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Protein

Alcohol dehydrogenase

Gene

adhT

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

NAD+-dependent alcohol dehydrogenase.

Catalytic activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactori

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

Enzyme 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

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.
IPR016040. NAD(P)-bd_dom.
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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliP12311.
SMRiP12311.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiView protein in InterPro
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
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.
ProtoNetiSearch...

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: May 10, 2017
This is version 101 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.