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Protein

Quinohemoprotein alcohol dehydrogenase ADH-IIG

Gene

qgdA

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. Active with primary alcohols, glycerol, 1,2-propanediol, 1,3-propanediol but not with methanol or sugar alcohols such as D-sorbitol.3 Publications

Catalytic activityi

A primary alcohol + azurin = an aldehyde + reduced azurin.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • pyrroloquinoline quinone2 PublicationsNote: Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-138-Cys-139 and the plane of Trp-266.2 Publications
  • Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication
  • heme2 PublicationsNote: Binds 1 heme group per subunit.2 Publications

Enzyme regulationi

Exhibits higher affinity for 1-butanol compared to 1,2-propanediol but inhibited by 10 mM 1-butanol.1 Publication

Kineticsi

  1. KM=33.2 mM for ethanol2 Publications
  2. KM=0.226 mM for propane-1,2-diol2 Publications
  3. KM=2.40 mM for glycerol2 Publications
  4. KM=0.055 mM for (S+)propane-1,2-diol2 Publications
  5. KM=3.32 mM for (R-)propane-1,2-diol2 Publications
  6. KM=0.043 mM for butane-1-ol2 Publications
  1. Vmax=11.5 µmol/min/mg enzyme with ethanol as substrate2 Publications
  2. Vmax=17.4 µmol/min/mg enzyme with propane-1,2-diol as substrate2 Publications
  3. Vmax=17.4 µmol/min/mg enzyme with glycerol as substrate2 Publications
  4. Vmax=21 µmol/min/mg enzyme with (S+)propane-1,2-diol as substrate2 Publications
  5. Vmax=12.2 µmol/min/mg enzyme with (R-)propane-1,2-diol as substrate2 Publications
  6. Vmax=8.50 µmol/min/mg enzyme with butane-1-ol as substrate2 Publications

pH dependencei

Optimum pH is 8.0.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921PQQ1 Publication
Binding sitei144 – 1441PQQ1 Publication
Binding sitei189 – 1891PQQ1 Publication
Metal bindingi207 – 2071Calcium1 Publication
Metal bindingi284 – 2841Calcium1 Publication
Binding sitei284 – 2841PQQ1 Publication
Active sitei329 – 3291Proton acceptorSequence analysisBy similarity
Metal bindingi329 – 3291Calcium1 Publication
Binding sitei329 – 3291Substrate
Binding sitei356 – 3561PQQ1 Publication
Binding sitei415 – 4151Substrate
Binding sitei635 – 6351Heme (covalent)PROSITE-ProRule annotation1 Publication
Binding sitei638 – 6381Heme (covalent)PROSITE-ProRule annotation1 Publication
Metal bindingi639 – 6391Iron (heme axial ligand); via tele nitrogenPROSITE-ProRule annotation1 Publication
Binding sitei651 – 6511Substrate
Metal bindingi676 – 6761Iron (heme axial ligand)PROSITE-ProRule annotation1 Publication
Binding sitei697 – 6971Substrate

GO - Molecular functioni

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

GO - Biological processi

  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding, PQQ

Enzyme and pathway databases

BRENDAi1.2.99.3. 5092.

Names & Taxonomyi

Protein namesi
Recommended name:
Quinohemoprotein alcohol dehydrogenase ADH-IIGImported (EC:1.1.9.11 Publication)
Short name:
ADH IIG1 Publication
Alternative name(s):
Alcohol dehydrogenase (azurin)By similarity
Gene namesi
Name:qgdAImported
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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 718689Quinohemoprotein alcohol dehydrogenase ADH-IIG1 PublicationPRO_0000419526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi138 ↔ 1391 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

(S+)-propane-1,2-diol is the most effective whereas (R-)-propane-1,2-diol, ethanediol and glycerol are weaker inducers.3 Publications

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1
718
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 425Combined sources
Helixi44 – 463Combined sources
Turni71 – 733Combined sources
Helixi74 – 763Combined sources
Beta strandi77 – 848Combined sources
Beta strandi96 – 983Combined sources
Beta strandi101 – 1055Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1155Combined sources
Turni116 – 1183Combined sources
Beta strandi121 – 1255Combined sources
Helixi131 – 1366Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi152 – 1565Combined sources
Beta strandi160 – 1667Combined sources
Turni167 – 1693Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi198 – 2014Combined sources
Turni206 – 2083Combined sources
Beta strandi213 – 2186Combined sources
Turni219 – 2213Combined sources
Beta strandi224 – 2318Combined sources
Helixi242 – 2487Combined sources
Helixi256 – 2594Combined sources
Beta strandi269 – 2724Combined sources
Turni273 – 2764Combined sources
Beta strandi277 – 2815Combined sources
Beta strandi285 – 2884Combined sources
Helixi290 – 2945Combined sources
Turni301 – 3044Combined sources
Beta strandi305 – 3106Combined sources
Turni311 – 3133Combined sources
Beta strandi316 – 3238Combined sources
Beta strandi336 – 3438Combined sources
Beta strandi346 – 3538Combined sources
Beta strandi358 – 3647Combined sources
Turni365 – 3673Combined sources
Beta strandi370 – 3778Combined sources
Beta strandi380 – 3867Combined sources
Turni387 – 3904Combined sources
Beta strandi391 – 3944Combined sources
Helixi396 – 3994Combined sources
Turni401 – 4033Combined sources
Beta strandi404 – 4063Combined sources
Beta strandi408 – 4125Combined sources
Turni427 – 4293Combined sources
Beta strandi432 – 4387Combined sources
Beta strandi441 – 4444Combined sources
Beta strandi462 – 4654Combined sources
Helixi472 – 4798Combined sources
Beta strandi483 – 4908Combined sources
Turni491 – 4944Combined sources
Beta strandi495 – 50511Combined sources
Beta strandi510 – 5134Combined sources
Turni514 – 5163Combined sources
Beta strandi517 – 5215Combined sources
Beta strandi525 – 5317Combined sources
Turni532 – 5343Combined sources
Beta strandi537 – 5426Combined sources
Beta strandi552 – 5565Combined sources
Beta strandi559 – 5668Combined sources
Helixi572 – 5754Combined sources
Helixi577 – 5804Combined sources
Helixi581 – 5833Combined sources
Beta strandi590 – 5967Combined sources
Helixi621 – 63414Combined sources
Helixi636 – 6394Combined sources
Helixi641 – 6433Combined sources
Beta strandi647 – 6493Combined sources
Helixi657 – 6615Combined sources
Helixi663 – 6675Combined sources
Turni668 – 6714Combined sources
Helixi672 – 6743Combined sources
Turni680 – 6823Combined sources
Helixi685 – 70420Combined sources
Helixi710 – 7123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YIQX-ray2.20A30-718[»]
ProteinModelPortaliQ4W6G0.
SMRiQ4W6G0. Positions 30-713.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4W6G0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini622 – 69978Cytochrome cPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni205 – 2073PQQ binding
Regioni264 – 2663PQQ binding
Regioni419 – 4202PQQ binding

Sequence similaritiesi

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

Keywords - Domaini

Signal

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.
[Graphical view]
PfamiPF13442. Cytochrome_CBB3. 1 hit.
PF01011. PQQ. 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.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q4W6G0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQTGLASLP LKSLAVAVLL SLAGTPALAA DIPANVDGAR IIAADKEPGN
60 70 80 90 100
WMSTGRTYDE QRYSPLKQIS DQNVGQLGLA WSYKLDLDRG VEATPIVVDG
110 120 130 140 150
AMYTTGPFSV VYALDARDGR LIWKYDPQSD RHRAGEACCD AVNRGVAVWK
160 170 180 190 200
GKVYVGVLDG RLEAIDAKTG QRAWSVDTRA DHKRSYTITG APRVVNGKVV
210 220 230 240 250
IGNGGAEFGV RGYVTAYDAE TGKEAWRFYT VPGDPKLPPE GKGMEIAAKT
260 270 280 290 300
WFGDAYVEQG GGGTAWDSFA YDPELNLLYI GVGNGSLWDP KWRSQAKGDN
310 320 330 340 350
LFLSSIVAVN ADTGEYVWHY QTTPGDAWDY TATQHMILAE LPIDGKPRKV
360 370 380 390 400
LMQAPKNGFF YVIDRATGEL LSAKGIVPQS WTKGMDMKTG RPILDEENAA
410 420 430 440 450
YWKNGKRNLV TPAFWGAHDW QPMSYNPDTG LVYIPAHIMS AYYEHIPEAP
460 470 480 490 500
KRNPFKSMYQ LGLRTGMMPE GAEGLLEMAK SWSGKLIAWD PVKQQAAWEV
510 520 530 540 550
PYVTIFNGGT LSTAGNLVFE GSADGRVIAY AADTGEKLWE QPAASGVMAA
560 570 580 590 600
PVTYSVDGEQ YVTFMAGWGG AFSTFAGALS LRAGVQPYAQ VLTYKLGGTA
610 620 630 640 650
KLQEPAPRPD TPKPPALSND TASIEAGAKL YDGYCSQCHG IHAVSGGVLP
660 670 680 690 700
DLRKLTPEKH QMFLGILFGG RVPDGMPSFA DAFTPEQVDQ IHQYLIKRAH
710
DLHQEGDTWK QFSAKSSH
Length:718
Mass (Da):78,113
Last modified:July 5, 2005 - v1
Checksum:iDF407A59574CE7F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB204833 Genomic DNA. Translation: BAD99293.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB204833 Genomic DNA. Translation: BAD99293.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YIQX-ray2.20A30-718[»]
ProteinModelPortaliQ4W6G0.
SMRiQ4W6G0. Positions 30-713.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.2.99.3. 5092.

Miscellaneous databases

EvolutionaryTraceiQ4W6G0.

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.
[Graphical view]
PfamiPF13442. Cytochrome_CBB3. 1 hit.
PF01011. PQQ. 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.
PROSITEiPS51007. CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase ADH-IIG from Pseudomonas putida HK5."
    Toyama H., Chen Z.W., Fukumoto M., Adachi O., Matsushita K., Mathews F.S.
    J. Mol. Biol. 352:91-104(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-40 AND 102-111, X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 30-718 IN COMPLEX WITH (R)-PROPANE-1,2-DIOL; CALCIUM; HEME AND PQQ, CATALYTIC ACTIVITY, STEREOSELECTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: HK51 Publication.
  2. "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols."
    Toyama H., Fujii A., Matsushita K., Shinagawa E., Ameyama M., Adachi O.
    J. Bacteriol. 177:2442-2450(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION.
    Strain: HK51 Publication.
  3. "Disruption of quinoprotein ethanol dehydrogenase gene and adjacent genes in Pseudomonas putida HK5."
    Promden W., Vangnai A.S., Pongsawasdi P., Adachi O., Matsushita K., Toyama H.
    FEMS Microbiol. Lett. 280:203-209(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
    Strain: HK51 Publication.
  4. "Analysis of the promoter activities of the genes encoding three quinoprotein alcohol dehydrogenases in Pseudomonas putida HK5."
    Promden W., Vangnai A.S., Toyama H., Matsushita K., Pongsawasdi P.
    Microbiology 155:594-603(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, STEREOSPECIFICITY.
    Strain: HK51 Publication.

Entry informationi

Entry nameiQGDA_PSEPU
AccessioniPrimary (citable) accession number: Q4W6G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: July 5, 2005
Last modified: December 9, 2015
This is version 58 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.