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Protein

Quinoprotein ethanol dehydrogenase

Gene

exaA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of primary alcohols except for methanol that is a very poor substrate.

Catalytic activityi

A primary alcohol + 2 cytochrome c = an aldehyde + 2 reduced cytochrome c + 2 H+.

Cofactori

Protein has several cofactor binding sites:
  • pyrroloquinoline quinoneNote: Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-139-Cys-140 and the plane of Trp-282.
  • Ca2+Note: Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Calcium 2
Metal bindingi48 – 481Calcium 2
Metal bindingi51 – 511Calcium 2
Metal bindingi213 – 2131Calcium 1
Metal bindingi300 – 3001Calcium 1
Active sitei350 – 3501Proton acceptorSequence analysis
Metal bindingi350 – 3501Calcium 1

GO - Molecular functioni

GO - Biological processi

  • ethanol oxidation Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Metal-binding, PQQ

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15517.
BRENDAi1.1.2.8. 5087.
1.1.2.B3. 5087.

Names & Taxonomyi

Protein namesi
Recommended name:
Quinoprotein ethanol dehydrogenase (EC:1.1.2.8)
Short name:
QEDH
Gene namesi
Name:exaA
Ordered Locus Names:PA1982
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA1982.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Add
BLAST
Chaini35 – 623589Quinoprotein ethanol dehydrogenasePRO_0000025565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi139 ↔ 140

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9Z4J7.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi208964.PA1982.

Structurei

Secondary structure

1
623
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi39 – 435Combined sources
Helixi45 – 473Combined sources
Turni72 – 743Combined sources
Helixi75 – 773Combined sources
Beta strandi79 – 857Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi104 – 1096Combined sources
Turni110 – 1123Combined sources
Beta strandi113 – 1219Combined sources
Beta strandi124 – 1296Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi153 – 1586Combined sources
Turni159 – 1613Combined sources
Beta strandi162 – 1709Combined sources
Beta strandi173 – 1786Combined sources
Helixi182 – 1843Combined sources
Beta strandi193 – 1964Combined sources
Turni198 – 2003Combined sources
Beta strandi203 – 2075Combined sources
Helixi212 – 2143Combined sources
Beta strandi219 – 2235Combined sources
Turni225 – 2273Combined sources
Beta strandi230 – 2378Combined sources
Beta strandi241 – 2444Combined sources
Beta strandi247 – 2537Combined sources
Helixi272 – 2765Combined sources
Beta strandi286 – 2883Combined sources
Turni289 – 2924Combined sources
Beta strandi293 – 2986Combined sources
Beta strandi301 – 3044Combined sources
Helixi306 – 3094Combined sources
Beta strandi325 – 3306Combined sources
Turni332 – 3343Combined sources
Beta strandi337 – 3448Combined sources
Beta strandi358 – 3636Combined sources
Beta strandi365 – 3673Combined sources
Beta strandi369 – 3768Combined sources
Beta strandi380 – 3867Combined sources
Turni387 – 3893Combined sources
Beta strandi392 – 4009Combined sources
Beta strandi404 – 4085Combined sources
Turni410 – 4123Combined sources
Beta strandi415 – 4173Combined sources
Beta strandi436 – 4405Combined sources
Turni455 – 4573Combined sources
Beta strandi460 – 4656Combined sources
Beta strandi467 – 4737Combined sources
Beta strandi487 – 4948Combined sources
Beta strandi499 – 5057Combined sources
Turni507 – 5093Combined sources
Beta strandi512 – 5209Combined sources
Beta strandi527 – 5293Combined sources
Turni530 – 5323Combined sources
Beta strandi533 – 5375Combined sources
Beta strandi541 – 5477Combined sources
Turni548 – 5503Combined sources
Beta strandi553 – 5586Combined sources
Beta strandi568 – 5725Combined sources
Beta strandi575 – 5828Combined sources
Helixi587 – 5915Combined sources
Helixi594 – 5996Combined sources
Beta strandi607 – 6126Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FLGX-ray2.60A/B35-616[»]
ProteinModelPortaliQ9Z4J7.
SMRiQ9Z4J7. Positions 35-616.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z4J7.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial PQQ dehydrogenase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105DZG. Bacteria.
COG4993. LUCA.
HOGENOMiHOG000217981.
InParanoidiQ9Z4J7.
KOiK00114.
OMAiKLTPAWS.
PhylomeDBiQ9Z4J7.

Family and domain databases

Gene3Di2.140.10.10. 1 hit.
InterProiIPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
PfamiPF01011. PQQ. 1 hit.
PF13360. PQQ_2. 1 hit.
[Graphical view]
SMARTiSM00564. PQQ. 6 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00363. BACTERIAL_PQQ_1. 1 hit.
PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z4J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTRTSPAPA GLLRPSLHCL AFAVALGSAG AALAKDVTWE DIANDDKTTG
60 70 80 90 100
DVLQYGMGTH AQRWSPLKQV NADNVFKLTP AWSYSFGDEK QRGQESQAIV
110 120 130 140 150
SDGVIYVTAS YSRLFALDAK TGKRLWTYNH RLPDDIRPCC DVVNRGAAIY
160 170 180 190 200
GDKVFFGTLD ASVVALNKNT GKVVWKKKFA DHGAGYTMTG APTIVKDGKT
210 220 230 240 250
GKVLLIHGSS GDEFGVVGRL FARDPDTGEE IWMRPFVEGH MGRLNGKDST
260 270 280 290 300
VTGDVKAPSW PDDRNSPTGK VESWSHGGGA PWQSASFDAE TNTIIVGAGN
310 320 330 340 350
PGPWNTWART AKGGNPHDYD SLYTSGQVGV DPSSGEVKWF YQHTPNDAWD
360 370 380 390 400
FSGNNELVLF DYKAKDGKIV KATAHADRNG FFYVVDRSNG KLQNAFPFVD
410 420 430 440 450
NITWASHIDL KTGRPVEREG QRPPLPEPGQ KHGKAVEVSP PFLGGKNWNP
460 470 480 490 500
MAYSQDTGLF YVPANHWKED YWTEEVSYTK GSAYLGMGFR IKRMYDDHVG
510 520 530 540 550
SLRAMDPVSG KVVWEHKEHL PLWAGVLATA GNLVFTGTGD GYFKAFDAKS
560 570 580 590 600
GKELWKFQTG SGIVSPPITW EQDGEQYLGV TVGYGGAVPL WGGDMADLTR
610 620
PVAQGGSFWV FKLPSWDNRT ASR
Length:623
Mass (Da):68,123
Last modified:May 1, 1999 - v1
Checksum:i32DDE5DF20B291D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009858 Genomic DNA. Translation: CAA08896.1.
AE004091 Genomic DNA. Translation: AAG05370.1.
AF068264 Genomic DNA. Translation: AAC79657.1.
PIRiB83399.
RefSeqiNP_250672.1. NC_002516.2.
WP_003088524.1. NZ_ASJY01000280.1.

Genome annotation databases

EnsemblBacteriaiAAG05370; AAG05370; PA1982.
GeneIDi880475.
KEGGipae:PA1982.
PATRICi19838371. VBIPseAer58763_2066.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009858 Genomic DNA. Translation: CAA08896.1.
AE004091 Genomic DNA. Translation: AAG05370.1.
AF068264 Genomic DNA. Translation: AAC79657.1.
PIRiB83399.
RefSeqiNP_250672.1. NC_002516.2.
WP_003088524.1. NZ_ASJY01000280.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FLGX-ray2.60A/B35-616[»]
ProteinModelPortaliQ9Z4J7.
SMRiQ9Z4J7. Positions 35-616.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA1982.

Proteomic databases

PaxDbiQ9Z4J7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG05370; AAG05370; PA1982.
GeneIDi880475.
KEGGipae:PA1982.
PATRICi19838371. VBIPseAer58763_2066.

Organism-specific databases

PseudoCAPiPA1982.

Phylogenomic databases

eggNOGiENOG4105DZG. Bacteria.
COG4993. LUCA.
HOGENOMiHOG000217981.
InParanoidiQ9Z4J7.
KOiK00114.
OMAiKLTPAWS.
PhylomeDBiQ9Z4J7.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15517.
BRENDAi1.1.2.8. 5087.
1.1.2.B3. 5087.

Miscellaneous databases

EvolutionaryTraceiQ9Z4J7.

Family and domain databases

Gene3Di2.140.10.10. 1 hit.
InterProiIPR018391. PQQ_beta_propeller_repeat.
IPR017512. PQQ_MeOH/EtOH_DH.
IPR002372. PQQ_repeat.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR001479. Quinoprotein_DH_CS.
[Graphical view]
PfamiPF01011. PQQ. 1 hit.
PF13360. PQQ_2. 1 hit.
[Graphical view]
SMARTiSM00564. PQQ. 6 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00363. BACTERIAL_PQQ_1. 1 hit.
PS00364. BACTERIAL_PQQ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEXAA_PSEAE
AccessioniPrimary (citable) accession number: Q9Z4J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: September 7, 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, Complete proteome, Reference proteome

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.