFKFE DPAERRRYFE LKAGAEIEKL REYLQENTFV GFLLGPKNSG
KGTYSKLFME AVGEERVAHI SVGDIVRSVH KDLEKASSHK ELVDFLKRRY RGFITIEKAL
EVILGRDIKT LLPTEVILAL VEREIDKIGR KAVFIDGFPR NLDQVSYSLY FRTLVGYRDD
PDFFVFIDVP EAVIDERMKY RVVCPECQSP RNTKLLRTKD VGYDASHKKF YLLCDNPNCS
GYGKIRMSPK EGDELGIEAI RNRIEADGEV MKMLLNLQGV PKVFLRNSVP VNQARENIDD
YEITPAFRYE LEKNGAVRVI EKPWTIKDDE GNDSYSLMPP PVALALIKQI VQVLGL
//
