QEDH_PSEPU
ID QEDH_PSEPU Reviewed; 623 AA.
AC A8R3S4;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Quinoprotein ethanol dehydrogenase {ECO:0000303|PubMed:18218017};
DE Short=QEDH {ECO:0000303|PubMed:18218017};
DE EC=1.1.2.8 {ECO:0000305|PubMed:18218017, ECO:0000305|PubMed:7730276};
DE AltName: Full=Quinoprotein alcohol dehydrogenase (cytochrome c) {ECO:0000305};
DE AltName: Full=Quinoprotein alcohol dehydrogenase (cytochrome c550) {ECO:0000305};
DE AltName: Full=Quinoprotein alcohol dehydrogenase ADH I {ECO:0000303|PubMed:7730276};
DE Short=ADH I {ECO:0000303|PubMed:7730276};
DE Flags: Precursor;
GN Name=qedA {ECO:0000303|PubMed:18218017};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, DISRUPTION
RP PHENOTYPE, PATHWAY, AND SUBCELLULAR LOCATION.
RC STRAIN=HK5;
RX PubMed=18218017; DOI=10.1111/j.1574-6968.2008.01060.x;
RA Promden W., Vangnai A.S., Pongsawasdi P., Adachi O., Matsushita K.,
RA Toyama H.;
RT "Disruption of quinoprotein ethanol dehydrogenase gene and adjacent genes
RT in Pseudomonas putida HK5.";
RL FEMS Microbiol. Lett. 280:203-209(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=HK5;
RX PubMed=7730276; DOI=10.1128/jb.177.9.2442-2450.1995;
RA Toyama H., Fujii A., Matsushita K., Shinagawa E., Ameyama M., Adachi O.;
RT "Three distinct quinoprotein alcohol dehydrogenases are expressed when
RT Pseudomonas putida is grown on different alcohols.";
RL J. Bacteriol. 177:2442-2450(1995).
RN [3]
RP INDUCTION.
RC STRAIN=HK5;
RX PubMed=19202108; DOI=10.1099/mic.0.021956-0;
RA Promden W., Vangnai A.S., Toyama H., Matsushita K., Pongsawasdi P.;
RT "Analysis of the promoter activities of the genes encoding three
RT quinoprotein alcohol dehydrogenases in Pseudomonas putida HK5.";
RL Microbiology 155:594-603(2009).
CC -!- FUNCTION: Catalyzes the oxidation of ethanol and other primary alcohols
CC to the corresponding aldehydes, except methanol, which is not a
CC substrate (PubMed:7730276). Uses a specific inducible cytochrome c550,
CC encoded by the adjacent gene in the locus, as electron acceptor (By
CC similarity). Is a key enzyme of the carbon and energy metabolism during
CC growth of P.putida on ethanol as the sole carbon and energy source
CC (PubMed:18218017). Displays lower activity on secondary alcohols,
CC aldehydes and diols. Is not active with sugar alcohols such as glycerol
CC and D-sorbitol (PubMed:7730276). In vitro, reacts well with phenazine
CC methosulfate (PMS) as an electron acceptor but not with NAD(P),
CC potassium ferricyanide, or molecular oxygen (PubMed:7730276).
CC {ECO:0000250|UniProtKB:Q9Z4J7, ECO:0000269|PubMed:18218017,
CC ECO:0000269|PubMed:7730276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + 2 Fe(III)-[cytochrome c] = an aldehyde + 2
CC Fe(II)-[cytochrome c] + 2 H(+); Xref=Rhea:RHEA:51020, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.1.2.8; Evidence={ECO:0000305|PubMed:18218017,
CC ECO:0000305|PubMed:7730276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51021;
CC Evidence={ECO:0000269|PubMed:18218017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + 2 Fe(III)-[cytochrome c] = acetaldehyde + 2 Fe(II)-
CC [cytochrome c] + 2 H(+); Xref=Rhea:RHEA:62200, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000305|PubMed:18218017, ECO:0000305|PubMed:7730276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62201;
CC Evidence={ECO:0000269|PubMed:18218017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + ethanol = acetaldehyde + AH2; Xref=Rhea:RHEA:33567,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15343, ChEBI:CHEBI:16236,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000269|PubMed:7730276};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-propanol + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome
CC c] + 2 H(+) + propanal; Xref=Rhea:RHEA:62204, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:28831, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000305|PubMed:7730276};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:7730276};
CC Note=Binds 1 PQQ group non-covalently per subunit (PubMed:7730276). PQQ
CC is inserted between disulfide Cys-139-Cys-140 and the plane of Trp-282
CC (By similarity). {ECO:0000250|UniProtKB:Q9Z4J7,
CC ECO:0000269|PubMed:7730276};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9Z4J7};
CC Note=Binds 2 calcium ions per subunit. One is located in the active-
CC site cavity near PQQ and the second calcium binds at the N-terminus and
CC contributes to the stability of the native enzyme.
CC {ECO:0000250|UniProtKB:Q9Z4J7};
CC -!- ACTIVITY REGULATION: Enhanced by the presence of ethylamine or NH4(+)
CC ions. {ECO:0000269|PubMed:7730276}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.163 mM for ethanol {ECO:0000269|PubMed:7730276};
CC KM=1.62 mM for butan-1-ol {ECO:0000269|PubMed:7730276};
CC KM=24.9 mM for propane-1,2-diol {ECO:0000269|PubMed:7730276};
CC Vmax=26.3 umol/min/mg enzyme with ethanol as substrate
CC {ECO:0000269|PubMed:7730276};
CC Vmax=21.5 umol/min/mg enzyme with butan-1-ol as substrate
CC {ECO:0000269|PubMed:7730276};
CC Vmax=12.3 umol/min/mg enzyme with propane-1,2-diol as substrate
CC {ECO:0000269|PubMed:7730276};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:7730276};
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7730276}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:18218017}.
CC -!- INDUCTION: Induced by ethanol, and to a lesser extent, by 1-propanol
CC and other alcohols (PubMed:7730276, PubMed:19202108). Repressed by
CC lactate, acetate and tricarboxylic acid cycle intermediates such as
CC citrate and succinate (PubMed:19202108). Up-regulated by exaE and agmR
CC (PubMed:18218017, PubMed:19202108). {ECO:0000269|PubMed:18218017,
CC ECO:0000269|PubMed:19202108, ECO:0000269|PubMed:7730276}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a strong reduction
CC in the growth rate on ethanol, however growth on 1-butanol or 1,2-
CC propanediol is not influenced. {ECO:0000269|PubMed:18218017}.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB333783; BAF91141.1; -; Genomic_DNA.
DR AlphaFoldDB; A8R3S4; -.
DR SMR; A8R3S4; -.
DR KEGG; ag:BAF91141; -.
DR UniPathway; UPA00780; UER00767.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0052934; F:alcohol dehydrogenase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd10277; PQQ_ADH_I; 1.
DR InterPro; IPR034119; ADHI.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR001479; Quinoprotein_DH_CS.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Metal-binding; Oxidoreductase; Periplasm; PQQ;
KW Repeat; Signal; WD repeat.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..623
FT /note="Quinoprotein ethanol dehydrogenase"
FT /evidence="ECO:0000269|PubMed:18218017"
FT /id="PRO_0000419533"
FT REPEAT 515..556
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 559..601
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REGION 242..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 95
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 145
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 189
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 207..209
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 378
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 523
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT BINDING 587
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
FT DISULFID 139..140
FT /evidence="ECO:0000250|UniProtKB:Q9Z4J7"
SQ SEQUENCE 623 AA; 68727 MW; 08435869960257CE CRC64;
MTIRSLPAAL SPLSMAVQAV LLVSSLALAP AANAKPVTWE DIANDHLNTQ NVLQYGMGTN
AQRWSPLAMV NDKNVFKLTP AWSYSFGDER QRGQESQAII NDGVIYVTGS YSRVFALDAK
TGRRLWTYNH RLPDNIRPCC DVVNRGAAIF GDKIYFGTLD ARVIALNKDT GKVVWNKKFG
DHSAGYTMTG APTLIKDQKS GKVLLIHGSS GDEFGVVGQL YARDPETGEE VWMRPFVEGH
MGRLNGKDST PTGDVKAPSW PDDPTTETGK VESWSHGGGA PWQSASFDPE TNTIIVGAGN
PGPWNTWART SKDGNPHDFD SLYTSGQVGV DPTTGEVKWF YQHTPNDAWD FSGNNELVLF
DYKDKDGKQY KATAHADRNG FFYVVDRTNG KLKNAFPFVD NITWASHIDL KTGRPVENEG
QRPAKPLPGE TKGKPVEVSP PFLGGKNWNP MAYSQDTGLF YVPANHWKEE YWTEEVNYKK
GSAYLGIGFR IKRMYEDHVG SLRAMDPTTG KVVWEHNERL PLWAGVLATK GNLVFTGTGD
GYFKAFNAKT GEELWKFQTG SGIVSPPITW EQDGEQYIGV TVGYGGAVPL WGGDMAELTK
PVAQGGSFWV FKIPAWDTKT AKR
