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Protein

NADP-dependent isopropanol dehydrogenase

Gene

adh

Organism
Thermoanaerobacter brockii (Thermoanaerobium brockii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.1 Publication

Catalytic activityi

Propan-2-ol + NADP+ = acetone + NADPH.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi37 – 371Zinc; catalytic2 Publications
Metal bindingi59 – 591Zinc; catalytic2 Publications
Metal bindingi150 – 1501Zinc; catalytic2 Publications
Binding sitei218 – 2181NADP1 Publication
Binding sitei340 – 3401NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1784NADP1 Publication
Nucleotide bindingi198 – 2003NADP1 Publication
Nucleotide bindingi265 – 2673NADP1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NADP, Zinc

Enzyme and pathway databases

BRENDAi1.1.1.2. 1463.

Names & Taxonomyi

Protein namesi
Recommended name:
NADP-dependent isopropanol dehydrogenase (EC:1.1.1.80)
Gene namesi
Name:adh
OrganismiThermoanaerobacter brockii (Thermoanaerobium brockii)
Taxonomic identifieri29323 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352NADP-dependent isopropanol dehydrogenasePRO_0000160749Add
BLAST

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87Combined sources
Beta strandi11 – 166Combined sources
Beta strandi27 – 359Combined sources
Helixi38 – 458Combined sources
Beta strandi53 – 564Combined sources
Beta strandi60 – 689Combined sources
Beta strandi80 – 834Combined sources
Beta strandi90 – 923Combined sources
Helixi93 – 964Combined sources
Helixi100 – 1023Combined sources
Turni106 – 1094Combined sources
Turni112 – 1143Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi124 – 1285Combined sources
Helixi129 – 1324Combined sources
Helixi142 – 1454Combined sources
Turni146 – 1505Combined sources
Helixi152 – 16110Combined sources
Beta strandi170 – 1734Combined sources
Helixi177 – 18711Combined sources
Turni188 – 1903Combined sources
Beta strandi192 – 1976Combined sources
Helixi201 – 21010Combined sources
Beta strandi213 – 2164Combined sources
Helixi218 – 2203Combined sources
Helixi223 – 2308Combined sources
Turni231 – 2333Combined sources
Beta strandi236 – 2416Combined sources
Helixi248 – 2558Combined sources
Beta strandi256 – 2649Combined sources
Beta strandi272 – 2776Combined sources
Helixi279 – 2846Combined sources
Beta strandi289 – 2924Combined sources
Helixi298 – 31013Combined sources
Helixi316 – 3194Combined sources
Beta strandi320 – 3267Combined sources
Helixi329 – 33810Combined sources
Beta strandi345 – 3506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXZX-ray2.99A/B/C/D1-352[»]
1YKFX-ray2.50A/B/C/D1-352[»]
2NVBX-ray2.80A/B/C/D1-352[»]
3FPCX-ray1.40A/B/C/D1-152[»]
A/B/C/D295-352[»]
3FPLX-ray1.90A153-295[»]
3FSRX-ray2.20A/B/C/D1-152[»]
A/B/C/D296-352[»]
3FTNX-ray2.19A/B/C/D1-152[»]
A/B/C/D296-352[»]
ProteinModelPortaliP14941.
SMRiP14941. Positions 1-352.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14941.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14941-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGFAMLSIG KVGWIEKEKP APGPFDAIVR PLAVAPCTSD IHTVFEGAIG
60 70 80 90 100
ERHNMILGHE AVGEVVEVGS EVKDFKPGDR VVVPAITPDW RTSEVQRGYH
110 120 130 140 150
QHSGGMLAGW KFSNVKDGVF GEFFHVNDAD MNLAHLPKEI PLEAAVMIPD
160 170 180 190 200
MMTTGFHGAE LADIELGATV AVLGIGPVGL MAVAGAKLRG AGRIIAVGSR
210 220 230 240 250
PVCVDAAKYY GATDIVNYKD GPIESQIMNL TEGKGVDAAI IAGGNADIMA
260 270 280 290 300
TAVKIVKPGG TIANVNYFGE GEVLPVPRLE WGCGMAHKTI KGGLCPGGRL
310 320 330 340 350
RMERLIDLVF YKRVDPSKLV THVFRGFDNI EKAFMLMKDK PKDLIKPVVI

LA
Length:352
Mass (Da):37,647
Last modified:April 1, 1990 - v1
Checksum:iE124A5351AD55185
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64841 Genomic DNA. Translation: CAA46053.1.
PIRiA32973.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64841 Genomic DNA. Translation: CAA46053.1.
PIRiA32973.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BXZX-ray2.99A/B/C/D1-352[»]
1YKFX-ray2.50A/B/C/D1-352[»]
2NVBX-ray2.80A/B/C/D1-352[»]
3FPCX-ray1.40A/B/C/D1-152[»]
A/B/C/D295-352[»]
3FPLX-ray1.90A153-295[»]
3FSRX-ray2.20A/B/C/D1-152[»]
A/B/C/D296-352[»]
3FTNX-ray2.19A/B/C/D1-152[»]
A/B/C/D296-352[»]
ProteinModelPortaliP14941.
SMRiP14941. Positions 1-352.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.1.2. 1463.

Miscellaneous databases

EvolutionaryTraceiP14941.

Family and domain databases

Gene3Di3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Amino acid sequence of alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii."
    Peretz M., Burstein Y.
    Biochemistry 28:6549-6555(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: ATCC 53556 / HTD4 / DSM 1457.
  2. Burstein Y.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 53556 / HTD4 / DSM 1457.
  3. "NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii."
    Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F.
    J. Mol. Biol. 278:967-981(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH NADP AND ZINC.
  4. "Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms."
    Goihberg E., Peretz M., Tel-Or S., Dym O., Shimon L., Frolow F., Burstein Y.
    Biochemistry 49:1943-1953(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 153-295 IN COMPLEX WITH ZINC, FUNCTION, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiADH_THEBR
AccessioniPrimary (citable) accession number: P14941
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.