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Protein

Quinohemoprotein alcohol dehydrogenase ADH IIB

Gene

qbdA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: -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.4 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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 sitei81Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei133Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei177Pyrroloquinoline quinoneCombined sources1 Publication1
Metal bindingi195CalciumCombined sources1 Publication1
Binding sitei252Pyrroloquinoline quinoneCombined sources1 Publication1
Metal bindingi272CalciumCombined sources1 Publication1
Active sitei317Proton acceptor1 Publication1
Metal bindingi317CalciumCombined sources1 Publication1
Binding sitei344Pyrroloquinoline quinoneCombined sources1 Publication1
Binding sitei547Pyrroloquinoline quinone; via amide nitrogenCombined sources1 Publication1
Binding sitei613Heme c (covalent)Combined sources1 Publication1
Binding sitei616Heme c (covalent)Combined sources1 Publication1
Metal bindingi617Iron (heme axial ligand); via tele nitrogenCombined sources1 Publication1
Metal bindingi655Iron (heme axial ligand)Combined sources1 Publication1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • electron transfer 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

Keywordsi

Molecular functionOxidoreductase
LigandCalcium, 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 IIB1 Publication (EC:1.1.9.13 Publications)
Short name:
ADH IIB1 Publication
Alternative name(s):
Alcohol dehydrogenase (azurin)Curated
Gene namesi
Name:qbdA1 Publication
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Chemistry databases

DrugBankiDB03205 Pyrroloquinoline Quinone

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 ↔ 128Combined sources1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ8GR64

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 – 194Pyrroloquinoline quinone bindingCombined sources1 Publication2
Regioni404 – 405Pyrroloquinoline quinone bindingCombined sources1 Publication2

Sequence similaritiesi

Belongs to the bacterial PQQ dehydrogenase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

KOiK17760

Family and domain databases

Gene3Di1.10.760.10, 1 hit
InterProiView protein in InterPro
IPR009056 Cyt_c-like_dom
IPR036909 Cyt_c-like_dom_sf
IPR018391 PQQ_beta_propeller_repeat
IPR017512 PQQ_MeOH/EtOH_DH
IPR002372 PQQ_repeat
IPR011047 Quinoprotein_ADH-like_supfam
IPR001479 Quinoprotein_DH_CS
PfamiView protein in Pfam
PF13442 Cytochrome_CBB3, 1 hit
PF13360 PQQ_2, 2 hits
SMARTiView protein in SMART
SM00564 PQQ, 5 hits
SUPFAMiSSF46626 SSF46626, 1 hit
SSF50998 SSF50998, 1 hit
TIGRFAMsiTIGR03075 PQQ_enz_alc_DH, 1 hit
PROSITEiView protein in PROSITE
PS00364 BACTERIAL_PQQ_2, 1 hit
PS51007 CYTC, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiQHED_PSEPU
AccessioniPrimary (citable) accession number: Q8GR64
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: March 1, 2003
Last modified: May 23, 2018
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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