KAD_ENCCU
ID KAD_ENCCU Reviewed; 177 AA.
AC Q8SVC2;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Adenylate kinase;
DE Short=AK;
DE EC=2.7.4.3;
DE AltName: Full=ATP-AMP transphosphorylase;
DE AltName: Full=ATP:AMP phosphotransferase;
DE AltName: Full=Adenylate monophosphate kinase;
GN OrderedLocusNames=ECU06_0650;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GB-M1;
RX PubMed=20003517; DOI=10.1186/1471-2164-10-607;
RA Peyretaillade E., Goncalves O., Terrat S., Dugat-Bony E., Wincker P.,
RA Cornman R.S., Evans J.D., Delbac F., Peyret P.;
RT "Identification of transcriptional signals in Encephalitozoon cuniculi
RT widespread among Microsporidia phylum: support for accurate structural
RT genome annotation.";
RL BMC Genomics 10:607-607(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL
RP STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism.
CC {ECO:0000250|UniProtKB:P69441}.
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:0000250|UniProtKB:P69441};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P69441}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16691553}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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; AL590446; CAD25425.2; -; Genomic_DNA.
DR RefSeq; NP_585821.1; NM_001041443.1.
DR AlphaFoldDB; Q8SVC2; -.
DR SMR; Q8SVC2; -.
DR STRING; 284813.Q8SVC2; -.
DR GeneID; 859245; -.
DR KEGG; ecu:ECU06_0650; -.
DR VEuPathDB; MicrosporidiaDB:ECU06_0650; -.
DR HOGENOM; CLU_032354_1_2_1; -.
DR InParanoid; Q8SVC2; -.
DR OrthoDB; 1004067at2759; -.
DR Proteomes; UP000000819; Chromosome VI.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..177
FT /note="Adenylate kinase"
FT /id="PRO_0000383113"
FT REGION 33..62
FT /note="NMP"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 119..127
FT /note="LID"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 13..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 34
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 39
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 60..62
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 85..88
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 124
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 135
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P69441"
SQ SEQUENCE 177 AA; 19963 MW; 453AB213AC355B56 CRC64;
MKYSRIVVMG PPGCGKGTQS SLISEKYEIP HVSSGDIIRE EMKKSSKEAT VIREMVNSGR
LAPDEIVNEL VLKKIRSMSK YILDGYPRRI EQAGMLGDDV DLVIFIDVDE DTCISRICGR
NEGRDDDDEE VGRKRCMVYN KETAPVLEFY KRHGKLLTIN GCASPGTVFE EIRRSIE
