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Adenylate kinase (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate kinase cytosolic and mitochondrial) (Adenylate monophosphate kinase)

 F7VP73_SORMK            Unreviewed;       278 AA.
F7VP73;
21-SEP-2011, integrated into UniProtKB/TrEMBL.
21-SEP-2011, sequence version 1.
20-DEC-2017, entry version 50.
RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_03168, ECO:0000256|SAAS:SAAS00720755};
EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_03168, ECO:0000256|SAAS:SAAS00720755};
AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_03168};
AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_03168};
AltName: Full=Adenylate kinase cytosolic and mitochondrial {ECO:0000256|HAMAP-Rule:MF_03168};
AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_03168};
Name=ADK1 {ECO:0000256|HAMAP-Rule:MF_03168};
ORFNames=SMAC_02310 {ECO:0000313|EMBL:CCC07301.1};
Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) /
K-hell).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Sordaria.
NCBI_TaxID=771870 {ECO:0000313|EMBL:CCC07301.1, ECO:0000313|Proteomes:UP000001881};
[1] {ECO:0000313|EMBL:CCC07301.1, ECO:0000313|Proteomes:UP000001881}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell
{ECO:0000313|Proteomes:UP000001881};
TISSUE=Mycelium {ECO:0000313|EMBL:CCC07301.1};
PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
Nowrousian M., Stajich J., Chu M., Engh I., Espagne E., Halliday K.,
Kamerewerd J., Kempken F., Knab B., Kuo H.C., Osiewacz H.D.,
Poeggeler S., Read N., Seiler S., Smith K., Zickler D., Kueck U.,
Freitag M.;
"De novo assembly of a 40 Mb eukaryotic genome from short sequence
reads: Sordaria macrospora, a model organism for fungal
morphogenesis.";
PLoS Genet. 6:E1000891-E1000891(2010).
-!- FUNCTION: Catalyzes the reversible transfer of the terminal
phosphate group between ATP and AMP. Plays an important role in
cellular energy homeostasis and in adenine nucleotide metabolism.
Adenylate kinase activity is critical for regulation of the
phosphate utilization and the AMP de novo biosynthesis pathways.
{ECO:0000256|HAMAP-Rule:MF_03168, ECO:0000256|SAAS:SAAS00720765}.
-!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000256|HAMAP-
Rule:MF_03168, ECO:0000256|SAAS:SAAS00720764}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03168,
ECO:0000256|SAAS:SAAS00720754}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000256|HAMAP-
Rule:MF_03168}. Mitochondrion intermembrane space
{ECO:0000256|HAMAP-Rule:MF_03168, ECO:0000256|SAAS:SAAS00720769}.
Note=Predominantly mitochondrial. {ECO:0000256|HAMAP-
Rule:MF_03168}.
-!- DOMAIN: Consists of three domains, a large central CORE domain and
two small peripheral domains, NMPbind and LID, which undergo
movements during catalysis. The LID domain closes over the site of
phosphoryl transfer upon ATP binding. Assembling and dissambling
the active center during each catalytic cycle provides an
effective means to prevent ATP hydrolysis. {ECO:0000256|HAMAP-
Rule:MF_03168}.
-!- SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily.
{ECO:0000256|HAMAP-Rule:MF_03168}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:CCC07301.1}.
-----------------------------------------------------------------------
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EMBL; CABT02000003; CCC07301.1; -; Genomic_DNA.
RefSeq; XP_003350638.1; XM_003350590.1.
ProteinModelPortal; F7VP73; -.
STRING; 771870.XP_003350638.1; -.
EnsemblFungi; CCC07301; CCC07301; SMAC_02310.
GeneID; 10808203; -.
KEGG; smp:SMAC_02310; -.
EuPathDB; FungiDB:SMAC_02310; -.
eggNOG; KOG3078; Eukaryota.
eggNOG; COG0563; LUCA.
InParanoid; F7VP73; -.
KO; K00939; -.
OrthoDB; EOG092C5OQU; -.
Proteomes; UP000001881; Unassembled WGS sequence.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0006172; P:ADP biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0046033; P:AMP metabolic process; IEA:UniProtKB-UniRule.
GO; GO:0046034; P:ATP metabolic process; IEA:UniProtKB-UniRule.
GO; GO:0006270; P:DNA replication initiation; IEA:EnsemblFungi.
CDD; cd01428; ADK; 1.
HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
HAMAP; MF_03168; Adenylate_kinase_AK2; 1.
InterPro; IPR006259; Adenyl_kin_sub.
InterPro; IPR000850; Adenylat/UMP-CMP_kin.
InterPro; IPR033690; Adenylat_kinase_CS.
InterPro; IPR007862; Adenylate_kinase_lid-dom.
InterPro; IPR028587; AK2.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR23359; PTHR23359; 1.
Pfam; PF05191; ADK_lid; 1.
PRINTS; PR00094; ADENYLTKNASE.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01351; adk; 1.
PROSITE; PS00113; ADENYLATE_KINASE; 1.
3: Inferred from homology;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03168,
ECO:0000256|SAAS:SAAS00720763}; Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000001881};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03168};
Kinase {ECO:0000256|HAMAP-Rule:MF_03168,
ECO:0000256|RuleBase:RU003330, ECO:0000256|SAAS:SAAS00720760};
Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03168,
ECO:0000256|SAAS:SAAS00720774};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03168,
ECO:0000256|SAAS:SAAS00720763};
Reference proteome {ECO:0000313|Proteomes:UP000001881};
Transferase {ECO:0000256|HAMAP-Rule:MF_03168,
ECO:0000256|RuleBase:RU003330, ECO:0000256|SAAS:SAAS00720760}.
DOMAIN 168 203 ADK_lid. {ECO:0000259|Pfam:PF05191}.
NP_BIND 50 55 ATP. {ECO:0000256|HAMAP-Rule:MF_03168}.
NP_BIND 97 99 AMP. {ECO:0000256|HAMAP-Rule:MF_03168}.
NP_BIND 126 129 AMP. {ECO:0000256|HAMAP-Rule:MF_03168}.
NP_BIND 177 178 ATP. {ECO:0000256|HAMAP-Rule:MF_03168}.
REGION 70 99 NMPbind. {ECO:0000256|HAMAP-
Rule:MF_03168}.
REGION 167 204 LID. {ECO:0000256|HAMAP-Rule:MF_03168}.
COILED 8 28 {ECO:0000256|SAM:Coils}.
COILED 199 219 {ECO:0000256|SAM:Coils}.
BINDING 71 71 AMP. {ECO:0000256|HAMAP-Rule:MF_03168}.
BINDING 76 76 AMP. {ECO:0000256|HAMAP-Rule:MF_03168}.
BINDING 133 133 AMP. {ECO:0000256|HAMAP-Rule:MF_03168}.
BINDING 168 168 ATP. {ECO:0000256|HAMAP-Rule:MF_03168}.
BINDING 201 201 AMP. {ECO:0000256|HAMAP-Rule:MF_03168}.
BINDING 212 212 AMP. {ECO:0000256|HAMAP-Rule:MF_03168}.
BINDING 240 240 ATP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_03168}.
SEQUENCE 278 AA; 30113 MW; D6B2117B54EE6619 CRC64;
MGFIDDEVKR LGDVIASLEG RVKSLEAREF SGKPTTTAEQ VRMILIGPPG AGKGTQAPKI
KEKFNCCHLA TGDMLRAQVA KGTALGKQAK KIMNEGGLVS DDIVIGMIKD ELENNKECQG
GFILDGFPRT VPQAEGLDAM LRERNLPLQH AVELKIDDSL LVARITGRLV HPASGRSYHL
TFNPPKEAMK DDITGEPLVQ RSDDNAEALR KRLETYHKQT APVVGYYQNT GIWKAIDASQ
EPGQVWKSLL AIFDGDKAKA SNAGSGILSK IAHAAKSS


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