KAD_GEOSE
ID KAD_GEOSE Reviewed; 217 AA.
AC P27142;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 122.
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, ECO:0000269|PubMed:1554691};
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 Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ZINC ION, BIOPHYSICOCHEMICAL PROPERTIES,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=1554691; DOI=10.1021/bi00127a002;
RA Glaser P., Presecan E., Delepierre M., Surewicz W.K., Mantsch H.H.,
RA Barzu O., Gilles A.M.;
RT "Zinc, a novel structural element found in the family of bacterial
RT adenylate kinases.";
RL Biochemistry 31:3038-3043(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schiltz E., Buerkle S., Stiehle H., Mader B., Schulz G.E.;
RL Submitted (APR-1992) to the PIR data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF COMPLEX WITH BI-SUBSTRATE ANALOG
RP AP5A AND ZINC.
RX PubMed=9715904;
RX DOI=10.1002/(sici)1097-0134(19980815)32:3<276::aid-prot3>3.0.co;2-g;
RA Berry M.B., Phillips G.N. Jr.;
RT "Crystal structures of Bacillus stearothermophilus adenylate kinase with
RT bound Ap5A, Mg2+ Ap5A, and Mn2+ Ap5A reveal an intermediate lid position
RT and six coordinate octahedral geometry for bound Mg2+ and Mn2+.";
RL Proteins 32:276-288(1998).
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, ECO:0000269|PubMed:1554691}.
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:1554691};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Thermal denaturation
CC midpoint (Tm) is 74.5 degrees Celsius. {ECO:0000269|PubMed:1554691};
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. Some bacteria have evolved a zinc-coordinating structure
CC that stabilizes the LID domain. {ECO:0000255|HAMAP-Rule:MF_00235,
CC ECO:0000305|PubMed:1554691, ECO:0000305|PubMed:9715904}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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DR EMBL; M88104; AAA22205.1; -; Genomic_DNA.
DR PIR; B42196; KIBSAF.
DR PDB; 1ZIN; X-ray; 1.60 A; A=1-217.
DR PDB; 1ZIO; X-ray; 1.96 A; A=1-217.
DR PDB; 1ZIP; X-ray; 1.85 A; A=1-217.
DR PDB; 4QBH; X-ray; 1.67 A; A/B=1-215.
DR PDB; 4QBI; X-ray; 1.67 A; A/B=1-215.
DR PDBsum; 1ZIN; -.
DR PDBsum; 1ZIO; -.
DR PDBsum; 1ZIP; -.
DR PDBsum; 4QBH; -.
DR PDBsum; 4QBI; -.
DR AlphaFoldDB; P27142; -.
DR SMR; P27142; -.
DR DrugBank; DB01717; Bis(Adenosine)-5'-Pentaphosphate.
DR BRENDA; 2.7.4.3; 623.
DR SABIO-RK; P27142; -.
DR UniPathway; UPA00588; UER00649.
DR EvolutionaryTrace; P27142; -.
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:0008270; F:zinc ion 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 3D-structure; ATP-binding; Cytoplasm; Kinase; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Transferase; Zinc.
FT CHAIN 1..217
FT /note="Adenylate kinase"
FT /id="PRO_0000158729"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT REGION 126..163
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 10..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 31
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 57..59
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 85..88
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 136..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 160
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 171
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:9715904"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1ZIN"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1ZIN"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:1ZIN"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:1ZIN"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1ZIN"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1ZIN"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1ZIN"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1ZIN"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1ZIN"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:1ZIP"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:1ZIN"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:1ZIN"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:1ZIN"
SQ SEQUENCE 217 AA; 24143 MW; D8701931117C53CF CRC64;
MNLVLMGLPG AGKGTQAEKI VAAYGIPHIS TGDMFRAAMK EGTPLGLQAK QYMDRGDLVP
DEVTIGIVRE RLSKDDCQNG FLLDGFPRTV AQAEALETML ADIGRKLDYV IHIDVRQDVL
MERLTGRRIC RNCGATYHLI FHPPAKPGVC DKCGGELYQR ADDNEATVAN RLEVNMKQMK
PLVDFYEQKG YLRNINGEQD MEKVFADIRE LLGGLAR
