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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)DescriptionActionsGraphical viewLength
Binding sitei92PQQ1 Publication1
Binding sitei144PQQ1 Publication1
Binding sitei189PQQ1 Publication1
Metal bindingi207Calcium1 Publication1
Metal bindingi284Calcium1 Publication1
Binding sitei284PQQ1 Publication1
Active sitei329Proton acceptorSequence analysisBy similarity1
Metal bindingi329Calcium1 Publication1
Binding sitei329Substrate1
Binding sitei356PQQ1 Publication1
Binding sitei415Substrate1
Binding sitei635Heme (covalent)PROSITE-ProRule annotation1 Publication1
Binding sitei638Heme (covalent)PROSITE-ProRule annotation1 Publication1
Metal bindingi639Iron (heme axial ligand); via tele nitrogenPROSITE-ProRule annotation1 Publication1
Binding sitei651Substrate1
Metal bindingi676Iron (heme axial ligand)PROSITE-ProRule annotation1 Publication1
Binding sitei697Substrate1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 291 PublicationAdd BLAST29
ChainiPRO_000041952630 – 718Quinohemoprotein alcohol dehydrogenase ADH-IIG1 PublicationAdd BLAST689

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

1718
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 42Combined sources5
Helixi44 – 46Combined sources3
Turni71 – 73Combined sources3
Helixi74 – 76Combined sources3
Beta strandi77 – 84Combined sources8
Beta strandi96 – 98Combined sources3
Beta strandi101 – 105Combined sources5
Helixi107 – 109Combined sources3
Beta strandi111 – 115Combined sources5
Turni116 – 118Combined sources3
Beta strandi121 – 125Combined sources5
Helixi131 – 136Combined sources6
Beta strandi147 – 149Combined sources3
Beta strandi152 – 156Combined sources5
Beta strandi160 – 166Combined sources7
Turni167 – 169Combined sources3
Beta strandi172 – 177Combined sources6
Beta strandi193 – 195Combined sources3
Beta strandi198 – 201Combined sources4
Turni206 – 208Combined sources3
Beta strandi213 – 218Combined sources6
Turni219 – 221Combined sources3
Beta strandi224 – 231Combined sources8
Helixi242 – 248Combined sources7
Helixi256 – 259Combined sources4
Beta strandi269 – 272Combined sources4
Turni273 – 276Combined sources4
Beta strandi277 – 281Combined sources5
Beta strandi285 – 288Combined sources4
Helixi290 – 294Combined sources5
Turni301 – 304Combined sources4
Beta strandi305 – 310Combined sources6
Turni311 – 313Combined sources3
Beta strandi316 – 323Combined sources8
Beta strandi336 – 343Combined sources8
Beta strandi346 – 353Combined sources8
Beta strandi358 – 364Combined sources7
Turni365 – 367Combined sources3
Beta strandi370 – 377Combined sources8
Beta strandi380 – 386Combined sources7
Turni387 – 390Combined sources4
Beta strandi391 – 394Combined sources4
Helixi396 – 399Combined sources4
Turni401 – 403Combined sources3
Beta strandi404 – 406Combined sources3
Beta strandi408 – 412Combined sources5
Turni427 – 429Combined sources3
Beta strandi432 – 438Combined sources7
Beta strandi441 – 444Combined sources4
Beta strandi462 – 465Combined sources4
Helixi472 – 479Combined sources8
Beta strandi483 – 490Combined sources8
Turni491 – 494Combined sources4
Beta strandi495 – 505Combined sources11
Beta strandi510 – 513Combined sources4
Turni514 – 516Combined sources3
Beta strandi517 – 521Combined sources5
Beta strandi525 – 531Combined sources7
Turni532 – 534Combined sources3
Beta strandi537 – 542Combined sources6
Beta strandi552 – 556Combined sources5
Beta strandi559 – 566Combined sources8
Helixi572 – 575Combined sources4
Helixi577 – 580Combined sources4
Helixi581 – 583Combined sources3
Beta strandi590 – 596Combined sources7
Helixi621 – 634Combined sources14
Helixi636 – 639Combined sources4
Helixi641 – 643Combined sources3
Beta strandi647 – 649Combined sources3
Helixi657 – 661Combined sources5
Helixi663 – 667Combined sources5
Turni668 – 671Combined sources4
Helixi672 – 674Combined sources3
Turni680 – 682Combined sources3
Helixi685 – 704Combined sources20
Helixi710 – 712Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ4W6G0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini622 – 699Cytochrome cPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni205 – 207PQQ binding3
Regioni264 – 266PQQ binding3
Regioni419 – 420PQQ binding2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YIQX-ray2.20A30-718[»]
ProteinModelPortaliQ4W6G0.
SMRiQ4W6G0.
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...

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: November 2, 2016
This is version 60 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.