ACL_RS00535

Uniprot: A9NEF4
Description: adenylate kinase
EC number: 2.7.4.3
Annotation score: 3 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000255|HAMAP-Rule:MF_00235}.
Cofactor:
Enzyme regulation:
Function [CC]: 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:0000255|HAMAP-Rule:MF_00235}.
Pathway: PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
Active site:
Binding site: BINDING 33 33 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.; BINDING 38 38 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.; BINDING 94 94 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.; BINDING 129 129 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.; BINDING 162 162 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.; BINDING 173 173 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.; BINDING 201 201 ATP; via carbonyl oxygen. {ECO:0000255|HAMAP-Rule:MF_00235}.
Calcium binding:
DNA binding:
Metal binding: METAL 132 132 Zinc; structural. {ECO:0000255|HAMAP-Rule:MF_00235}.; METAL 135 135 Zinc; structural. {ECO:0000255|HAMAP-Rule:MF_00235}.; METAL 152 152 Zinc; structural. {ECO:0000255|HAMAP-Rule:MF_00235}.; METAL 155 155 Zinc; structural. {ECO:0000255|HAMAP-Rule:MF_00235}.
Nucleotide binding: NP_BIND 12 17 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.; NP_BIND 59 61 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.; NP_BIND 87 90 AMP. {ECO:0000255|HAMAP-Rule:MF_00235}.; NP_BIND 138 139 ATP. {ECO:0000255|HAMAP-Rule:MF_00235}.
Site:
Gene names (primary): adk
Gene names (synonym):
Mass: 24,354
Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}.
Gene ontology (GO): cytoplasm [GO:0005737]; adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; AMP salvage [GO:0044209]
Gene ontology IDs: GO:0004017; GO:0005524; GO:0005737; GO:0044209; GO:0046872
Chain: CHAIN 1 217 Adenylate kinase. /FTId=PRO_1000191115.
Signal peptide:
Domain [CC]: 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:0000255|HAMAP-Rule:MF_00235}.
Sequence similarities: SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-Rule:MF_00235}.
Protein families: Adenylate kinase family
Coiled coil:
Domain [FT]:
Motif:
Region: REGION 32 61 NMPbind. {ECO:0000255|HAMAP-Rule:MF_00235}.; REGION 128 165 LID. {ECO:0000255|HAMAP-Rule:MF_00235}.
EMBL: CP000896
ProteinModelPortal: A9NEF4
MEROPS:
EnsemblBacteria KO: ABX80734
UniPathway: K00939
CDD:
Gene3D: cd01428
HAMAP: 3.40.50.300
InterPro: MF_00235
PANTHER: IPR006259;IPR000850;IPR007862;IPR027417
PIRSF: PTHR23359
PRINTS:
PROSITE: PR00094
Pfam: PS00113
ProDom: PF05191
SMART:
SUPFAM:
TIGRFAMs: SSF52540

94517-95171(+)

>nucleotide sequence
ATGAAAACAAGGATGATATTTGTAGGCCCTCCTGGGGCTGGCAAGGGATCACAGGCAAAA
ATAATTTCACAGACATTAAATATCCCACATATATCAACCGGTGATATGTTCAGAACACAT
ATAAAGGGTAGTACGCCACTTGGTTTGGAAGCTAAAAAGTATACAGACCAAGGGCTACTT
GTACCTGATGATGTAACCAATCAAATGGTTAAAGATCGCCTAAGTCAGAAAGATGTTGAA
AAGGGATTCATCTTTGATGGATATCCAAGAACACCTGATCAAGCAATTTTCTTAGACAAT
CTATTAATGGTAACAAATCAAAAACTTGATGTAGTATTAAATATTTCATCAAGTGATGAA
GTTATTGTTAAACGAATCACAGGTAGAAGAACATGCCCAGTATGTGGTGCTATATATCAT
GTTGATAACTATCCACCAAAAGTGGCAGGTATTTGTGATAATGATGGTGCAACCTTGGTT
CAAAGAAAAGATGATCAAAAAGAAACAATTATTCGTAGACTTAGTGTTTACAAAGAAGAA
ACATTCCCATTAATTAAGTATTATGCACATAAAAACTTACTTATGGATGTTGATGGTAAT
CAACCTTTAGAGGTGATTACAAAACATGTATTAGAAATTCTGGAGCAAAAATGA

>protein sequence
MKTRMIFVGPPGAGKGSQAKIISQTLNIPHISTGDMFRTHIKGSTPLGLEAKKYTDQGLL
VPDDVTNQMVKDRLSQKDVEKGFIFDGYPRTPDQAIFLDNLLMVTNQKLDVVLNISSSDE
VIVKRITGRRTCPVCGAIYHVDNYPPKVAGICDNDGATLVQRKDDQKETIIRRLSVYKEE
TFPLIKYYAHKNLLMDVDGNQPLEVITKHVLEILEQKW