ID K7FSU9_PELSI Unreviewed; 195 AA.
AC K7FSU9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Adenylate kinase isoenzyme 1 {ECO:0000256|HAMAP-Rule:MF_03171};
DE Short=AK 1 {ECO:0000256|HAMAP-Rule:MF_03171};
DE EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03171};
DE EC=2.7.4.6 {ECO:0000256|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP-AMP transphosphorylase 1 {ECO:0000256|HAMAP-Rule:MF_03171};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_03171};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03171};
DE AltName: Full=Myokinase {ECO:0000256|HAMAP-Rule:MF_03171};
GN Name=AK1 {ECO:0000256|HAMAP-Rule:MF_03171,
GN ECO:0000313|Ensembl:ENSPSIP00000011109.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000011109.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000011109.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Also displays broad nucleoside diphosphate
CC kinase activity. Plays an important role in cellular energy homeostasis
CC and in adenine nucleotide metabolism. {ECO:0000256|HAMAP-
CC Rule:MF_03171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + thiamine diphosphate = AMP + thiamine triphosphate;
CC Xref=Rhea:RHEA:69180, ChEBI:CHEBI:58937, ChEBI:CHEBI:58938,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00034400};
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|HAMAP-Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GDP = ADP + GTP; Xref=Rhea:RHEA:27686,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00034442};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + UDP = ADP + UTP; Xref=Rhea:RHEA:25098,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00034451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dGDP = ADP + dGTP; Xref=Rhea:RHEA:27690,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00034407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dTDP = ADP + dTTP; Xref=Rhea:RHEA:27682,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|ARBA:ARBA00034432};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-
CC diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930,
CC ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=2.7.4.10; Evidence={ECO:0000256|ARBA:ARBA00034410};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC Rule:MF_03171}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_03171}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000256|HAMAP-Rule:MF_03171}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03171}.
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DR EMBL; AGCU01057997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01057998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01057999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01058000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01058001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01058002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01058003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01058004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01058005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01058006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006119051.2; XM_006118989.2.
DR RefSeq; XP_006119055.1; XM_006118993.2.
DR RefSeq; XP_006119056.1; XM_006118994.2.
DR RefSeq; XP_006119057.1; XM_006118995.2.
DR AlphaFoldDB; K7FSU9; -.
DR Ensembl; ENSPSIT00000011165.1; ENSPSIP00000011109.1; ENSPSIG00000009976.1.
DR GeneID; 102455130; -.
DR CTD; 203; -.
DR GeneTree; ENSGT00940000158325; -.
DR HOGENOM; CLU_032354_0_3_1; -.
DR OrthoDB; 1330004at2759; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IEA:RHEA.
DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IEA:InterPro.
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 HAMAP; MF_03171; Adenylate_kinase_AK1; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR028582; AK1.
DR InterPro; IPR006267; AK1/5.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01360; aden_kin_iso1; 1.
DR PANTHER; PTHR23359:SF59; ADENYLATE KINASE ISOENZYME 1; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 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|HAMAP-Rule:MF_03171};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03171};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03171};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03171};
KW Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03171}.
FT REGION 39..68
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT REGION 132..142
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 19..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 40
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 45
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 66..68
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 95..98
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 102
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 139
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 150
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03171"
SQ SEQUENCE 195 AA; 21503 MW; CC553212DBEAA7A5 CRC64;
MATEKLKNSK IIFVVGGPGS GKGTQCEKIV QKYGYTHLST GDLLRAEVSS GSERGKKLSA
IMEKGELVPL DTVLDMLRDA MVAKADISKG FLIDGYPREV KQGAEFEKKI APPTLLLYVD
AGKDTMVKRL LKRGETSGRV DDNEETIKKR LDTYYKATEP VIAFYEKRGI VRKLSAEGSV
DDVFVQVCTH LDALK
//
