GCW_00380

Uniprot: A0A0F6CJX4
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:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331, ECO:0000256|SAAS:SAAS00079620}.
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:0000256|HAMAP-Rule:MF_00235}.
Pathway: PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00235}.
Active site:
Binding site: BINDING 32 32 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.; BINDING 37 37 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.; BINDING 94 94 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.; BINDING 125 125 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}.
Calcium binding:
DNA binding:
Metal binding:
Nucleotide binding: NP_BIND 11 16 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.; NP_BIND 87 90 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.; NP_BIND 134 135 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
Site:
Gene names (primary): adk
Gene names (synonym):
Mass: 24,963
Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003331}.
Gene ontology (GO): cytoplasm [GO:0005737]; adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; nucleotide biosynthetic process [GO:0009165]
Gene ontology IDs: GO:0004017; GO:0005524; GO:0005737; GO:0009165
Chain:
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. {ECO:0000256|HAMAP-Rule:MF_00235}.
Sequence similarities: SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000256|HAMAP-Rule:MF_00235, ECO:0000256|RuleBase:RU003330}.
Protein families: Adenylate kinase family
Coiled coil:
Domain [FT]: DOMAIN 125 162 ADK_lid. {ECO:0000259|Pfam:PF05191}.
Motif:
Region: REGION 31 61 NMPbind. {ECO:0000256|HAMAP-Rule:MF_00235}.; REGION 124 163 LID. {ECO:0000256|HAMAP-Rule:MF_00235}.
EMBL: CP006916
ProteinModelPortal: A0A0F6CJX4
MEROPS:
EnsemblBacteria KO: AHB99396
UniPathway: K00939
CDD:
Gene3D: cd01428
HAMAP: 3.40.50.300
InterPro: MF_00235
PANTHER: IPR006259;IPR000850;IPR007862;IPR027417
PIRSF: PTHR23359
PRINTS:
PROSITE: PR00094
Pfam:
ProDom: PF05191
SMART:
SUPFAM:
TIGRFAMs: SSF52540
78796-79441(+)

>nucleotide sequence
GTGATAAGATTAATTTTTCTAGGTGCACCTGGAACAGGTAAAGGGACGATCTCTTCTTAT
TTAAAAGAACAGCACGGTTTTTTCCACATTTCAAGCGGAGATCTATTTCGCTTTTATGCT
AAAGAAGAAAAAACCGCTTTAGCTGAAGAGATCAAAAGTTATATTAATAACGGACTTTAT
GTCCCAGATGAGTTAACTAACCGTACGGTAGCTGATTTTTATCATAAAAATCAATCCCAA
GATAAGATTATCTTTGATGGGTATCCAAGAACACTTAATCAATGTGAATACATTGATGAG
ATCATCAAATTTACTCACGTCATCTTATTACAACCAACCGATTGAGATATGATCATCAAT
CGACTAAGTTCACGTCGATCATGTCCACAATGTAAACGAATTTACAATATTAATTCGGTT
GATTTTAAACCTAAAGTGGCTAATCTTTGTGATCTTTGTAAAGTTGAATTAATCCATCGA
AAAGATGATGATCCTAGTGTGGTAAGCACTAGAATCAACGTTTATAACGAACAAACTAAA
CCAGTAATCGAATACTACAAGAAGAAAAACTTATTACACTTAGTTGATGCTAATAAGAGT
TTTGAAGAGTTATACAAGCTTGTTTTAGAGATCGTTAACAAATAA

>protein sequence
VIRLIFLGAPGTGKGTISSYLKEQHGFFHISSGDLFRFYAKEEKTALAEEIKSYINNGLY
VPDELTNRTVADFYHKNQSQDKIIFDGYPRTLNQCEYIDEIIKFTHVILLQPTDWDMIIN
RLSSRRSCPQCKRIYNINSVDFKPKVANLCDLCKVELIHRKDDDPSVVSTRINVYNEQTK
PVIEYYKKKNLLHLVDANKSFEELYKLVLEIVNK