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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)DescriptionActionsGraphical viewLength
Metal bindingi37Zinc; catalytic2 Publications1
Metal bindingi59Zinc; catalytic2 Publications1
Metal bindingi150Zinc; catalytic2 Publications1
Binding sitei218NADP1 Publication1
Binding sitei340NADP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi175 – 178NADP1 Publication4
Nucleotide bindingi198 – 200NADP1 Publication3
Nucleotide bindingi265 – 267NADP1 Publication3

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001607491 – 352NADP-dependent isopropanol dehydrogenaseAdd BLAST352

Interactioni

Subunit structurei

Homotetramer.2 Publications

Structurei

Secondary structure

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 8Combined sources7
Beta strandi11 – 16Combined sources6
Beta strandi27 – 35Combined sources9
Helixi38 – 45Combined sources8
Beta strandi53 – 56Combined sources4
Beta strandi60 – 68Combined sources9
Beta strandi80 – 83Combined sources4
Beta strandi90 – 92Combined sources3
Helixi93 – 96Combined sources4
Helixi100 – 102Combined sources3
Turni106 – 109Combined sources4
Turni112 – 114Combined sources3
Beta strandi119 – 122Combined sources4
Beta strandi124 – 128Combined sources5
Helixi129 – 132Combined sources4
Helixi142 – 145Combined sources4
Turni146 – 150Combined sources5
Helixi153 – 161Combined sources9
Beta strandi170 – 173Combined sources4
Helixi177 – 187Combined sources11
Turni188 – 190Combined sources3
Beta strandi192 – 197Combined sources6
Helixi201 – 210Combined sources10
Beta strandi213 – 216Combined sources4
Helixi218 – 220Combined sources3
Helixi223 – 230Combined sources8
Turni231 – 233Combined sources3
Beta strandi236 – 241Combined sources6
Helixi248 – 255Combined sources8
Beta strandi256 – 264Combined sources9
Beta strandi272 – 277Combined sources6
Helixi279 – 284Combined sources6
Beta strandi289 – 292Combined sources4
Helixi298 – 310Combined sources13
Helixi316 – 319Combined sources4
Beta strandi320 – 326Combined sources7
Helixi329 – 338Combined sources10
Beta strandi345 – 350Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
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...

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: November 30, 2016
This is version 121 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.