ID   D5LKV6_9ESCH            Unreviewed;       175 AA.
AC   D5LKV6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
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:ADF44269.1};
OS   Escherichia sp. E1492.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=754315 {ECO:0000313|EMBL:ADF44269.1};
RN   [1] {ECO:0000313|EMBL:ADF44269.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=E1492 {ECO:0000313|EMBL:ADF44269.1};
RA   Walk S.T., Alm E.W., Gordon D.M., Ram J.L., Toranzos G.A., Tiedje J.M.,
RA   Whittam T.S.;
RT   "Cryptic Lineages of the Genus Escherichia.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GU937686; ADF44269.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5LKV6; -.
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          112..147
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADF44269.1"
FT   NON_TER         175
FT                   /evidence="ECO:0000313|EMBL:ADF44269.1"
SQ   SEQUENCE   175 AA;  19537 MW;  FE286A1B58FCEAC4 CRC64;
     GKGTQAQFIM EKYGIPQIST GDMLRAAVKS GSELGKQAKD IMDAGKLVTD ELVIALVKER
     IAQEDCRNGF LLDGFPRTIP QADAMKEAGI NVDYVLEFDV PDELIVDRIV GRRVHAPSGR
     VYHVKFNPPK VEGKDDVTGE ELTTRKDDQE ETVRKRLVEY HQMTAPLIGY YSKEA
//