ADH_MORSE
ID ADH_MORSE Reviewed; 338 AA.
AC Q8GIX7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Alcohol dehydrogenase {ECO:0000303|PubMed:16511007, ECO:0000303|PubMed:32596590};
DE Short=ADH {ECO:0000303|PubMed:16511007, ECO:0000303|PubMed:32596590};
DE EC=1.1.1.1 {ECO:0000269|PubMed:32596590, ECO:0000269|PubMed:9660191};
GN Name=adh {ECO:0000312|EMBL:CAD29583.1};
OS Moraxella sp. (strain TAE123).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella; unclassified Moraxella.
OX NCBI_TaxID=191545;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TAE123;
RA Tsigos I., Bouriotis V.;
RT "Cold adapted alcohol dehydrogenase from an Antarctic psychrophilic
RT bacterium.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=TAE123;
RX PubMed=9660191; DOI=10.1046/j.1432-1327.1998.2540356.x;
RA Tsigos I., Velonia K., Smonou I., Bouriotis V.;
RT "Purification and characterization of an alcohol dehydrogenase from the
RT Antarctic psychrophile Moraxella sp. TAE123.";
RL Eur. J. Biochem. 254:356-362(1998).
RN [3]
RP IDENTIFICATION AS A TYPE-A DEHYDROGENASE.
RC STRAIN=TAE123;
RX PubMed=9990458; DOI=10.1016/s0960-894x(98)00678-7;
RA Velonia K., Tsigos I., Bouriotis V., Smonou I.;
RT "Stereospecificity of hydrogen transfer by the NAD+-linked alcohol
RT dehydrogenase from the antarctic psychrophile Moraxella sp. TAE123.";
RL Bioorg. Med. Chem. Lett. 9:65-68(1999).
RN [4]
RP SUBUNIT, COFACTOR, AND CRYSTALLIZATION.
RC STRAIN=TAE123;
RX PubMed=16511007; DOI=10.1107/s1744309105002253;
RA Papanikolau Y., Tsigos I., Papadovasilaki M., Bouriotis V., Petratos K.;
RT "Crystallization and preliminary X-ray diffraction studies of an alcohol
RT dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123.";
RL Acta Crystallogr. F 61:246-248(2005).
RN [5] {ECO:0007744|PDB:4Z6K}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND DOMAIN.
RC STRAIN=TAE123;
RX PubMed=32596590; DOI=10.1021/acsomega.0c01210;
RA Petratos K., Gessmann R., Daskalakis V., Papadovasilaki M., Papanikolau Y.,
RA Tsigos I., Bouriotis V.;
RT "Structure and Dynamics of a Thermostable Alcohol Dehydrogenase from the
RT Antarctic Psychrophile Moraxella sp. TAE123.";
RL ACS Omega 5:14523-14534(2020).
CC -!- FUNCTION: Psychrophilic alcohol dehydrogenase that exhibits a wide
CC range of substrate specificity, oxidizing mainly primary and secondary
CC aliphatic alcohols, utilizing NAD(+) as a cosubstrate. In vitro, shows
CC highest reaction rates for ethanol as a substrate and gradually
CC decreases its reaction rates as the length and branching of the carbon
CC chain of the alcohol substrates increase. To a lesser extent, is also
CC able to reduce aldehydes and ketones. Do not catalyze the further
CC oxidation of aldehydes to carboxylic acids. Cannot use NADP(+) instead
CC of NAD(+). {ECO:0000269|PubMed:9660191}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:32596590, ECO:0000269|PubMed:9660191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10737;
CC Evidence={ECO:0000305|PubMed:9660191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:9660191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10741;
CC Evidence={ECO:0000305|PubMed:9660191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:32596590, ECO:0000269|PubMed:9660191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25291;
CC Evidence={ECO:0000305|PubMed:9660191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-propanol + NAD(+) = H(+) + NADH + propanal;
CC Xref=Rhea:RHEA:50704, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:28831, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:9660191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50705;
CC Evidence={ECO:0000305|PubMed:9660191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butan-1-ol + NAD(+) = butanal + H(+) + NADH;
CC Xref=Rhea:RHEA:33199, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743,
CC ChEBI:CHEBI:28885, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:9660191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33200;
CC Evidence={ECO:0000305|PubMed:9660191};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + propan-2-ol = acetone + H(+) + NADH;
CC Xref=Rhea:RHEA:41984, ChEBI:CHEBI:15347, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17824, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:9660191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41985;
CC Evidence={ECO:0000305|PubMed:9660191};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16511007, ECO:0000269|PubMed:32596590};
CC Note=Binds 2 Zn(2+) ions per subunit. One metal ion is located at the
CC active-site region and has been termed catalytic, while the second
CC metal ion has been termed structural. {ECO:0000269|PubMed:16511007,
CC ECO:0000269|PubMed:32596590};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for ethanol (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9660191};
CC KM=0.51 mM for propan-1-ol (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9660191};
CC KM=0.52 mM for butan-1-ol (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9660191};
CC KM=1.32 mM for propan-2-ol (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9660191};
CC KM=1.16 mM for acetone (at pH 6.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9660191};
CC KM=0.18 mM for NAD(+) (at pH 7.4 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9660191};
CC KM=0.23 mM for NADH (at pH 6.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:9660191};
CC KM=0.7 mM for ethanol (at pH 7.4 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:32596590};
CC Vmax=2.64 umol/min/mg enzyme for the oxidation of ethanol (at pH 7.4
CC and 25 degrees Celsius) {ECO:0000269|PubMed:9660191};
CC Vmax=2.35 umol/min/mg enzyme for the oxidation of propan-1-ol (at pH
CC 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:9660191};
CC Vmax=2.34 umol/min/mg enzyme for the oxidation of butan-1-ol (at pH
CC 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:9660191};
CC Vmax=1.84 umol/min/mg enzyme for the oxidation of propan-2-ol (at pH
CC 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:9660191};
CC Vmax=1.97 umol/min/mg enzyme for the reduction of acetone (at pH 6.0
CC and 25 degrees Celsius) {ECO:0000269|PubMed:9660191};
CC Note=kcat is 549.1 min(-1) for the oxidation of ethanol (at pH 7.4
CC and 30 degrees Celsius). kcat is 488.8 min(-1) for the oxidation of
CC propan-1-ol (at pH 7.4 and 30 degrees Celsius). kcat is 486.7 min(-1)
CC for the oxidation of butan-1-ol (at pH 7.4 and 30 degrees Celsius).
CC kcat is 382.7 min(-1) for the oxidation of propan-2-ol (at pH 7.4 and
CC 30 degrees Celsius). kcat is 409.8 min(-1) for the reduction of
CC acetone (at pH 6.0 and 30 degrees Celsius) (PubMed:9660191). kcat is
CC 9.4 sec(-1) for the oxidation of ethanol (at pH 7.4 and 30 degrees
CC Celsius) (PubMed:32596590). {ECO:0000269|PubMed:32596590,
CC ECO:0000269|PubMed:9660191};
CC pH dependence:
CC Optimum pH is 7.4 and 6.0 for the oxidation of ethanol and reduction
CC of acetone, respectively. {ECO:0000269|PubMed:9660191};
CC Temperature dependence:
CC Is a very thermostable, cold-adapted enzyme. Is active from 10 to at
CC least 53 degrees Celsius and unfolds at 89 degrees Celsius.
CC {ECO:0000269|PubMed:32596590};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16511007,
CC ECO:0000269|PubMed:32596590, ECO:0000269|PubMed:9660191}.
CC -!- DOMAIN: Each subunit comprises two distinct structural domains: the
CC catalytic domain (residues 1-150 and 288-340/345) and the nucleotide-
CC binding domain (residues 151-287). {ECO:0000269|PubMed:32596590}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- CAUTION: The protein characterized in PubMed:9660191 corresponds to
CC this sequence and not to the fragment sequence described in this
CC article. {ECO:0000305|PubMed:32596590, ECO:0000305|PubMed:9660191}.
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DR EMBL; AJ441109; CAD29583.1; -; Genomic_DNA.
DR PDB; 4Z6K; X-ray; 1.90 A; A/B/C/D=1-338.
DR PDBsum; 4Z6K; -.
DR AlphaFoldDB; Q8GIX7; -.
DR SMR; Q8GIX7; -.
DR BRENDA; 1.1.1.1; 3421.
DR GO; GO:1990362; F:butanol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..338
FT /note="Alcohol dehydrogenase"
FT /id="PRO_0000451116"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:32596590,
FT ECO:0007744|PDB:4Z6K"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:32596590,
FT ECO:0007744|PDB:4Z6K"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:32596590,
FT ECO:0007744|PDB:4Z6K"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32596590,
FT ECO:0007744|PDB:4Z6K"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32596590,
FT ECO:0007744|PDB:4Z6K"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32596590,
FT ECO:0007744|PDB:4Z6K"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="structural"
FT /evidence="ECO:0000269|PubMed:32596590,
FT ECO:0007744|PDB:4Z6K"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:32596590,
FT ECO:0007744|PDB:4Z6K"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 27..37
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4Z6K"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:4Z6K"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:4Z6K"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:4Z6K"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4Z6K"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:4Z6K"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:4Z6K"
SQ SEQUENCE 338 AA; 35587 MW; A2D90CD2484B144B CRC64;
MKAAVLHEFG QSLQIEEVDI PTPGAGEIVV KMQASGVCHT DLHAVEGDWP VKPSPPFIPG
HEGVGLITAV GEGVTHVKEG DRVGVAWLYS ACGHCTHCLG GWETLCESQQ NSGYSVNGSF
AEYVLANANY VGIIPESVDS IEIAPVLCAG VTVYKGLKMT DTKPGDWVVI SGIGGLGHMA
VQYAIAMGLN VAAVDIDDDK LAFAKKLGAK VTVNAKNTDP AEYLQKEIGG AHGALVTAVS
AKAFDQALSM LRRGGTLVCN GLPPGDFPVS IFDTVLNGIT IRGSIVGTRL DLQESLDMAA
AGKVKATVTA EPLENINDIF ERMRQGKIEG RIVIDYTM
