KAD_ECOLI
ID KAD_ECOLI Reviewed; 214 AA.
AC P69441; P05082; P77123; Q2MBV3;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 154.
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}; Synonyms=dnaW, plsA;
GN OrderedLocusNames=b0474, JW0463;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2997739; DOI=10.1093/nar/13.19.7139;
RA Brune M., Schumann R., Wittinghofer F.;
RT "Cloning and sequencing of the adenylate kinase gene (adk) of Escherichia
RT coli.";
RL Nucleic Acids Res. 13:7139-7151(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.
RX PubMed=3299380; DOI=10.1073/pnas.84.15.5177;
RA Bardwell J.C.A., Craig E.A.;
RT "Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia
RT coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5177-5181(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-214.
RX PubMed=2051480; DOI=10.1016/0022-2836(91)90180-e;
RA Miyamoto K., Nakahigashi K., Nishimura K., Inokuchi H.;
RT "Isolation and characterization of visible light-sensitive mutants of
RT Escherichia coli K12.";
RL J. Mol. Biol. 219:393-398(1991).
RN [7]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 1-11.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [10]
RP FUNCTION.
RX PubMed=166976; DOI=10.1128/jb.123.1.128-136.1975;
RA Glaser M., Nulty W., Vagelos P.R.;
RT "Role of adenylate kinase in the regulation of macromolecular biosynthesis
RT in a putative mutant of Escherichia coli defective in membrane phospholipid
RT biosynthesis.";
RL J. Bacteriol. 123:128-136(1975).
RN [11]
RP FUNCTION.
RX PubMed=6243627; DOI=10.1128/jb.141.1.405-408.1980;
RA Esmon B.E., Kensil C.R., Cheng C.H., Glaser M.;
RT "Genetic analysis of Escherichia coli mutants defective in adenylate kinase
RT and sn-glycerol 3-phosphate acyltransferase.";
RL J. Bacteriol. 141:405-408(1980).
RN [12]
RP MUTAGENESIS OF GLY-10 AND LYS-13.
RX PubMed=2844237; DOI=10.1021/bi00413a020;
RA Reinstein J., Brune M., Wittinghofer A.;
RT "Mutations in the nucleotide binding loop of adenylate kinase of
RT Escherichia coli.";
RL Biochemistry 27:4712-4720(1988).
RN [13]
RP MUTAGENESIS OF PRO-9; GLY-10 AND LYS-13.
RX PubMed=2223776; DOI=10.1021/bi00484a014;
RA Reinstein J., Schlichting I., Wittinghofer A.;
RT "Structurally and catalytically important residues in the phosphate binding
RT loop of adenylate kinase of Escherichia coli.";
RL Biochemistry 29:7451-7459(1990).
RN [14]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [15]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10398370;
RX DOI=10.1002/(sici)1097-0134(19990801)36:2<238::aid-prot9>3.0.co;2-k;
RA Munier-Lehmann H., Burlacu-Miron S., Craescu C.T., Mantsch H.H.,
RA Schultz C.P.;
RT "A new subfamily of short bacterial adenylate kinases with the
RT Mycobacterium tuberculosis enzyme as a model: a predictive and experimental
RT study.";
RL Proteins 36:238-248(1999).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH THE INHIBITOR AP5A.
RX PubMed=1548697; DOI=10.1016/0022-2836(92)90582-5;
RA Mueller C.W., Schulz G.E.;
RT "Structure of the complex between adenylate kinase from Escherichia coli
RT and the inhibitor Ap5A refined at 1.9-A resolution. A model for a catalytic
RT transition state.";
RL J. Mol. Biol. 224:159-177(1992).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS PRO-9 AND GLY-10 IN
RP COMPLEX WITH THE INHIBITOR AP5A.
RX PubMed=8451239; DOI=10.1002/prot.340150106;
RA Mueller C.W., Schulz G.E.;
RT "Crystal structures of two mutants of adenylate kinase from Escherichia
RT coli that modify the Gly-loop.";
RL Proteins 15:42-49(1993).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH AMP AND AMPPNP.
RX PubMed=7937733; DOI=10.1002/prot.340190304;
RA Berry M.B., Meador B., Bilderback T., Liang P., Glaser M.,
RA Phillips G.N. Jr.;
RT "The closed conformation of a highly flexible protein: the structure of E.
RT coli adenylate kinase with bound AMP and AMPPNP.";
RL Proteins 19:183-198(1994).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RC STRAIN=K12;
RX PubMed=8805521; DOI=10.1016/s0969-2126(96)00018-4;
RA Mueller C.W., Schlauderer G.J., Reinstein J., Schulz G.E.;
RT "Adenylate kinase motions during catalysis: an energetic counterweight
RT balancing substrate binding.";
RL Structure 4:147-156(1996).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ADP AND AMP.
RX PubMed=16302237; DOI=10.1002/prot.20699;
RA Berry M.B., Bae E., Bilderback T.R., Glaser M., Phillips G.N. Jr.;
RT "Crystal structure of ADP/AMP complex of Escherichia coli adenylate
RT kinase.";
RL Proteins 62:555-556(2006).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG
RP AP5A.
RX PubMed=19805185; DOI=10.1073/pnas.0906510106;
RA Schrank T.P., Bolen D.W., Hilser V.J.;
RT "Rational modulation of conformational fluctuations in adenylate kinase
RT reveals a local unfolding mechanism for allostery and functional adaptation
RT in proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16984-16989(2009).
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:166976, ECO:0000269|PubMed:6243627}.
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:10398370};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=51 uM for ATP (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10398370};
CC KM=38 uM for AMP (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10398370};
CC KM=92 uM for ADP (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:10398370};
CC Vmax=1020 umol/min/mg enzyme for the forward reaction (at pH 7.4 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:10398370};
CC Vmax=605 umol/min/mg enzyme for the reverse reaction (at pH 7.4 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:10398370};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. Thermostable. Is half-
CC inactivated at 52 degrees Celsius. {ECO:0000269|PubMed:10398370};
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 ECO:0000269|PubMed:16302237, ECO:0000269|PubMed:19805185,
CC ECO:0000269|PubMed:8451239}.
CC -!- INTERACTION:
CC P69441; P0A8T7: rpoC; NbExp=2; IntAct=EBI-543592, EBI-543604;
CC P69441; P77806: ybdL; NbExp=3; IntAct=EBI-543592, EBI-543661;
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 ECO:0000305|PubMed:8805521}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00235}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40228.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X03038; CAA26840.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40228.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73576.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76253.1; -; Genomic_DNA.
DR EMBL; M38777; AAA23461.1; -; Genomic_DNA.
DR EMBL; D90259; BAA14303.1; -; Genomic_DNA.
DR PIR; A24275; KIECA.
DR RefSeq; NP_415007.1; NC_000913.3.
DR RefSeq; WP_001220233.1; NZ_STEB01000007.1.
DR PDB; 1AKE; X-ray; 2.00 A; A/B=1-214.
DR PDB; 1ANK; X-ray; 2.00 A; A/B=1-214.
DR PDB; 1E4V; X-ray; 1.85 A; A/B=1-214.
DR PDB; 1E4Y; X-ray; 1.85 A; A/B=1-214.
DR PDB; 2ECK; X-ray; 2.80 A; A/B=1-214.
DR PDB; 3HPQ; X-ray; 2.00 A; A/B=1-214.
DR PDB; 3HPR; X-ray; 2.00 A; A/B=1-214.
DR PDB; 4AKE; X-ray; 2.20 A; A/B=1-214.
DR PDB; 4X8H; X-ray; 2.50 A; A=1-214.
DR PDB; 4X8L; X-ray; 1.70 A; A/B=1-214.
DR PDB; 4X8M; X-ray; 2.60 A; A=1-214.
DR PDB; 4X8O; X-ray; 2.10 A; A/B=1-214.
DR PDB; 5EJE; X-ray; 1.90 A; A/B=1-214.
DR PDB; 6F7U; X-ray; 1.40 A; A=1-214.
DR PDB; 6HAM; X-ray; 2.55 A; A=1-214.
DR PDB; 6RZE; X-ray; 1.69 A; A=1-214.
DR PDB; 6S36; X-ray; 1.60 A; A=1-214.
DR PDB; 7APU; X-ray; 1.36 A; A/B=1-214.
DR PDBsum; 1AKE; -.
DR PDBsum; 1ANK; -.
DR PDBsum; 1E4V; -.
DR PDBsum; 1E4Y; -.
DR PDBsum; 2ECK; -.
DR PDBsum; 3HPQ; -.
DR PDBsum; 3HPR; -.
DR PDBsum; 4AKE; -.
DR PDBsum; 4X8H; -.
DR PDBsum; 4X8L; -.
DR PDBsum; 4X8M; -.
DR PDBsum; 4X8O; -.
DR PDBsum; 5EJE; -.
DR PDBsum; 6F7U; -.
DR PDBsum; 6HAM; -.
DR PDBsum; 6RZE; -.
DR PDBsum; 6S36; -.
DR PDBsum; 7APU; -.
DR AlphaFoldDB; P69441; -.
DR SMR; P69441; -.
DR BioGRID; 4261613; 20.
DR BioGRID; 849486; 1.
DR DIP; DIP-47903N; -.
DR IntAct; P69441; 13.
DR STRING; 511145.b0474; -.
DR DrugBank; DB01717; Bis(Adenosine)-5'-Pentaphosphate.
DR iPTMnet; P69441; -.
DR SWISS-2DPAGE; P69441; -.
DR jPOST; P69441; -.
DR PaxDb; P69441; -.
DR PRIDE; P69441; -.
DR EnsemblBacteria; AAC73576; AAC73576; b0474.
DR EnsemblBacteria; BAE76253; BAE76253; BAE76253.
DR GeneID; 60903750; -.
DR GeneID; 66671224; -.
DR GeneID; 945097; -.
DR KEGG; ecj:JW0463; -.
DR KEGG; eco:b0474; -.
DR PATRIC; fig|1411691.4.peg.1802; -.
DR EchoBASE; EB0031; -.
DR eggNOG; COG0563; Bacteria.
DR HOGENOM; CLU_032354_1_2_6; -.
DR InParanoid; P69441; -.
DR OMA; FHNRMRV; -.
DR PhylomeDB; P69441; -.
DR BioCyc; EcoCyc:ADENYL-KIN-MON; -.
DR BioCyc; MetaCyc:ADENYL-KIN-MON; -.
DR BRENDA; 2.7.4.3; 2026.
DR SABIO-RK; P69441; -.
DR UniPathway; UPA00588; UER00649.
DR EvolutionaryTrace; P69441; -.
DR PRO; PR:P69441; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:EcoCyc.
DR GO; GO:0016208; F:AMP binding; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:EcoCyc.
DR GO; GO:0006172; P:ADP biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0009132; P:nucleoside diphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0009123; P:nucleoside monophosphate metabolic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015951; P:purine ribonucleotide interconversion; IMP:EcoCyc.
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; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..214
FT /note="Adenylate kinase"
FT /id="PRO_0000158767"
FT REGION 30..59
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:8805521"
FT REGION 122..159
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:8805521"
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:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733,
FT ECO:0000269|PubMed:8451239"
FT BINDING 31
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733,
FT ECO:0000269|PubMed:8451239"
FT BINDING 36
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733,
FT ECO:0000269|PubMed:8451239"
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:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733,
FT ECO:0000269|PubMed:8451239"
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:1548697, ECO:0000269|PubMed:19805185,
FT ECO:0000269|PubMed:8451239"
FT BINDING 92
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733,
FT ECO:0000269|PubMed:8451239"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:16302237"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733,
FT ECO:0000269|PubMed:8451239"
FT BINDING 132..133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:8451239"
FT BINDING 156
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733,
FT ECO:0000269|PubMed:8451239"
FT BINDING 167
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:19805185,
FT ECO:0000269|PubMed:8451239"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT ECO:0000269|PubMed:1548697, ECO:0000269|PubMed:16302237,
FT ECO:0000269|PubMed:19805185, ECO:0000269|PubMed:7937733,
FT ECO:0000269|PubMed:8451239"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 9
FT /note="P->G: No loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:2223776,
FT ECO:0000269|PubMed:8451239"
FT MUTAGEN 10
FT /note="G->V: No loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:2223776,
FT ECO:0000269|PubMed:2844237, ECO:0000269|PubMed:8451239"
FT MUTAGEN 13
FT /note="K->Q: Drastic reduction in enzyme activity."
FT /evidence="ECO:0000269|PubMed:2223776,
FT ECO:0000269|PubMed:2844237"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:6F7U"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4X8L"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6F7U"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:6F7U"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:6F7U"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6F7U"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6F7U"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6F7U"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:6F7U"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 161..187
FT /evidence="ECO:0007829|PDB:6F7U"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6F7U"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:6F7U"
SQ SEQUENCE 214 AA; 23586 MW; BB917C84000A80EE CRC64;
MRIILLGAPG AGKGTQAQFI MEKYGIPQIS TGDMLRAAVK SGSELGKQAK DIMDAGKLVT
DELVIALVKE RIAQEDCRNG FLLDGFPRTI PQADAMKEAG INVDYVLEFD VPDELIVDRI
VGRRVHAPSG RVYHVKFNPP KVEGKDDVTG EELTTRKDDQ EETVRKRLVE YHQMTAPLIG
YYSKEAEAGN TKYAKVDGTK PVAEVRADLE KILG
