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Protein

Alcohol dehydrogenase

Gene

adhT

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

NAD+-dependent alcohol dehydrogenase.

Catalytic activityi

A primary alcohol + NAD+ = an aldehyde + NADH.
A secondary alcohol + NAD+ = a ketone + NADH.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Activity regulationi

Substrate inhibition is not observed with any alcohols, and the enzyme-NADH dissociation is not considered to be a rate-limiting step.

Temperature dependencei

Thermostable.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi38Zinc 1; catalyticBy similarity1
Metal bindingi61Zinc 1; catalyticBy similarity1
Metal bindingi92Zinc 2By similarity1
Metal bindingi95Zinc 2By similarity1
Metal bindingi98Zinc 2By similarity1
Metal bindingi106Zinc 2By similarity1
Metal bindingi148Zinc 1; catalyticBy similarity1
Binding sitei195NADBy similarity1
Binding sitei200NADBy similarity1
Binding sitei331NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi172 – 177NADBy similarity6
Nucleotide bindingi260 – 262NADBy similarity3

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase (EC:1.1.1.1)
Alternative name(s):
ADH-T
Gene namesi
Name:adhT
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38C → S: No activity. 1 Publication1
Mutagenesisi40T → A: No activity. 1 Publication1
Mutagenesisi40T → S: Little decrease in activity. 1 Publication1
Mutagenesisi43H → A: No activity. 1 Publication1
Mutagenesisi43H → R: Higher level of activity at pH 9. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001607361 – 337Alcohol dehydrogenaseAdd BLAST337

Proteomic databases

PRIDEiP12311

Structurei

3D structure databases

ProteinModelPortaliP12311
SMRiP12311
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiView protein in InterPro
IPR013149 ADH_C
IPR013154 ADH_N
IPR002328 ADH_Zn_CS
IPR011032 GroES-like_sf
IPR036291 NAD(P)-bd_dom_sf
IPR020843 PKS_ER
PfamiView protein in Pfam
PF08240 ADH_N, 1 hit
PF00107 ADH_zinc_N, 1 hit
SMARTiView protein in SMART
SM00829 PKS_ER, 1 hit
SUPFAMiSSF50129 SSF50129, 1 hit
SSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00059 ADH_ZINC, 1 hit

Sequencei

Sequence statusi: Complete.

P12311-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKAAVVEQFK KPLQVKEVEK PKISYGEVLV RIKACGVCHT DLHAAHGDWP
60 70 80 90 100
VKPKLPLIPG HEGVGVIEEV GPGVTHLKVG DRVGIPWLYS ACGHCDYCLS
110 120 130 140 150
GQETLCERQQ NAGYSVDGGY AEYCRAAADY VVKIPDNLSF EEAAPIFCAG
160 170 180 190 200
VTTYKALKVT GAKPGEWVAI YGIGGLGHVA VQYAKAMGLN VVAVDLGDEK
210 220 230 240 250
LELAKQLGAD LVVNPKHDDA AQWIKEKVGG VHATVVTAVS KAAFESAYKS
260 270 280 290 300
IRRGGACVLV GLPPEEIPIP IFDTVLNGVK IIGSIVGTRK DLQEALQFAA
310 320 330
EGKVKTIVEV QPLENINDVF DRMLKGQING RVVLKVD
Length:337
Mass (Da):36,100
Last modified:November 1, 1995 - v2
Checksum:iB9B35A80EE9B7A86
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22Missing AA sequence (PubMed:4578954).Curated1
Sequence conflicti33Missing AA sequence (PubMed:4578954).Curated1
Sequence conflicti52 – 53KP → PK AA sequence (PubMed:436831).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90421 Genomic DNA Translation: BAA14411.1
PIRiA42654
RefSeqiWP_033015595.1, NZ_LQYV01000078.1

Similar proteinsi

Entry informationi

Entry nameiADH1_GEOSE
AccessioniPrimary (citable) accession number: P12311
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1995
Last modified: September 12, 2018
This is version 105 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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