SUCC_ECOLI
ID SUCC_ECOLI Reviewed; 388 AA.
AC P0A836; P07460;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10353839, ECO:0000269|PubMed:7040388};
DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558};
GN OrderedLocusNames=b0728, JW0717;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3002435; DOI=10.1021/bi00343a031;
RA Buck D., Spencer M.E., Guest J.R.;
RT "Primary structure of the succinyl-CoA synthetase of Escherichia coli.";
RL Biochemistry 24:6245-6252(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 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 [6]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=7040388; DOI=10.1016/s0021-9258(18)34601-5;
RA Vogel H.J., Bridger W.A.;
RT "A phosphorus 31 nuclear magnetic resonance study of the intermediates of
RT the Escherichia coli succinyl coenzyme A synthetase reaction. Evidence for
RT substrate synergism and catalytic cooperativity.";
RL J. Biol. Chem. 257:4834-4842(1982).
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10353839; DOI=10.1021/bi990527s;
RA Joyce M.A., Fraser M.E., Brownie E.R., James M.N., Bridger W.A.,
RA Wolodko W.T.;
RT "Probing the nucleotide-binding site of Escherichia coli succinyl-CoA
RT synthetase.";
RL Biochemistry 38:7273-7283(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUCD, CATALYTIC
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8144675; DOI=10.2210/pdb1scu/pdb;
RA Wolodko W.T., Fraser M.E., James M.N.G., Bridger W.A.;
RT "The crystal structure of succinyl-CoA synthetase from Escherichia coli at
RT 2.5-A resolution.";
RL J. Biol. Chem. 269:10883-10890(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH SUCD.
RX PubMed=9917402; DOI=10.1006/jmbi.1998.2324;
RA Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.;
RT "A detailed structural description of Escherichia coli succinyl-CoA
RT synthetase.";
RL J. Mol. Biol. 285:1633-1653(1999).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH SUCD; ADP AND
RP MAGNESIUM.
RX PubMed=10625475; DOI=10.1021/bi991696f;
RA Joyce M.A., Fraser M.E., James M.N., Bridger W.A., Wolodko W.T.;
RT "ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by
RT X-ray crystallography.";
RL Biochemistry 39:17-25(2000).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF MUTANT ALA-197 IN COMPLEX WITH
RP SUCD.
RX PubMed=11781092; DOI=10.1021/bi011518y;
RA Fraser M.E., Joyce M.A., Ryan D.G., Wolodko W.T.;
RT "Two glutamate residues, Glu 208 alpha and Glu 197 beta, are crucial for
RT phosphorylation and dephosphorylation of the active-site histidine residue
RT in succinyl-CoA synthetase.";
RL Biochemistry 41:537-546(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH SUCD.
RX PubMed=17642514; DOI=10.1107/s0907444907029319;
RA Hidber E., Brownie E.R., Hayakawa K., Fraser M.E.;
RT "Participation of Cys123alpha of Escherichia coli succinyl-CoA synthetase
RT in catalysis.";
RL Acta Crystallogr. D 63:876-884(2007).
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC either ATP or GTP and thus represents the only step of substrate-level
CC phosphorylation in the TCA. The beta subunit provides nucleotide
CC specificity of the enzyme and binds the substrate succinate, while the
CC binding sites for coenzyme A and phosphate are found in the alpha
CC subunit. Can use either ATP or GTP, but prefers ATP. It can also
CC function in the other direction for anabolic purposes, and this may be
CC particularly important for providing succinyl-CoA during anaerobic
CC growth when the oxidative route from 2-oxoglutarate is severely
CC repressed. {ECO:0000255|HAMAP-Rule:MF_00558,
CC ECO:0000269|PubMed:10353839}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00558, ECO:0000269|PubMed:10353839,
CC ECO:0000269|PubMed:7040388};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558,
CC ECO:0000269|PubMed:10625475, ECO:0000269|PubMed:7040388};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00558,
CC ECO:0000269|PubMed:10625475};
CC -!- ACTIVITY REGULATION: Exhibits two interesting properties: 'substrate
CC synergism', in which the enzyme is most active for the catalysis of its
CC partial reactions only when all the substrate-binding sites are
CC occupied, and 'catalytic cooperativity' between alternating active
CC sites in the tetramer, whereby the interaction of substrates
CC (particularly ATP) at one site is needed to promote catalysis at the
CC other.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 uM for ATP {ECO:0000269|PubMed:10353839};
CC KM=394 uM for GTP {ECO:0000269|PubMed:10353839};
CC Note=kcat is 2684 min(-1) with ATP as substrate and 1471 min(-1) with
CC GTP as substrate. {ECO:0000269|PubMed:10353839};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:8144675};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00558, ECO:0000305|PubMed:10353839}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:8144675,
CC ECO:0000269|PubMed:9917402}.
CC -!- INTERACTION:
CC P0A836; P0AGE9: sucD; NbExp=4; IntAct=EBI-369117, EBI-369078;
CC -!- MISCELLANEOUS: Succinyl-CoA synthetase (SCS) of E.coli catalyzes its
CC reaction via three steps that involve phosphoryl enzyme and enzyme-
CC bound succinyl phosphate as intermediates.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00558}.
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DR EMBL; J01619; AAA23899.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73822.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35394.1; -; Genomic_DNA.
DR PIR; A24090; SYECSB.
DR RefSeq; NP_415256.1; NC_000913.3.
DR RefSeq; WP_001048602.1; NZ_STEB01000035.1.
DR PDB; 1CQI; X-ray; 3.30 A; B/E=1-385.
DR PDB; 1CQJ; X-ray; 2.90 A; B/E=1-385.
DR PDB; 1JKJ; X-ray; 2.35 A; B/E=1-388.
DR PDB; 1JLL; X-ray; 2.69 A; B/E=1-388.
DR PDB; 1SCU; X-ray; 2.50 A; B/E=1-388.
DR PDB; 2NU6; X-ray; 2.55 A; B/E=1-388.
DR PDB; 2NU7; X-ray; 2.20 A; B/E=1-388.
DR PDB; 2NU8; X-ray; 2.15 A; B/E=1-388.
DR PDB; 2NU9; X-ray; 2.90 A; B/E/G/I=1-388.
DR PDB; 2NUA; X-ray; 2.95 A; B/E=1-388.
DR PDB; 2SCU; X-ray; 2.30 A; B/E=1-388.
DR PDBsum; 1CQI; -.
DR PDBsum; 1CQJ; -.
DR PDBsum; 1JKJ; -.
DR PDBsum; 1JLL; -.
DR PDBsum; 1SCU; -.
DR PDBsum; 2NU6; -.
DR PDBsum; 2NU7; -.
DR PDBsum; 2NU8; -.
DR PDBsum; 2NU9; -.
DR PDBsum; 2NUA; -.
DR PDBsum; 2SCU; -.
DR AlphaFoldDB; P0A836; -.
DR SMR; P0A836; -.
DR BioGRID; 4259946; 19.
DR ComplexPortal; CPX-1092; Succinyl-CoA synthetase.
DR DIP; DIP-31852N; -.
DR IntAct; P0A836; 30.
DR STRING; 511145.b0728; -.
DR CarbonylDB; P0A836; -.
DR SWISS-2DPAGE; P0A836; -.
DR jPOST; P0A836; -.
DR PaxDb; P0A836; -.
DR PRIDE; P0A836; -.
DR EnsemblBacteria; AAC73822; AAC73822; b0728.
DR EnsemblBacteria; BAA35394; BAA35394; BAA35394.
DR GeneID; 66671003; -.
DR GeneID; 945312; -.
DR KEGG; ecj:JW0717; -.
DR KEGG; eco:b0728; -.
DR PATRIC; fig|1411691.4.peg.1545; -.
DR EchoBASE; EB0974; -.
DR eggNOG; COG0045; Bacteria.
DR HOGENOM; CLU_037430_4_0_6; -.
DR InParanoid; P0A836; -.
DR OMA; ITACDEV; -.
DR PhylomeDB; P0A836; -.
DR BioCyc; EcoCyc:SUCCCOASYN-BETA; -.
DR BioCyc; MetaCyc:SUCCCOASYN-BETA; -.
DR BRENDA; 6.2.1.5; 2165.
DR UniPathway; UPA00223; UER00999.
DR EvolutionaryTrace; P0A836; -.
DR PRO; PR:P0A836; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042709; C:succinate-CoA ligase complex; IBA:GO_Central.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IMP:EcoliWiki.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IMP:EcoliWiki.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11815; PTHR11815; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..388
FT /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT /id="PRO_0000102832"
FT DOMAIN 9..244
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558,
FT ECO:0000269|PubMed:10625475"
FT BINDING 53..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558,
FT ECO:0000269|PubMed:10625475"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558,
FT ECO:0000269|PubMed:10625475"
FT BINDING 102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558,
FT ECO:0000269|PubMed:10625475"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558,
FT ECO:0000269|PubMed:10625475"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558,
FT ECO:0000269|PubMed:10625475"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558,
FT ECO:0000269|PubMed:10625475"
FT BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT BINDING 321..323
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT MUTAGEN 197
FT /note="E->A: Prevents phosphorylation of the enzyme
FT intermediate in both reaction directions."
FT /evidence="ECO:0000269|PubMed:11781092"
FT MUTAGEN 197
FT /note="E->Q: Prevents phosphorylation of the enzyme
FT intermediate by ATP."
FT /evidence="ECO:0000269|PubMed:11781092"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2NU8"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 104..115
FT /evidence="ECO:0007829|PDB:2NU8"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2NU8"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 172..190
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 193..204
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2SCU"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1JLL"
FT HELIX 325..339
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 354..362
FT /evidence="ECO:0007829|PDB:2NU8"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:2NU8"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:2NU8"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:2NU8"
SQ SEQUENCE 388 AA; 41393 MW; 09C429EC97A823CF CRC64;
MNLHEYQAKQ LFARYGLPAP VGYACTTPRE AEEAASKIGA GPWVVKCQVH AGGRGKAGGV
KVVNSKEDIR AFAENWLGKR LVTYQTDANG QPVNQILVEA ATDIAKELYL GAVVDRSSRR
VVFMASTEGG VEIEKVAEET PHLIHKVALD PLTGPMPYQG RELAFKLGLE GKLVQQFTKI
FMGLATIFLE RDLALIEINP LVITKQGDLI CLDGKLGADG NALFRQPDLR EMRDQSQEDP
REAQAAQWEL NYVALDGNIG CMVNGAGLAM GTMDIVKLHG GEPANFLDVG GGATKERVTE
AFKIILSDDK VKAVLVNIFG GIVRCDLIAD GIIGAVAEVG VNVPVVVRLE GNNAELGAKK
LADSGLNIIA AKGLTDAAQQ VVAAVEGK
