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Database: UniProt
Entry: L8GAD6_PSED2
LinkDB: L8GAD6_PSED2
Original site: L8GAD6_PSED2 
ID   L8GAD6_PSED2            Unreviewed;       266 AA.
AC   L8GAD6;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=GMDG_04344 {ECO:0000313|EMBL:ELR09864.1};
OS   Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS   white-nose syndrome fungus) (Geomyces destructans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR09864.1, ECO:0000313|Proteomes:UP000011064};
RN   [1] {ECO:0000313|Proteomes:UP000011064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Geomyces destructans 20631-21.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03169}.
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DR   EMBL; GL573245; ELR09864.1; -; Genomic_DNA.
DR   RefSeq; XP_012742764.1; XM_012887310.1.
DR   AlphaFoldDB; L8GAD6; -.
DR   STRING; 658429.L8GAD6; -.
DR   VEuPathDB; FungiDB:GMDG_04344; -.
DR   HOGENOM; CLU_032354_1_1_1; -.
DR   InParanoid; L8GAD6; -.
DR   OrthoDB; 167111at2759; -.
DR   Proteomes; UP000011064; Unassembled WGS sequence.
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   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; 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   PANTHER; PTHR23359:SF242; GTP:AMP PHOSPHOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF00406; ADK; 2.
DR   Pfam; PF05191; ADK_lid; 1.
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   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|HAMAP-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}; Reference proteome {ECO:0000313|Proteomes:UP000011064};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03169}.
FT   DOMAIN          174..209
FT                   /note="Adenylate kinase active site lid"
FT                   /evidence="ECO:0000259|Pfam:PF05191"
FT   REGION          33..62
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   REGION          173..210
FT                   /note="LID"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         34
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         39
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         60..62
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         137..140
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         144
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         174
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         207
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         218
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT   BINDING         247
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
SQ   SEQUENCE   266 AA;  29446 MW;  E63BCC76CA12204A CRC64;
     MKLSKAARII LVGAPGTQSA RLQTAFAQLS AISSGDLLRT HVQNRTPLGI RAESAIKAGS
     LVPDAMILRL ILAELKDRNW LFTGRPEQPY TLNSSSSAGG EDAVFVAGDM LDTPSLLASF
     PEPRTCDQPS SSFILDGFPR TAEQAVQLDN LVPINLVVHL DTPFSVIMDR IAGRWVHAPS
     GRSYNTSFNA PRVPGRDDVT GERLTKRADD DEGVWLERLE KFKETSEPLL EHYARKGVLW
     RVEGRTSDEI TPKLHKEFAR RFALRD
//
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