SPM_005025

Uniprot: A0A037UKT3
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 91 91 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.; BINDING 126 126 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.; BINDING 159 159 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.; BINDING 170 170 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.; BINDING 198 198 ATP; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_00235}.
Calcium binding:
DNA binding:
Metal binding: METAL 129 129 Zinc; structural. {ECO:0000256|HAMAP-Rule:MF_00235}.; METAL 132 132 Zinc; structural. {ECO:0000256|HAMAP-Rule:MF_00235}.; METAL 149 149 Zinc; structural. {ECO:0000256|HAMAP-Rule:MF_00235}.; METAL 151 151 Zinc; structural. {ECO:0000256|HAMAP-Rule:MF_00235}.
Nucleotide binding: NP_BIND 11 16 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.; NP_BIND 84 87 AMP. {ECO:0000256|HAMAP-Rule:MF_00235}.; NP_BIND 135 136 ATP. {ECO:0000256|HAMAP-Rule:MF_00235}.
Site:
Gene names (primary): adk
Gene names (synonym):
Mass: 24,010
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]; zinc ion binding [GO:0008270]; nucleotide biosynthetic process [GO:0009165]
Gene ontology IDs: GO:0004017; GO:0005524; GO:0005737; GO:0008270; 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. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain. {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 126 161 ADK_lid. {ECO:0000259|Pfam:PF05191}.
Motif:
Region: REGION 31 60 NMPbind. {ECO:0000256|HAMAP-Rule:MF_00235}.; REGION 125 162 LID. {ECO:0000256|HAMAP-Rule:MF_00235}.
EMBL: AGBZ02000004
ProteinModelPortal:
MEROPS:
EnsemblBacteria KO: KAI92102
UniPathway:
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

68548-69187(+)

>nucleotide sequence
ATGCGAAATTTTATTTTGTTAGGAGCTCCTGGAAGTGGAAAAGGAACCCAATCAGACCAT
TTAGTCAAAAAGTTTGGTTTTACTCATATTTCAACTGGCAATATTATTCGAGATAATATT
AAGCAAAAAACACCATTAGGTATTTTGTGTCAACAGTATGCTGACCAGGGAAAATTAGTT
CCGGATGATATTATGATTCAAATGGTTGAAAACCATTTACAAATAGTAAGTGGTGATTTA
ATTTGAGATGGTTTTCCACGCACAATTGCACAAGCAAAAAAATTAGATCAATTATTGCAA
AAACTAAATAGCAAAGTTGACCATACGTTATATTTTGAAATTGATGAAGCAAAGTTAATC
GAACGAATTACGGGACGTTTAACTTGTCTAACTTGTGGGCGAACATATCATAAAACAGCA
TTGCCACCAAAAGTAGCATGAATTTGTGATGATGATCAAACCCCATTAGTACAACGAAAA
GATGATAACGAAGAAAAAATTAAAATTAGATTAGCGGCATATCATGCTGATACTGCACCG
TTAATTGAATATTATTTAAATCAGCAAGTATTAACCGTTATTGATGCTGATATGGAAGGA
CATGCTGTTTGAGATCAAATTATGGCAGTTTTAAAATAA

>protein sequence
MRNFILLGAPGSGKGTQSDHLVKKFGFTHISTGNIIRDNIKQKTPLGILCQQYADQGKLV
PDDIMIQMVENHLQIVSGDLIWDGFPRTIAQAKKLDQLLQKLNSKVDHTLYFEIDEAKLI
ERITGRLTCLTCGRTYHKTALPPKVAWICDDDQTPLVQRKDDNEEKIKIRLAAYHADTAP
LIEYYLNQQVLTVIDADMEGHAVWDQIMAVLK