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Protein

Quinohemoprotein alcohol dehydrogenase ADH IIB

Gene

qbdA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the dye-linked oxidation of primary alcohols to the corresponding aldehydes and the (subsequent) oxidation of the aldehydes to carboxylic acids. Exhibits activity with longer mono-alcohols (C-4 to C-7) but not with methanol or glycerol. Reacts with 1,2-propanediol and 1,3-propanediol but not with sugar alcohols such as D-sorbitol.3 Publications

Catalytic activityi

A primary alcohol + azurin = an aldehyde + reduced azurin.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • pyrroloquinoline quinone2 PublicationsNote: Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-127-Cys-128 and the plane of Trp-254.2 Publications
  • Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication
  • heme2 PublicationsNote: Binds 1 heme group per subunit.2 Publications

Enzyme regulationi

Inhibited by 10 mM 1-butanol.1 Publication

Redox potential

E0 is +185 mV for heme c at pH 7.0, +188 mV for heme c at pH 8.0, +172 mV for heme c at pH 8.0 and 0.3 M KCl and +189 mV for ADH IIB-Azurin complex.3 Publications

Manual assertion based on experiment ini

Kineticsi

  1. KM=5.61 mM for ethanol3 Publications
  2. KM=0.105 mM for butane-1-ol3 Publications
  3. KM=10.2 mM for propane-1,2-diol3 Publications
  4. KM=3.71 mM for (S+)propane-1,2-diol3 Publications
  5. KM=4.58 mM for (R-)propane-1,2-diol3 Publications
  6. KM=0.015 mM for butane-1-ol3 Publications
  7. KM=100 µM for azurin (from P.putida in the presence of 30 mM Tris-HCl pH 8.0)3 Publications
  8. KM=51 µM for azurin (from P.putida in the presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)3 Publications
  9. KM=25 µM for azurin (from P.putida in the presence of 30 mM Tris-HCl pH 8.0 and 0.5 M KCl)3 Publications
  10. KM=202 µM for azurin (from P.aerugionosa in the presence of 30 mM Tris-HCl pH 8.0)3 Publications
  11. KM=95 µM for potassium ferricyanide (in the presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)3 Publications
  1. Vmax=15.4 µmol/min/mg enzyme with ethanol as substrate3 Publications
  2. Vmax=17.1 µmol/min/mg enzyme with butane-1-ol as substrate3 Publications
  3. Vmax=4.27 µmol/min/mg enzyme with propane-1,2-diol as substrate3 Publications
  4. Vmax=2.61 µmol/min/mg enzyme with (S+)propane-1,2-diol as substrate3 Publications
  5. Vmax=7.10 µmol/min/mg enzyme with (R-)propane-1,2-diol as substrate3 Publications
  6. Vmax=31 µmol/min/mg enzyme with butane-1-ol as substrate3 Publications
  7. Vmax=62.5 µmol/min/mg enzyme toward azurin (from P.putida in the presence of 30 mM Tris-HCl pH 8.0)3 Publications
  8. Vmax=52.6 µmol/min/mg enzyme toward azurin (from P.putida in the presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)3 Publications
  9. Vmax=41.7 µmol/min/mg enzyme toward azurin (from P.putida in the presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)3 Publications
  10. Vmax=22.3 µmol/min/mg enzyme toward azurin (from P.aeruginosa in the presence of 30 mM Tris-HCl pH 8.0)3 Publications
  11. Vmax=45.5 µmol/min/mg enzyme toward potassium ferricyanide (in the presence of 30 mM Tris-HCl pH 8.0)3 Publications

pH dependencei

Optimum pH is 8.0.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei81PQQ1
Binding sitei133PQQ1
Binding sitei177PQQ1
Metal bindingi195Calcium1 Publication1
Metal bindingi272Calcium1 Publication1
Binding sitei272PQQ1
Active sitei317Proton acceptorSequence analysisBy similarity1
Metal bindingi317Calcium1 Publication1
Binding sitei317Substrate1 Publication1
Binding sitei344PQQ1
Binding sitei399Substrate; via carbonyl oxygen1 Publication1
Binding sitei613Heme (covalent)PROSITE-ProRule annotation1 Publication1
Binding sitei616Heme (covalent)PROSITE-ProRule annotation1 Publication1
Metal bindingi617Iron (heme axial ligand); via tele nitrogenPROSITE-ProRule annotation1 Publication1
Metal bindingi655Iron (heme axial ligand)PROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • electron carrier activity Source: UniProtKB
  • heme binding Source: UniProtKB
  • metal ion binding Source: UniProtKB
  • oxidoreductase activity Source: UniProtKB
  • oxidoreductase activity, acting on CH-OH group of donors Source: InterPro
  • pyrroloquinoline quinone binding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding, PQQ

Enzyme and pathway databases

BRENDAi1.1.9.1. 5092.
1.2.99.3. 5092.

Names & Taxonomyi

Protein namesi
Recommended name:
Quinohemoprotein alcohol dehydrogenase ADH IIBImported (EC:1.1.9.11 Publication)
Short name:
ADH IIB1 Publication
Alternative name(s):
Alcohol dehydrogenase (azurin)By similarity
Gene namesi
Name:qbdAImported
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

  • Periplasm By similarityCurated

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 222 PublicationsAdd BLAST22
ChainiPRO_000041952523 – 690Quinohemoprotein alcohol dehydrogenase ADH IIB1 PublicationAdd BLAST668

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi127 ↔ 1281 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

By 1-butanol. Primary and secondary C3,C4 alcohols as well as butyraldehyde.3 Publications

Interactioni

Subunit structurei

Monomer.3 Publications

Structurei

Secondary structure

1690
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 32Combined sources6
Turni33 – 35Combined sources3
Turni60 – 62Combined sources3
Helixi63 – 65Combined sources3
Beta strandi66 – 73Combined sources8
Beta strandi85 – 87Combined sources3
Beta strandi90 – 95Combined sources6
Helixi96 – 98Combined sources3
Beta strandi99 – 104Combined sources6
Turni105 – 107Combined sources3
Beta strandi110 – 114Combined sources5
Helixi120 – 125Combined sources6
Beta strandi136 – 139Combined sources4
Beta strandi141 – 145Combined sources5
Beta strandi149 – 155Combined sources7
Turni156 – 158Combined sources3
Beta strandi161 – 166Combined sources6
Beta strandi181 – 183Combined sources3
Beta strandi186 – 189Combined sources4
Turni194 – 196Combined sources3
Beta strandi201 – 206Combined sources6
Turni207 – 209Combined sources3
Beta strandi212 – 219Combined sources8
Helixi230 – 236Combined sources7
Helixi244 – 247Combined sources4
Beta strandi257 – 260Combined sources4
Turni261 – 264Combined sources4
Beta strandi265 – 269Combined sources5
Beta strandi273 – 276Combined sources4
Helixi278 – 281Combined sources4
Turni289 – 292Combined sources4
Beta strandi293 – 297Combined sources5
Turni299 – 301Combined sources3
Beta strandi304 – 311Combined sources8
Beta strandi324 – 331Combined sources8
Beta strandi334 – 341Combined sources8
Beta strandi346 – 352Combined sources7
Turni353 – 355Combined sources3
Beta strandi358 – 365Combined sources8
Beta strandi369 – 373Combined sources5
Turni375 – 377Combined sources3
Beta strandi380 – 382Combined sources3
Turni384 – 387Combined sources4
Beta strandi389 – 391Combined sources3
Beta strandi393 – 397Combined sources5
Beta strandi409 – 411Combined sources3
Turni412 – 415Combined sources4
Beta strandi416 – 423Combined sources8
Beta strandi426 – 428Combined sources3
Helixi432 – 434Combined sources3
Helixi447 – 449Combined sources3
Helixi455 – 457Combined sources3
Beta strandi459 – 466Combined sources8
Turni467 – 470Combined sources4
Beta strandi471 – 481Combined sources11
Beta strandi486 – 489Combined sources4
Turni490 – 492Combined sources3
Beta strandi493 – 497Combined sources5
Beta strandi501 – 507Combined sources7
Turni508 – 510Combined sources3
Beta strandi513 – 518Combined sources6
Beta strandi528 – 532Combined sources5
Beta strandi535 – 542Combined sources8
Helixi547 – 551Combined sources5
Helixi554 – 557Combined sources4
Beta strandi566 – 572Combined sources7
Helixi599 – 612Combined sources14
Helixi614 – 617Combined sources4
Helixi619 – 621Combined sources3
Beta strandi625 – 627Combined sources3
Helixi630 – 632Combined sources3
Helixi635 – 639Combined sources5
Helixi641 – 647Combined sources7
Helixi651 – 653Combined sources3
Turni659 – 661Combined sources3
Helixi664 – 684Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KV9X-ray1.90A23-690[»]
ProteinModelPortaliQ8GR64.
SMRiQ8GR64.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GR64.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini600 – 678Cytochrome cPROSITE-ProRule annotationAdd BLAST79

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni193 – 195PQQ binding3
Regioni252 – 254PQQ binding3
Regioni404 – 405PQQ binding2

Sequence similaritiesi

Belongs to the bacterial PQQ dehydrogenase family.Sequence analysis
Contains 1 cytochrome c domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

KOiK17760.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
2.140.10.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR018391. 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]
PfamiPF13442. Cytochrome_CBB3. 1 hit.
PF13360. PQQ_2. 2 hits.
[Graphical view]
SMARTiSM00564. PQQ. 5 hits.
[Graphical view]
SUPFAMiSSF46626. SSF46626. 1 hit.
SSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00364. BACTERIAL_PQQ_2. 1 hit.
PS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8GR64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKPLRTSLL MLCLATPLAA LAAGVDEAAI RATEQAGGEW LSHGRTYAEQ
60 70 80 90 100
RFSPLKQIDA SNVRSLGLAW YMDLDNTRGL EATPLFHDGV IYTSMSWSRV
110 120 130 140 150
IAVDAASGKE LWRYDPEVAK VKARTSCCDA VNRGVALWGD KVYVGTLDGR
160 170 180 190 200
LIALDAKTGK AIWSQQTTDP AKPYSITGAP RVVKGKVIIG NGGAEYGVRG
210 220 230 240 250
FVSAYDADTG KLAWRFYTVP GDPALPYEHP ELREAAKTWQ GDQYWKLGGG
260 270 280 290 300
GTVWDSMAYD PELDLLYVGT GNGSPWNREV RSPGGGDNLY LSSILAIRPD
310 320 330 340 350
TGKLAWHYQV TPGDSWDFTA TQQITLAELN IDGKPRKVLM QAPKNGFFYV
360 370 380 390 400
LDRTNGKLIS AEKFGKVTWA EKVDLATGRP VEAPGVRYEK EPIVMWPSPF
410 420 430 440 450
GAHNWHSMSF NPGTGLVYIP YQEVPGVYRN EGKDFVTRKA FNTAAGFADA
460 470 480 490 500
TDVPAAVVSG ALLAWDPVKQ KAAWKVPYPT HWNGGTLSTA GNLVFQGTAA
510 520 530 540 550
GQMHAYSADK GEALWQFEAQ SGIVAAPMTF ELAGRQYVAI MAGWGGVATL
560 570 580 590 600
TGGESMNLPG MKNRSRLLVF ALDGKAQLPP PAPAPAKVER VPQPVTAAPE
610 620 630 640 650
QVQAGKQLYG QFCSVCHGMG TISGGLIPDL RQSSDATREH FQQIVLQGAL
660 670 680 690
KPLGMPSFDD SLKPEEVEQI KLYVMSREYE DYMARHKAAP
Length:690
Mass (Da):74,969
Last modified:March 1, 2003 - v1
Checksum:iF5198701D0937613
GO

Mass spectrometryi

Molecular mass is 73262 Da from positions 23 - 690. Determined by MALDI. The measured mass is that of QbdA with a single heme bound.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091400 Genomic DNA. Translation: BAC15559.1.
RefSeqiWP_058541185.1. NZ_LKGZ01000023.1.

Genome annotation databases

KEGGiag:BAC15559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB091400 Genomic DNA. Translation: BAC15559.1.
RefSeqiWP_058541185.1. NZ_LKGZ01000023.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KV9X-ray1.90A23-690[»]
ProteinModelPortaliQ8GR64.
SMRiQ8GR64.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAC15559.

Phylogenomic databases

KOiK17760.

Enzyme and pathway databases

BRENDAi1.1.9.1. 5092.
1.2.99.3. 5092.

Miscellaneous databases

EvolutionaryTraceiQ8GR64.

Family and domain databases

Gene3Di1.10.760.10. 1 hit.
2.140.10.10. 1 hit.
InterProiIPR009056. Cyt_c-like_dom.
IPR018391. 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]
PfamiPF13442. Cytochrome_CBB3. 1 hit.
PF13360. PQQ_2. 2 hits.
[Graphical view]
SMARTiSM00564. PQQ. 5 hits.
[Graphical view]
SUPFAMiSSF46626. SSF46626. 1 hit.
SSF50998. SSF50998. 1 hit.
TIGRFAMsiTIGR03075. PQQ_enz_alc_DH. 1 hit.
PROSITEiPS00364. BACTERIAL_PQQ_2. 1 hit.
PS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQHED_PSEPU
AccessioniPrimary (citable) accession number: Q8GR64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 77 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.