ID A0A094DHF2_9PEZI Unreviewed; 282 AA.
AC A0A094DHF2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=V496_03784 {ECO:0000313|EMBL:KFY63683.1};
OS Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY63683.1, ECO:0000313|Proteomes:UP000029302};
RN [1] {ECO:0000313|EMBL:KFY63683.1, ECO:0000313|Proteomes:UP000029302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY63683.1}.
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DR EMBL; JPJY01000603; KFY63683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DHF2; -.
DR STRING; 1420909.A0A094DHF2; -.
DR HOGENOM; CLU_032354_1_1_1; -.
DR OrthoDB; 167111at2759; -.
DR Proteomes; UP000029302; 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:SF22; GTP:AMP PHOSPHOTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR Pfam; PF00406; ADK; 2.
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 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|HAMAP-Rule:MF_03169};
KW Reference proteome {ECO:0000313|Proteomes:UP000029302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03169}.
FT DOMAIN 178..213
FT /note="Adenylate kinase active site lid"
FT /evidence="ECO:0000259|Pfam:PF05191"
FT REGION 37..66
FT /note="NMPbind"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT REGION 177..214
FT /note="LID"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 38
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 43
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 64..66
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 141..144
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 148
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 211
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 222
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
FT BINDING 251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03169"
SQ SEQUENCE 282 AA; 30717 MW; 69EE8472CE88E0EF CRC64;
MKLSKAARII LVGAPGVGKG TQSARLLTAF PQLSAISSGD LLRTHVQNRT PLGIRAESAI
KAGSLVPDAM ILRLILHELK SRNWLFPGAP EQSYSLNSSS SAGGEDAAFA AGDMLDTPSL
LASFPSPRTC DEPGSSFILD GFPRTAEQAQ QLDNLVPINL VVHLDTPFSV IMDRIAGRWV
HAPSGRSYNT SFNAPRVPGL DDVTGEKLTK RADDDEGVWL ERLEKFKETS EPLLEHYARK
GVLWRVEGET SDEITPKLHR EFARRFAARD EMGAVGGWVN TT
//
