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Adenylate kinase (AK) (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase)

 A0A1J0GLS1_9CLOT        Unreviewed;       220 AA.
A0A1J0GLS1;
15-FEB-2017, integrated into UniProtKB/TrEMBL.
15-FEB-2017, sequence version 1.
25-OCT-2017, entry version 7.
RecName: Full=Adenylate kinase {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00914410};
Short=AK {ECO:0000256|HAMAP-Rule:MF_00235};
EC=2.7.4.3 {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763757};
AltName: Full=ATP-AMP transphosphorylase {ECO:0000256|HAMAP-Rule:MF_00235};
AltName: Full=ATP:AMP phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00235};
AltName: Full=Adenylate monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_00235};
Name=adk {ECO:0000256|HAMAP-Rule:MF_00235};
ORFNames=A7L45_20805 {ECO:0000313|EMBL:APC42324.1};
Clostridium estertheticum subsp. estertheticum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1552 {ECO:0000313|EMBL:APC42324.1, ECO:0000313|Proteomes:UP000182569};
[1] {ECO:0000313|Proteomes:UP000182569}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=DSM 8809 {ECO:0000313|Proteomes:UP000182569};
PubMed=27891116;
Yu Z., Gunn L., Brennan E., Reid R., Wall P.G., Gaora O.P., Hurley D.,
Bolton D., Fanning S.;
"Complete Genome Sequence of Clostridium estertheticum DSM 8809, a
Microbe Identified in Spoiled Vacuum Packed Beef.";
Front. Microbiol. 7:1764-1764(2016).
-!- 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.
{ECO:0000256|HAMAP-Rule:MF_00235}.
-!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000256|HAMAP-
Rule:MF_00235, ECO:0000256|RuleBase:RU003331,
ECO:0000256|SAAS:SAAS00763738}.
-!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway;
AMP from ADP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|SAAS:SAAS00914379}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00914390}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331}.
-!- 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. Some bacteria have
evolved a zinc-coordinating structure that stabilizes the LID
domain. {ECO:0000256|HAMAP-Rule:MF_00235}.
-!- SIMILARITY: Belongs to the adenylate kinase family.
{ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003330}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00235}.
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EMBL; CP015756; APC42324.1; -; Genomic_DNA.
RefSeq; WP_071614611.1; NZ_CP015756.1.
KEGG; ceu:A7L45_20805; -.
KO; K00939; -.
UniPathway; UPA00588; UER00649.
Proteomes; UP000182569; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
CDD; cd01428; ADK; 1.
HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
InterPro; IPR006259; Adenyl_kin_sub.
InterPro; IPR000850; Adenylat/UMP-CMP_kin.
InterPro; IPR033690; Adenylat_kinase_CS.
InterPro; IPR007862; Adenylate_kinase_lid-dom.
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_00235,
ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
Complete proteome {ECO:0000313|Proteomes:UP000182569};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00235};
Kinase {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:APC42324.1};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00235};
Nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|SAAS:SAAS00914406};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00763703};
Reference proteome {ECO:0000313|Proteomes:UP000182569};
Transferase {ECO:0000256|HAMAP-Rule:MF_00235,
ECO:0000256|RuleBase:RU003330, ECO:0000313|EMBL:APC42324.1};
Zinc {ECO:0000256|HAMAP-Rule:MF_00235}.
DOMAIN 127 162 ADK_lid. {ECO:0000259|Pfam:PF05191}.
NP_BIND 10 15 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
NP_BIND 85 88 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
NP_BIND 136 137 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
REGION 30 59 NMPbind. {ECO:0000256|HAMAP-
Rule:MF_00235}.
REGION 126 163 LID. {ECO:0000256|HAMAP-Rule:MF_00235}.
METAL 130 130 Zinc; structural. {ECO:0000256|HAMAP-
Rule:MF_00235}.
METAL 133 133 Zinc; structural. {ECO:0000256|HAMAP-
Rule:MF_00235}.
METAL 150 150 Zinc; structural. {ECO:0000256|HAMAP-
Rule:MF_00235}.
METAL 153 153 Zinc; structural. {ECO:0000256|HAMAP-
Rule:MF_00235}.
BINDING 31 31 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 36 36 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 92 92 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 127 127 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 160 160 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 171 171 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.
BINDING 199 199 ATP; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_00235}.
SEQUENCE 220 AA; 24447 MW; 97EDAC976D217A6C CRC64;
MRIILLGPPG AGKGTQAKSI SNKFSIPHIS TGDIFRKNIS EKTPLGIEAK RHIDKGHLVP
DKLTIDIIKD RLDNEDCVNG FLLDGYPRTV NQGEALKTLL DEKDIHLDTA LLIKVPREFI
LDRMTGRRVC LACGASYHIA FNPSKVDGKC DLCGSDLVQR ADDTEVTVNE RIDIYEAQTQ
PLIKYYGDKN LLSEVDGTQE INSVFDSICS ILAEIKNDKH


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