HDHA_ECOLI
ID HDHA_ECOLI Reviewed; 255 AA.
AC P0AET8; P25529;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=7alpha-hydroxysteroid dehydrogenase {ECO:0000303|PubMed:2007545};
DE Short=7alpha-HSDH {ECO:0000303|PubMed:2007545};
DE EC=1.1.1.159 {ECO:0000269|PubMed:2007545, ECO:0000269|PubMed:9722677};
DE AltName: Full=NAD-dependent 7alpha-hydroxysteroid dehydrogenase {ECO:0000305|PubMed:2007545};
GN Name=hdhA; Synonyms=hsdH {ECO:0000303|PubMed:2007545};
GN OrderedLocusNames=b1619, JW1611;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 33694 / HB101;
RX PubMed=2007545; DOI=10.1128/jb.173.7.2173-2179.1991;
RA Yoshimoto T., Higashi H., Kanatani A., Lin X.S., Nagai H., Oyama H.,
RA Kurazono K., Tsuru D.;
RT "Cloning and sequencing of the 7 alpha-hydroxysteroid dehydrogenase gene
RT from Escherichia coli HB101 and characterization of the expressed enzyme.";
RL J. Bacteriol. 173:2173-2179(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 169-255.
RA Jefferson R.A.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0007744|PDB:1AHH, ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH
RP GLYCOCHENODEOXYCHOLATE AND NAD, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP REACTION MECHANISM, AND ACTIVE SITE.
RC STRAIN=ATCC 33694 / HB101;
RX PubMed=8672472; DOI=10.1021/bi951904d;
RA Tanaka N., Nonaka T., Tanabe T., Yoshimoto T., Tsuru D., Mitsui Y.;
RT "Crystal structures of the binary and ternary complexes of 7 alpha-
RT hydroxysteroid dehydrogenase from Escherichia coli.";
RL Biochemistry 35:7715-7730(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND MUTANTS PHE-159;
RP HIS-159 AND ARG-163, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF SER-146; TYR-159 AND LYS-163, REACTION MECHANISM, AND ACTIVE
RP SITE.
RX PubMed=9722677; DOI=10.1093/oxfordjournals.jbchem.a022159;
RA Tanabe T., Tanaka N., Uchikawa K., Kabashima T., Ito K., Nonaka T.,
RA Mitsui Y., Tsuru M., Yoshimoto T.;
RT "Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action
RT of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli.";
RL J. Biochem. 124:634-641(1998).
CC -!- FUNCTION: 7alpha-hydroxysteroid dehydrogenase involved in the
CC metabolism of bile acids. Catalyzes the NAD(+)-dependent oxidation of
CC the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as the major
CC human bile acids cholate and chenodeoxycholate, to the corresponding 7-
CC oxosteroids. To a lesser extent, can also act on
CC taurochenodeoxycholate, taurocholate and glycocholate (PubMed:2007545).
CC Can also use glycochenodeoxycholate as substrate (PubMed:8672472). Is
CC not able to use NADP(+) instead of NAD(+) as the electron acceptor
CC (PubMed:2007545). {ECO:0000269|PubMed:2007545,
CC ECO:0000269|PubMed:8672472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholate + NAD(+) = 3alpha,12alpha-dihydroxy-7-oxo-5beta-
CC cholanate + H(+) + NADH; Xref=Rhea:RHEA:19409, ChEBI:CHEBI:11893,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.1.1.159;
CC Evidence={ECO:0000269|PubMed:2007545, ECO:0000269|PubMed:9722677};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19410;
CC Evidence={ECO:0000305|PubMed:2007545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholate + NAD(+) = 7-oxolithocholate + H(+) + NADH;
CC Xref=Rhea:RHEA:42036, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78605;
CC Evidence={ECO:0000269|PubMed:2007545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42037;
CC Evidence={ECO:0000305|PubMed:2007545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + taurochenodeoxycholate = 7-oxotaurolithocholate +
CC H(+) + NADH; Xref=Rhea:RHEA:53824, ChEBI:CHEBI:9407,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:137724; Evidence={ECO:0000269|PubMed:2007545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53825;
CC Evidence={ECO:0000305|PubMed:2007545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + taurocholate = 7-oxo-taurodeoxycholate + H(+) + NADH;
CC Xref=Rhea:RHEA:53848, ChEBI:CHEBI:15378, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137820;
CC Evidence={ECO:0000269|PubMed:2007545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53849;
CC Evidence={ECO:0000305|PubMed:2007545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycocholate + NAD(+) = 7-oxo-glycodeoxycholate + H(+) + NADH;
CC Xref=Rhea:RHEA:53852, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137824;
CC Evidence={ECO:0000269|PubMed:2007545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53853;
CC Evidence={ECO:0000305|PubMed:2007545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycochenodeoxycholate + NAD(+) = 7-oxoglycolithocholate +
CC H(+) + NADH; Xref=Rhea:RHEA:53844, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36252, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:137818; Evidence={ECO:0000269|PubMed:8672472};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53845;
CC Evidence={ECO:0000305|PubMed:8672472};
CC -!- ACTIVITY REGULATION: Inhibited by N-bromosuccinimide, diethyl
CC pyrocarbonate, and some metal ions such as Co(2+), Fe(2+) and Cu(2+).
CC {ECO:0000269|PubMed:2007545}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.19 mM for taurochenodeoxycholate {ECO:0000269|PubMed:2007545};
CC KM=0.43 mM for chenodeoxycholate {ECO:0000269|PubMed:2007545};
CC KM=1.2 mM for cholate {ECO:0000269|PubMed:2007545};
CC KM=1.25 mM for glycocholate {ECO:0000269|PubMed:2007545};
CC KM=2.0 mM for taurocholate {ECO:0000269|PubMed:2007545};
CC KM=0.279 mM for NAD(+) {ECO:0000269|PubMed:9722677};
CC KM=0.361 mM for cholate {ECO:0000269|PubMed:9722677};
CC Note=kcat is 3798 sec(-1) with cholate as substrate (PubMed:2007545).
CC kcat is 491 sec(-1) with chenodeoxycholate as substrate
CC (PubMed:2007545). kcat is 206 sec(-1) with taurochenodeoxycholate as
CC substrate (PubMed:2007545). kcat is 188 sec(-1) with taurocholate as
CC substrate (PubMed:2007545). kcat is 25 sec(-1) with glycocholate as
CC substrate (PubMed:2007545). kcat is 151 sec(-1) with cholate as
CC substrate (PubMed:9722677). {ECO:0000269|PubMed:2007545,
CC ECO:0000269|PubMed:9722677};
CC pH dependence:
CC Optimum pH is 8.5 (PubMed:2007545). The enzyme is stable between pH 8
CC and 9 (PubMed:2007545). {ECO:0000269|PubMed:2007545};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:2007545,
CC ECO:0000269|PubMed:8672472}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; D10497; BAA01384.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74691.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15370.1; -; Genomic_DNA.
DR EMBL; M14641; AAA68921.1; -; Genomic_DNA.
DR PIR; A38527; A38527.
DR RefSeq; NP_416136.1; NC_000913.3.
DR RefSeq; WP_000483353.1; NZ_STEB01000003.1.
DR PDB; 1AHH; X-ray; 2.30 A; A/B=1-255.
DR PDB; 1AHI; X-ray; 2.30 A; A/B=1-255.
DR PDB; 1FMC; X-ray; 1.80 A; A/B=1-255.
DR PDB; 7ENY; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1-255.
DR PDBsum; 1AHH; -.
DR PDBsum; 1AHI; -.
DR PDBsum; 1FMC; -.
DR PDBsum; 7ENY; -.
DR AlphaFoldDB; P0AET8; -.
DR SMR; P0AET8; -.
DR BioGRID; 4259598; 31.
DR DIP; DIP-9875N; -.
DR IntAct; P0AET8; 5.
DR STRING; 511145.b1619; -.
DR DrugBank; DB02123; Glycochenodeoxycholic Acid.
DR SwissLipids; SLP:000001736; -.
DR SWISS-2DPAGE; P0AET8; -.
DR jPOST; P0AET8; -.
DR PaxDb; P0AET8; -.
DR PRIDE; P0AET8; -.
DR EnsemblBacteria; AAC74691; AAC74691; b1619.
DR EnsemblBacteria; BAA15370; BAA15370; BAA15370.
DR GeneID; 946151; -.
DR KEGG; ag:BAA01384; -.
DR KEGG; ecj:JW1611; -.
DR KEGG; eco:b1619; -.
DR PATRIC; fig|1411691.4.peg.642; -.
DR EchoBASE; EB0420; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_3_6; -.
DR InParanoid; P0AET8; -.
DR OMA; VYLCCKA; -.
DR PhylomeDB; P0AET8; -.
DR BioCyc; EcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MON; -.
DR BioCyc; MetaCyc:7-ALPHA-HYDROXYSTEROID-DEH-MON; -.
DR BRENDA; 1.1.1.159; 2026.
DR EvolutionaryTrace; P0AET8; -.
DR PRO; PR:P0AET8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0106281; F:chenodeoxycholate 7-alpha-dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0008709; F:cholate 7-alpha-dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0030573; P:bile acid catabolic process; IDA:EcoCyc.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bile acid catabolism; Direct protein sequencing;
KW Lipid degradation; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome; Steroid metabolism.
FT CHAIN 1..255
FT /note="7alpha-hydroxysteroid dehydrogenase"
FT /id="PRO_0000054708"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:8672472,
FT ECO:0000305|PubMed:9722677"
FT BINDING 23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC"
FT BINDING 42..43
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHH, ECO:0007744|PDB:1AHI,
FT ECO:0007744|PDB:1FMC"
FT BINDING 68..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHH, ECO:0007744|PDB:1AHI,
FT ECO:0007744|PDB:1FMC"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHH, ECO:0007744|PDB:1AHI,
FT ECO:0007744|PDB:1FMC"
FT BINDING 99
FT /ligand="glycochenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36252"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC"
FT BINDING 146
FT /ligand="glycochenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36252"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC"
FT BINDING 151
FT /ligand="glycochenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36252"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC"
FT BINDING 159
FT /ligand="glycochenodeoxycholate"
FT /ligand_id="ChEBI:CHEBI:36252"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHI, ECO:0007744|PDB:1FMC"
FT BINDING 163
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHH, ECO:0007744|PDB:1AHI,
FT ECO:0007744|PDB:1FMC"
FT BINDING 192..194
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8672472,
FT ECO:0007744|PDB:1AHH, ECO:0007744|PDB:1AHI,
FT ECO:0007744|PDB:1FMC"
FT SITE 146
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:8672472,
FT ECO:0000305|PubMed:9722677"
FT SITE 163
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000305|PubMed:8672472,
FT ECO:0000305|PubMed:9722677"
FT MUTAGEN 146
FT /note="S->A,H: Reduction of the catalytic efficiency by
FT over 65%. No effect on the affinity for cholate and NAD."
FT /evidence="ECO:0000269|PubMed:9722677"
FT MUTAGEN 159
FT /note="Y->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9722677"
FT MUTAGEN 159
FT /note="Y->H: Reduction of the catalytic efficiency by
FT 87.7%. No effect on the affinity for cholate and NAD."
FT /evidence="ECO:0000269|PubMed:9722677"
FT MUTAGEN 163
FT /note="K->I: Reduction of the catalytic efficiency by 95%.
FT No effect on the affinity for cholate and NAD."
FT /evidence="ECO:0000269|PubMed:9722677"
FT MUTAGEN 163
FT /note="K->R: Reduction of the catalytic efficiency by 35%.
FT No effect on the affinity for cholate and NAD."
FT /evidence="ECO:0000269|PubMed:9722677"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:1FMC"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:1FMC"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1FMC"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1FMC"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:1FMC"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:1FMC"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:1FMC"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 157..178
FT /evidence="ECO:0007829|PDB:1FMC"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1FMC"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:1FMC"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1FMC"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:1FMC"
SQ SEQUENCE 255 AA; 26779 MW; 66CF70E85BD67B6D CRC64;
MFNSDNLRLD GKCAIITGAG AGIGKEIAIT FATAGASVVV SDINADAANH VVDEIQQLGG
QAFACRCDIT SEQELSALAD FAISKLGKVD ILVNNAGGGG PKPFDMPMAD FRRAYELNVF
SFFHLSQLVA PEMEKNGGGV ILTITSMAAE NKNINMTSYA SSKAAASHLV RNMAFDLGEK
NIRVNGIAPG AILTDALKSV ITPEIEQKML QHTPIRRLGQ PQDIANAALF LCSPAASWVS
GQILTVSGGG VQELN
