ID C8Z2W5_ECOLX Unreviewed; 145 AA.
AC C8Z2W5;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Adenylate kinase {ECO:0000256|RuleBase:RU003331};
DE EC=2.7.4.3 {ECO:0000256|RuleBase:RU003331};
DE Flags: Fragment;
GN Name=adk {ECO:0000313|EMBL:CAX62453.1};
OS Escherichia coli O157:NM.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=626528 {ECO:0000313|EMBL:CAX62453.1};
RN [1] {ECO:0000313|EMBL:CAX62453.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=318 {ECO:0000313|EMBL:CAX62453.1}, 319
RC {ECO:0000313|EMBL:CAX62454.1}, 320 {ECO:0000313|EMBL:CAX62455.1}, and
RC B47 {ECO:0000313|EMBL:CAX62474.1};
RA Toth I., Schmidt H., Kardos G., Lancz Z., Creuzburg K., Damjanova I.,
RA Paszti J., Beutin L., Nagy B.;
RT "Virulence genes and molecular typing of different groups of Escherichia
RT coli O157 strains in cattle.";
RL Appl. Environ. Microbiol. 75:6282-6291(2009).
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|ARBA:ARBA00007220, ECO:0000256|RuleBase:RU003330}.
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DR EMBL; FN257313; CAX62453.1; -; Genomic_DNA.
DR EMBL; FN257314; CAX62454.1; -; Genomic_DNA.
DR EMBL; FN257315; CAX62455.1; -; Genomic_DNA.
DR EMBL; FN257334; CAX62474.1; -; Genomic_DNA.
DR AlphaFoldDB; C8Z2W5; -.
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 CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR PANTHER; PTHR23359:SF206; UMP-CMP KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
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, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003331};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT DOMAIN 89..124
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAX62453.1"
FT NON_TER 145
FT /evidence="ECO:0000313|EMBL:CAX62453.1"
SQ SEQUENCE 145 AA; 16256 MW; 1B429498D1D9D7C1 CRC64;
LRAAVKSGSE LGKQAKDIMD AGKLVTDELV IALVKERIAQ EDCRNGFLLD GFPRTIPQAD
AMKEAGINVD YVLEFDVPDE LIVDRIVGRR VHAPSGRVYH VKFNPPKVEG KDDVTGEELT
TRKDDQEETV RKRLVEYHQM TAPLI
//
