ID G2GXY6_9ENTR Unreviewed; 161 AA.
AC G2GXY6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Adenylate kinase {ECO:0000256|RuleBase:RU003331};
DE EC=2.7.4.3 {ECO:0000256|RuleBase:RU003331};
DE Flags: Fragment;
GN ORFNames=Rin_00006320 {ECO:0000313|EMBL:EGY29412.1};
OS Candidatus Regiella insecticola 5.15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX NCBI_TaxID=1005043 {ECO:0000313|EMBL:EGY29412.1, ECO:0000313|Proteomes:UP000004116};
RN [1] {ECO:0000313|EMBL:EGY29412.1, ECO:0000313|Proteomes:UP000004116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R5.15 {ECO:0000313|Proteomes:UP000004116};
RX PubMed=21948522; DOI=10.1101/gr.125351.111;
RA Hansen A.K., Vorburger C., Moran N.A.;
RT "Genomic basis of endosymbiont-conferred protection against an insect
RT parasitoid.";
RL Genome Res. 22:106-114(2012).
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 -!- 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:EGY29412.1}.
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DR EMBL; AGCA01000134; EGY29412.1; -; Genomic_DNA.
DR RefSeq; WP_006706329.1; NZ_AGCA01000134.1.
DR AlphaFoldDB; G2GXY6; -.
DR PATRIC; fig|1005043.3.peg.593; -.
DR OrthoDB; 9805030at2; -.
DR Proteomes; UP000004116; 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 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; 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 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|RuleBase:RU003331};
KW Reference proteome {ECO:0000313|Proteomes:UP000004116};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003330}.
FT DOMAIN 70..105
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGY29412.1"
SQ SEQUENCE 161 AA; 18250 MW; AE679D231F2775B1 CRC64;
EEGKLVPDEL AIALVKQRIS QDDCRGGFLL DGFPRTLSQA DAIIEAGINI DYVLEFDVPD
QVIIERIAGR RIHAPSGRIY HLRFNPPKIE NKDDITGEPL TLRKDDQEAT VRQRLVEYHQ
QTEPLLSYYR KQAAAGNTHY FKLDGTHKVG EIRDELTAIL G
//
