KAD_NEIME
ID KAD_NEIME Reviewed; 215 AA.
AC P0DH56; P49980; P69344;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00235};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235};
DE AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
GN Name=adk {ECO:0000255|HAMAP-Rule:MF_00235};
OS Neisseria meningitidis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=020, 1001, 3910, 4100, 4146, 5005, 5010, 5013, 5035, 5043,
RC ATCC 43831, HF110, HF113, HF116, HF130, HF147, HF16, HF175, HF200, HF4,
RC HF46, HF79, HF8, HF85, M470, N94II, P63, and S3446;
RX PubMed=7479835; DOI=10.1073/pnas.92.23.10535;
RA Feil E., Carpenter G., Spratt B.G.;
RT "Electrophoretic variation in adenylate kinase of Neisseria meningitidis is
RT due to inter- and intraspecies recombination.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10535-10539(1995).
CC -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC group between ATP and AMP. Plays an important role in cellular energy
CC homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00235};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC small peripheral domains, NMPbind and LID, which undergo movements
CC during catalysis. The LID domain closes over the site of phosphoryl
CC transfer upon ATP binding. Assembling and dissambling the active center
CC during each catalytic cycle provides an effective means to prevent ATP
CC hydrolysis. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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DR EMBL; L36469; AAA99172.1; -; Genomic_DNA.
DR EMBL; L36470; AAA99173.1; -; Genomic_DNA.
DR EMBL; L47130; AAC41495.1; -; Genomic_DNA.
DR EMBL; L47131; AAC41494.1; -; Genomic_DNA.
DR EMBL; L47132; AAC41497.1; -; Genomic_DNA.
DR EMBL; L47133; AAC41496.1; -; Genomic_DNA.
DR EMBL; L47134; AAC41498.1; -; Genomic_DNA.
DR EMBL; L47136; AAC41499.1; -; Genomic_DNA.
DR EMBL; L47137; AAC41501.1; -; Genomic_DNA.
DR EMBL; L47138; AAC41502.1; -; Genomic_DNA.
DR EMBL; L47139; AAC41503.1; -; Genomic_DNA.
DR EMBL; L47140; AAC41504.1; -; Genomic_DNA.
DR EMBL; L47141; AAC41505.1; -; Genomic_DNA.
DR EMBL; L47142; AAC41508.1; -; Genomic_DNA.
DR EMBL; L47143; AAC41506.1; -; Genomic_DNA.
DR EMBL; L47144; AAC41507.1; -; Genomic_DNA.
DR EMBL; L47145; AAC41510.1; -; Genomic_DNA.
DR EMBL; L47146; AAC41509.1; -; Genomic_DNA.
DR EMBL; L47147; AAC41511.1; -; Genomic_DNA.
DR EMBL; L47148; AAC41512.1; -; Genomic_DNA.
DR EMBL; L47149; AAC41514.1; -; Genomic_DNA.
DR EMBL; L47150; AAC41513.1; -; Genomic_DNA.
DR EMBL; L47151; AAC41515.1; -; Genomic_DNA.
DR EMBL; L47152; AAC41516.1; -; Genomic_DNA.
DR EMBL; L47153; AAC41517.1; -; Genomic_DNA.
DR EMBL; L47154; AAC41489.1; -; Genomic_DNA.
DR EMBL; L47155; AAC41493.1; -; Genomic_DNA.
DR EMBL; L47157; AAC41491.1; -; Genomic_DNA.
DR EMBL; L47158; AAC41492.1; -; Genomic_DNA.
DR PIR; S61841; S61841.
DR RefSeq; WP_002213936.1; NZ_WSOH01000001.1.
DR RefSeq; WP_002219494.1; NZ_RQJM01000001.1.
DR AlphaFoldDB; P0DH56; -.
DR SMR; P0DH56; -.
DR GeneID; 61281052; -.
DR OMA; FHNRMRV; -.
DR UniPathway; UPA00588; UER00649.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01428; ADK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR InterPro; IPR006259; Adenyl_kin_sub.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR033690; Adenylat_kinase_CS.
DR InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 1.
DR Pfam; PF05191; ADK_lid; 1.
DR PRINTS; PR00094; ADENYLTKNASE.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01351; adk; 1.
DR PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..215
FT /note="Adenylate kinase"
FT /id="PRO_0000158814"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT REGION 122..159
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 31
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 57..59
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 85..88
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 132..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 156
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 167
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT VARIANT 5
FT /note="L -> F (in strain: S3446 and 020)"
FT VARIANT 55
FT /note="E -> K (in strain: HF4, HF8, HF16, HF85, HF110,
FT HF116 and HF175)"
FT VARIANT 139
FT /note="P -> S (in strain: HF130)"
FT VARIANT 201
FT /note="P -> A (in strain: HF4, HF8, HF16, HF79, HF85,
FT HF110, HF113, HF116, HF147, HF175 and HF200)"
FT VARIANT 211..212
FT /note="GA -> KG (in strain: HF4, HF8, HF16, HF79, HF85,
FT HF110, HF113, HF116, HF147, HF175 and HF200)"
SQ SEQUENCE 215 AA; 23217 MW; 845DA8C390468D23 CRC64;
MKALLLGAPG AGKGTQAQFI TAAFGIPQIS TGDMLRAAIK AGTPLGLEAK KIIDEGGLVR
DDIIIGMVKE RIAQDDCKNG FLFDGFPRTL AQAEAMVEAG VDLDAVVEID VPDSVIVDRM
SGRRVHLASG RTYHVTYNPP KVEGKDDVTG EDLIQRDDDK EETVKKRLAV YHEQTEVLVD
FYSKLEGEHA PKYIKVDGTQ PVEAVKAEVL GALGK
