ID F1R4S7_DANRE Unreviewed; 225 AA.
AC F1R4S7; A0A8M1PGD5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=GTP:AMP phosphotransferase AK3, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03169};
DE EC=2.7.4.10 {ECO:0000256|HAMAP-Rule:MF_03169};
DE AltName: Full=Adenylate kinase 3 {ECO:0000256|HAMAP-Rule:MF_03169};
DE Short=AK 3 {ECO:0000256|HAMAP-Rule:MF_03169};
GN Name=ak3 {ECO:0000313|Ensembl:ENSDARP00000116187,
GN ECO:0000313|RefSeq:NP_998295.2,
GN ECO:0000313|ZFIN:ZDB-GENE-040426-2142};
GN Synonyms=AK3 {ECO:0000256|HAMAP-Rule:MF_03169}, ak3l1
GN {ECO:0000313|RefSeq:NP_998295.2}, id:ibd3034
GN {ECO:0000313|RefSeq:NP_998295.2}, sb:cb845
GN {ECO:0000313|RefSeq:NP_998295.2}, wu:fa02c11
GN {ECO:0000313|RefSeq:NP_998295.2}, wu:fc20h08
GN {ECO:0000313|RefSeq:NP_998295.2}, zgc:64135
GN {ECO:0000313|RefSeq:NP_998295.2};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000116187};
RN [1] {ECO:0000313|RefSeq:NP_998295.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_998295.2};
RX PubMed=22139419;
RA Gieger C., Radhakrishnan A., Cvejic A., Tang W., Porcu E., Pistis G.,
RA Serbanovic-Canic J., Elling U., Goodall A.H., Labrune Y., Lopez L.M.,
RA Magi R., Meacham S., Okada Y., Pirastu N., Sorice R., Teumer A., Voss K.,
RA Zhang W., Ramirez-Solis R., Bis J.C., Ellinghaus D., Gogele M.,
RA Hottenga J.J., Langenberg C., Kovacs P., O'Reilly P.F., Shin S.Y., Esko T.,
RA Hartiala J., Kanoni S., Murgia F., Parsa A., Stephens J., van der Harst P.,
RA Ellen van der Schoot C., Allayee H., Attwood A., Balkau B., Bastardot F.,
RA Basu S., Baumeister S.E., Biino G., Bomba L., Bonnefond A., Cambien F.,
RA Chambers J.C., Cucca F., D'Adamo P., Davies G., de Boer R.A., de Geus E.J.,
RA Doring A., Elliott P., Erdmann J., Evans D.M., Falchi M., Feng W.,
RA Folsom A.R., Frazer I.H., Gibson Q.D., Glazer N.L., Hammond C.,
RA Hartikainen A.L., Heckbert S.R., Hengstenberg C., Hersch M., Illig T.,
RA Loos R.J., Jolley J., Khaw K.T., Kuhnel B., Kyrtsonis M.C., Lagou V.,
RA Lloyd-Jones H., Lumley T., Mangino M., Maschio A., Mateo Leach I.,
RA McKnight B., Memari Y., Mitchell B.D., Montgomery G.W., Nakamura Y.,
RA Nauck M., Navis G., Nothlings U., Nolte I.M., Porteous D.J., Pouta A.,
RA Pramstaller P.P., Pullat J., Ring S.M., Rotter J.I., Ruggiero D.,
RA Ruokonen A., Sala C., Samani N.J., Sambrook J., Schlessinger D.,
RA Schreiber S., Schunkert H., Scott J., Smith N.L., Snieder H., Starr J.M.,
RA Stumvoll M., Takahashi A., Tang W.H., Taylor K., Tenesa A., Lay Thein S.,
RA Tonjes A., Uda M., Ulivi S., van Veldhuisen D.J., Visscher P.M., Volker U.,
RA Wichmann H.E., Wiggins K.L., Willemsen G., Yang T.P., Hua Zhao J.,
RA Zitting P., Bradley J.R., Dedoussis G.V., Gasparini P., Hazen S.L.,
RA Metspalu A., Pirastu M., Shuldiner A.R., Joost van Pelt L., Zwaginga J.J.,
RA Boomsma D.I., Deary I.J., Franke A., Froguel P., Ganesh S.K.,
RA Jarvelin M.R., Martin N.G., Meisinger C., Psaty B.M., Spector T.D.,
RA Wareham N.J., Akkerman J.W., Ciullo M., Deloukas P., Greinacher A.,
RA Jupe S., Kamatani N., Khadake J., Kooner J.S., Penninger J., Prokopenko I.,
RA Stemple D., Toniolo D., Wernisch L., Sanna S., Hicks A.A., Rendon A.,
RA Ferreira M.A., Ouwehand W.H., Soranzo N.;
RT "New gene functions in megakaryopoiesis and platelet formation.";
RL Nature 480:201-208(2011).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000116187}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116187};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000116187, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116187};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000313|RefSeq:NP_998295.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_998295.2};
RX PubMed=25975375;
RA Long Y., Yan J., Song G., Li X., Li X., Li Q., Cui Z.;
RT "Transcriptional events co-regulated by hypoxia and cold stresses in
RT Zebrafish larvae.";
RL BMC Genomics 16:385-385(2015).
RN [5] {ECO:0000313|RefSeq:NP_998295.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_998295.2};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [6] {ECO:0000313|RefSeq:NP_998295.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_998295.2};
RX PubMed=27473876;
RA Xiaohuan H., Yang Z., Linyan L., Zhenhua F., Linyan Z., Zhijian W.,
RA Ling W., Deshou W., Jing W.;
RT "Characterization of the POU5F1 Homologue in Nile Tilapia: From Expression
RT Pattern to Biological Activity.";
RL Stem Cells Dev. 25:1386-1395(2016).
RN [7] {ECO:0000313|RefSeq:NP_998295.2}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_998295.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved in maintaining the homeostasis of cellular
CC nucleotides by catalyzing the interconversion of nucleoside phosphates.
CC Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase
CC activities. {ECO:0000256|HAMAP-Rule:MF_03169}.
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|HAMAP-Rule:MF_03169};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03169}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|HAMAP-Rule:MF_03169}.
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 GTP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent GTP
CC hydrolysis. {ECO:0000256|HAMAP-Rule:MF_03169}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03169}.
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DR EMBL; CT027818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_998295.2; NM_213130.2.
DR STRING; 7955.ENSDARP00000116187; -.
DR PaxDb; 7955-ENSDARP00000116187; -.
DR Ensembl; ENSDART00000132995; ENSDARP00000116187; ENSDARG00000058226.
DR Ensembl; ENSDART00000132995.2; ENSDARP00000116187.1; ENSDARG00000058226.6.
DR GeneID; 406404; -.
DR KEGG; dre:406404; -.
DR AGR; ZFIN:ZDB-GENE-040426-2142; -.
DR CTD; 50808; -.
DR ZFIN; ZDB-GENE-040426-2142; ak3.
DR eggNOG; KOG3078; Eukaryota.
DR HOGENOM; CLU_032354_1_1_1; -.
DR OMA; TIAHFST; -.
DR OrthoDB; 167111at2759; -.
DR PhylomeDB; F1R4S7; -.
DR TreeFam; TF312916; -.
DR Reactome; R-DRE-983231; Factors involved in megakaryocyte development and platelet production.
DR Proteomes; UP000000437; Chromosome 10.
DR Bgee; ENSDARG00000058226; Expressed in gastrula and 31 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046899; F:nucleoside triphosphate adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central.
DR GO; GO:0046039; P:GTP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0046041; P:ITP metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0061515; P:myeloid cell development; IMP:ZFIN.
DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central.
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_03169; Adenylate_kinase_AK3; 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; IPR036193; ADK_active_lid_dom_sf.
DR InterPro; IPR028586; AK3/Ak4_mitochondrial.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01351; adk; 1.
DR PANTHER; PTHR23359:SF68; GTP:AMP PHOSPHOTRANSFERASE AK3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 1: Evidence at protein level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03169};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03169};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03169};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03169};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1R4S7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03169}.
FT DOMAIN 127..162
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
FT REGION 36..65
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT REGION 126..163
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT REGION 145..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 37
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 42
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 63..65
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 90..93
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 97
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 136..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 160
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 171
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
SQ SEQUENCE 225 AA; 25037 MW; F1F7DEE2F8F2685C CRC64;
MGLQSVFRAV IMGAPGSGKG TVSSRIAQSF GLKHLSSGDM LRANIEAKTD LGLLMKSCID
QGQLVPDDVI SRLILSSLRG LEKTSWLLDG FPRTVAQAEA LDCVYDVDSV INLDVPFQTI
RERLTSRWVH LPSGRVYNID FNPPKKPGLD DVTGEPLVQR DDDSPETVSR RLKDYERQTQ
PVLEYYRSKG VLETFSGTET NKIWPHVHTF LSRKIPGHKQ AMGKA
//
