KAD_STRP2
ID KAD_STRP2 Reviewed; 212 AA.
AC Q04ML5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=SPD_0214;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
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; CP000410; ABJ54173.1; -; Genomic_DNA.
DR RefSeq; WP_001050431.1; NC_008533.2.
DR PDB; 4NTZ; X-ray; 1.69 A; A=1-212.
DR PDB; 4NU0; X-ray; 1.48 A; A/B=1-212.
DR PDB; 4W5H; X-ray; 1.96 A; A=1-212.
DR PDB; 4W5J; X-ray; 1.65 A; A/B/C/D=1-212.
DR PDBsum; 4NTZ; -.
DR PDBsum; 4NU0; -.
DR PDBsum; 4W5H; -.
DR PDBsum; 4W5J; -.
DR AlphaFoldDB; Q04ML5; -.
DR SMR; Q04ML5; -.
DR STRING; 373153.SPD_0214; -.
DR PRIDE; Q04ML5; -.
DR EnsemblBacteria; ABJ54173; ABJ54173; SPD_0214.
DR GeneID; 60233344; -.
DR GeneID; 66805437; -.
DR KEGG; spd:SPD_0214; -.
DR eggNOG; COG0563; Bacteria.
DR HOGENOM; CLU_032354_1_2_9; -.
DR OMA; FHNRMRV; -.
DR OrthoDB; 1491686at2; -.
DR BioCyc; SPNE373153:G1G6V-237-MON; -.
DR BRENDA; 2.7.4.3; 1960.
DR UniPathway; UPA00588; UER00649.
DR Proteomes; UP000001452; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 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; Nucleotide biosynthesis;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..212
FT /note="Adenylate kinase"
FT /id="PRO_1000058912"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT REGION 127..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 86..89
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 93
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT BINDING 137..138
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 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4NU0"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 31..40
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:4NU0"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:4NU0"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4W5J"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:4NU0"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:4NU0"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:4NU0"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4NU0"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:4NU0"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:4NU0"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 161..183
FT /evidence="ECO:0007829|PDB:4NU0"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:4NU0"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:4NU0"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:4NU0"
SQ SEQUENCE 212 AA; 23721 MW; 11E0D8BC2F01D3C4 CRC64;
MNLLIMGLPG AGKGTQAAKI VEQFHVAHIS TGDMFRAAMA NQTEMGVLAK SYIDKGELVP
DEVTNGIVKE RLSQDDIKET GFLLDGYPRT IEQAHALDKT LAELGIELEG IINIEVNPDS
LLERLSGRII HRVTGETFHK VFNPPVDYKE EDYYQREDDK PETVKRRLDV NIAQGEPIIA
HYRAKGLVHD IEGNQDINDV FSDIEKVLTN LK
