(data stored in ACNUC7421 zone)

SWISSPROT: A2Q8K9_ASPNC

ID   A2Q8K9_ASPNC            Unreviewed;       234 AA.
AC   A2Q8K9;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=GTP:AMP phosphotransferase, 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=ADK2 {ECO:0000256|HAMAP-Rule:MF_03169};
GN   ORFNames=An01g04710 {ECO:0000313|EMBL:CAK37006.1};
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=425011 {ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK37006.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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 {ECO:0000256|HAMAP-
CC       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; AM269963; CAK37006.1; -; Genomic_DNA.
DR   RefSeq; XP_001388898.1; XM_001388861.2.
DR   PaxDb; A2Q8K9; -.
DR   EnsemblFungi; CAK37006; CAK37006; An01g04710.
DR   GeneID; 4978474; -.
DR   KEGG; ang:ANI_1_608014; -.
DR   HOGENOM; HOG000238772; -.
DR   KO; K00939; -.
DR   Proteomes; UP000006706; Chromosome 2R.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:InterPro.
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; IEA:UniProtKB-UniRule.
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:0046039; P:GTP metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046041; P:ITP metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01428; ADK; 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; IPR028586; AK3/Ak4_mitochondrial.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; PTHR23359; 1.
DR   Pfam; PF05191; ADK_lid; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01351; adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A2Q8K9.
DR   SWISS-2DPAGE; A2Q8K9.
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_03169};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_03169, ECO:0000256|RuleBase:RU003330};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03169};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03169};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03169,
KW   ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:CAK37006.1}.
FT   DOMAIN          145..180
FT                   /note="ADK_lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
FT   NP_BIND         21..26
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   NP_BIND         69..71
FT                   /note="AMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   NP_BIND         108..111
FT                   /note="AMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   NP_BIND         154..155
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   REGION          42..71
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   REGION          144..181
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         43
FT                   /note="AMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         48
FT                   /note="AMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         115
FT                   /note="AMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         145
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         178
FT                   /note="AMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         189
FT                   /note="AMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         218
FT                   /note="GTP; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
SQ   SEQUENCE   234 AA;  26003 MW;  02BAAA9A56ED459C CRC64;
     MTATIRQLRK AARIILIGAP GVGKGTQTER LLTRYPELAS ISSGDLLREN VRRKTPLGLQ
     AEATMQSGNL VPDSMILDLI SSEFKSRGWL SSAPTSSILP SASFILDGFP RTATQASSLE
     TIVPVNFVVH LVTPPSVILS RIASRWVHEP SGRVYNTDFN APKVPGKDDV TGEPLTQRED
     DSIDTWKQRL HKFEETSKAL LEHYQRKGCL WRVEGDTSDE ISPKLFAEIE RQFC
//

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