KAD_SPOGL
ID KAD_SPOGL Reviewed; 217 AA.
AC P84139;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Sporosarcina globispora (Bacillus globisporus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1459;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS)
RP OF COMPLEX WITH BI-SUBSTRATE ANALOG AP5A AND ZINC, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15100224; DOI=10.1074/jbc.m401865200;
RA Bae E., Phillips G.N. Jr.;
RT "Structures and analysis of highly homologous psychrophilic, mesophilic,
RT and thermophilic adenylate kinases.";
RL J. Biol. Chem. 279:28202-28208(2004).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, AND ZINC ION.
RX PubMed=8288548; DOI=10.1128/jb.176.2.520-523.1994;
RA Gilles A.-M., Glaser P., Perrier V., Meier A., Longin R., Sebald M.,
RA Maignan L., Pistotnik E., Barzu O.;
RT "Zinc, a structural component of adenylate kinases from Gram-positive
RT bacteria.";
RL J. Bacteriol. 176:520-523(1994).
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:15100224}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. Thermal denaturation
CC midpoint (Tm) is 43.3 degrees Celsius and is raised to 60.4 degrees
CC Celsius when AK is complexed with the inhibitor Ap5A.
CC {ECO:0000269|PubMed:15100224};
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:15100224, ECO:0000305|PubMed:8288548}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
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DR PDB; 1S3G; X-ray; 2.25 A; A=1-217.
DR PDB; 5X6J; X-ray; 2.10 A; A=1-217.
DR PDBsum; 1S3G; -.
DR PDBsum; 5X6J; -.
DR AlphaFoldDB; P84139; -.
DR SMR; P84139; -.
DR DrugBank; DB01717; Bis(Adenosine)-5'-Pentaphosphate.
DR BRENDA; 2.7.4.3; 659.
DR UniPathway; UPA00588; UER00649.
DR EvolutionaryTrace; P84139; -.
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; Direct protein sequencing; Kinase;
KW Metal-binding; Nucleotide biosynthesis; Nucleotide-binding; Transferase;
KW Zinc.
FT CHAIN 1..217
FT /note="Adenylate kinase"
FT /id="PRO_0000158724"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
FT REGION 126..163
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
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:15100224"
FT BINDING 31
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
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:15100224"
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:15100224"
FT BINDING 92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
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:15100224"
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:15100224"
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:15100224"
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:15100224"
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:15100224"
FT BINDING 160
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
FT BINDING 171
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
FT BINDING 199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:15100224"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:5X6J"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5X6J"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:5X6J"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:5X6J"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:5X6J"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:5X6J"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5X6J"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5X6J"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:5X6J"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5X6J"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:5X6J"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:5X6J"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:5X6J"
FT HELIX 201..212
FT /evidence="ECO:0007829|PDB:5X6J"
SQ SEQUENCE 217 AA; 23888 MW; A8E28D5CF7C747AE CRC64;
MNIVLMGLPG AGKGTQADRI VEKYGTPHIS TGDMFRAAIQ EGTELGVKAK SFMDQGALVP
DEVTIGIVRE RLSKSDCDNG FLLDGFPRTV PQAEALDQLL ADMGRKIEHV LNIQVEKEEL
IARLTGRRIC KVCGTSYHLL FNPPQVEGKC DKDGGELYQR ADDNPDTVTN RLEVNMNQTA
PLLAFYDSKE VLVNINGQKD IKDVFKDLDV ILQGNGQ
