KAD_BORP1
ID KAD_BORP1 Reviewed; 218 AA.
AC J7RC67; P39068;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 45.
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}; OrderedLocusNames=BN118_0657;
OS Bordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 / 18323).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=568706;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 9797 / DSM 5571 / NCTC 10739 / 18323;
RX PubMed=8281944; DOI=10.1111/j.1432-1033.1993.tb18448.x;
RA Gilles A.M., Sismeiro O., Munier H., Fabian H., Mantsch H.H.,
RA Surewicz W.K., Craescu C.C., Barzu O., Danchin A.;
RT "Structural and physico-chemical characteristics of Bordetella pertussis
RT adenylate kinase, a tryptophan-containing enzyme.";
RL Eur. J. Biochem. 218:921-927(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9797 / DSM 5571 / NCTC 10739 / 18323;
RX PubMed=23051057; DOI=10.1186/1471-2164-13-545;
RA Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M.,
RA Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.;
RT "Comparative genomics of the classical Bordetella subspecies: the evolution
RT and exchange of virulence-associated diversity amongst closely related
RT pathogens.";
RL BMC Genomics 13:545-545(2012).
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 ECO:0000269|PubMed:8281944};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for ATP {ECO:0000269|PubMed:8281944};
CC KM=82 uM for AMP {ECO:0000269|PubMed:8281944};
CC KM=100 uM for ADP {ECO:0000269|PubMed:8281944};
CC Vmax=536 umol/min/mg enzyme toward ATP {ECO:0000269|PubMed:8281944};
CC Vmax=420 umol/min/mg enzyme toward ADP {ECO:0000269|PubMed:8281944};
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; Z29715; CAA82801.1; -; Genomic_DNA.
DR EMBL; HE965805; CCJ62082.1; -; Genomic_DNA.
DR PIR; S43016; S43016.
DR RefSeq; WP_003812899.1; NC_018518.1.
DR AlphaFoldDB; J7RC67; -.
DR SMR; J7RC67; -.
DR STRING; 568706.BN118_0657; -.
DR EnsemblBacteria; CCJ62082; CCJ62082; BN118_0657.
DR GeneID; 56478169; -.
DR GeneID; 66438251; -.
DR KEGG; bper:BN118_0657; -.
DR eggNOG; COG0563; Bacteria.
DR HOGENOM; CLU_032354_1_2_4; -.
DR OMA; FHNRMRV; -.
DR SABIO-RK; J7RC67; -.
DR UniPathway; UPA00588; UER00649.
DR Proteomes; UP000005250; Chromosome.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..218
FT /note="Adenylate kinase"
FT /id="PRO_0000421305"
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 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT CONFLICT 122
FT /note="G -> E (in Ref. 1; CAA82801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 23715 MW; FCD1A7F5965F07FA CRC64;
MRLILLGPPG AGKGTQAAFL TQHYGIPQIS TGDMLRAAVK AGTPLGLEAK KVMDAGGLVS
DDLIIGLVRD RLTQPDCANG YLFDGFPRTI PQADALKSAG IALDYVVEIE VPESDIIERM
SGRRVHPASG RSYHVRFNPP KAEGVDDVTG EPLVQRDDDR EETVRHRLNV YQNQTRPLVD
YYSSWAQSDA AAAPKYRKIS GVGSVDEIKS RLSQALQS
