BUDC_CORGT
ID BUDC_CORGT Reviewed; 258 AA.
AC Q9ZNN8;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=L-2,3-butanediol dehydrogenase;
DE Short=L-BDH;
DE EC=1.1.1.76;
DE AltName: Full=(S,S)-butanediol dehydrogenase;
DE AltName: Full=Diacetyl reductase [(S)-acetoin forming] {ECO:0000303|Ref.1};
DE EC=1.1.1.304 {ECO:0000269|Ref.1};
GN Name=budC {ECO:0000303|Ref.1};
OS Corynebacterium glutamicum (Brevibacterium saccharolyticum).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=1718;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA36159.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, FUNCTION, AND
RP GENE NAME.
RC STRAIN=C-1012 {ECO:0000269|Ref.1};
RX DOI=10.1016/S0922-338X(98)80132-3;
RA Ui S., Otagiri M., Mimura A., Dohmae N., Takio K., Ohkuma M., Kudo T.;
RT "Cloning, expression and nucleotide sequence of the L-2,3-butanediol
RT dehydrogenase gene from Brevibacterium saccharolyticum C-1012.";
RL J. Ferment. Bioeng. 86:290-295(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, STEREOSPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=C-1012;
RX PubMed=11577733; DOI=10.1271/bbb.65.1876;
RA Takusagawa Y., Otagiri M., Ui S., Ohtsuki T., Mimura A., Ohkuma M.,
RA Kudo T.;
RT "Purification and characterization of L-2,3-butanediol dehydrogenase of
RT Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 65:1876-1878(2001).
RN [3] {ECO:0000305, ECO:0000312|PDB:3A28}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NAD,
RP STEREOSELECTIVITY, AND MUTAGENESIS OF ILE-142 AND PHE-148.
RX PubMed=19941855; DOI=10.1016/j.febslet.2009.11.068;
RA Otagiri M., Ui S., Takusagawa Y., Ohtsuki T., Kurisu G., Kusunoki M.;
RT "Structural basis for chiral substrate recognition by two 2,3-butanediol
RT dehydrogenases.";
RL FEBS Lett. 584:219-223(2010).
CC -!- FUNCTION: Catalyzes the reversible reduction of (S)-acetoin to (S,S)-
CC butane-2,3-diol (L-BD) in the presence of NADH. To a lesser extent, can
CC also catalyze the irreversible reduction of diacetyl to (S)-acetoin.
CC Cannot oxidize meso-BD, D-BD, 2-butanol, 1,2-propanediol, ethanol,
CC acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, and n-propanol.
CC Cannot reduce (R)-acetoin, acetol, dihydroxyacetone and 2,4-
CC pentanedione. {ECO:0000269|PubMed:11577733, ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S,S)-butane-2,3-diol + NAD(+) = (S)-acetoin + H(+) + NADH;
CC Xref=Rhea:RHEA:12184, ChEBI:CHEBI:15378, ChEBI:CHEBI:15687,
CC ChEBI:CHEBI:16812, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.76;
CC Evidence={ECO:0000269|PubMed:11577733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-acetoin + NAD(+) = diacetyl + H(+) + NADH;
CC Xref=Rhea:RHEA:27286, ChEBI:CHEBI:15378, ChEBI:CHEBI:15687,
CC ChEBI:CHEBI:16583, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.304; Evidence={ECO:0000269|PubMed:11577733,
CC ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Slightly activated by Ba(2+), Ca(2+), Mn(2+),
CC Mg(2+), and Co(2+), while Hg(2+) and Cu(2+) cause marked inhibition of
CC the activity. Ni(2+), Zn(2+) and Cd(2+) have no effect on the catalytic
CC activity. Is also slightly inhibited by lactate, pyruvate, succinate,
CC acetate and formate. {ECO:0000269|PubMed:11577733}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.10 mM for NADH (at pH 6.0) {ECO:0000269|PubMed:11577733};
CC KM=0.44 mM for (S)-acetoin (at pH 6.0) {ECO:0000269|PubMed:11577733};
CC KM=0.07 mM for NAD(+) (at pH 10.5) {ECO:0000269|PubMed:11577733};
CC KM=0.22 mM for (S,S)-butane-2,3-diol (at pH 10.5)
CC {ECO:0000269|PubMed:11577733};
CC pH dependence:
CC Optimum pH is 10.5 for the oxidative reaction with L-BD and 6.0 for
CC the reductive reaction with (S)-acetoin. Stable from pH 7.0 to 9.0.
CC {ECO:0000269|PubMed:11577733};
CC Temperature dependence:
CC Stable up to 37 degrees Celsius but is rapidly inactivated over 40
CC degrees Celsius. {ECO:0000269|PubMed:11577733};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11577733,
CC ECO:0000269|PubMed:19941855}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255}.
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DR EMBL; AB009078; BAA36159.1; -; Genomic_DNA.
DR PDB; 3A28; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-258.
DR PDB; 3WYE; X-ray; 1.58 A; A/B=86-120, A/B=137-163, A/B=184-238.
DR PDBsum; 3A28; -.
DR PDBsum; 3WYE; -.
DR AlphaFoldDB; Q9ZNN8; -.
DR SMR; Q9ZNN8; -.
DR KEGG; ag:BAA36159; -.
DR BRENDA; 1.1.1.76; 960.
DR EvolutionaryTrace; Q9ZNN8; -.
DR GO; GO:0047512; F:(S,S)-butanediol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0052588; F:diacetyl reductase ((S)-acetoin forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; IDA:UniProtKB.
DR GO; GO:0070404; F:NADH binding; IDA:UniProtKB.
DR GO; GO:0045150; P:acetoin catabolic process; IEA:InterPro.
DR GO; GO:0045149; P:acetoin metabolic process; IDA:UniProtKB.
DR GO; GO:0034077; P:butanediol metabolic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR InterPro; IPR014007; 23BDH.
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 TIGRFAMs; TIGR02415; 23BDH; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase.
FT CHAIN 1..258
FT /note="L-2,3-butanediol dehydrogenase"
FT /id="PRO_0000418972"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q48436,
FT ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 12..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19941855"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19941855"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19941855"
FT BINDING 61..62
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19941855"
FT BINDING 88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19941855"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19941855"
FT BINDING 158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19941855"
FT BINDING 184..189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:19941855"
FT MUTAGEN 142
FT /note="I->Q: Loss of L-BD oxidizing activity, and does not
FT gain the ability to use meso-BD as substrate; when
FT associated with N-148."
FT /evidence="ECO:0000269|PubMed:19941855"
FT MUTAGEN 142
FT /note="I->Q: Loss of L-BD oxidizing activity. Does not gain
FT the ability to use meso-BD as substrate."
FT /evidence="ECO:0000269|PubMed:19941855"
FT MUTAGEN 148
FT /note="F->N: Loss of L-BD oxidizing activity, and does not
FT gain the ability to use meso-BD as substrate; when
FT associated with Q-142."
FT /evidence="ECO:0000269|PubMed:19941855"
FT MUTAGEN 148
FT /note="F->N: Loss of L-BD oxidizing activity. Does not gain
FT the ability to use meso-BD as substrate."
FT /evidence="ECO:0000269|PubMed:19941855"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3A28"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3A28"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:3A28"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3A28"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3A28"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:3A28"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:3A28"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:3A28"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:3A28"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3A28"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:3WYE"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3A28"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3A28"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:3A28"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:3WYE"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 226..237
FT /evidence="ECO:0007829|PDB:3WYE"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3A28"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:3A28"
SQ SEQUENCE 258 AA; 27108 MW; 96A81BD2AE33E55E CRC64;
MSKVAMVTGG AQGIGRGISE KLAADGFDIA VADLPQQEEQ AAETIKLIEA ADQKAVFVGL
DVTDKANFDS AIDEAAEKLG GFDVLVNNAG IAQIKPLLEV TEEDLKQIYS VNVFSVFFGI
QAASRKFDEL GVKGKIINAA SIAAIQGFPI LSAYSTTKFA VRGLTQAAAQ ELAPKGHTVN
AYAPGIVGTG MWEQIDAELS KINGKPIGEN FKEYSSSIAL GRPSVPEDVA GLVSFLASEN
SNYVTGQVML VDGGMLYN
