QHED_COMTE
ID QHED_COMTE Reviewed; 708 AA.
AC Q46444;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Quinohemoprotein alcohol dehydrogenase {ECO:0000303|PubMed:3521592};
DE Short=QH-ADH {ECO:0000303|PubMed:11714714};
DE EC=1.1.9.1 {ECO:0000269|PubMed:3521592};
DE AltName: Full=Alcohol dehydrogenase (azurin) {ECO:0000305};
DE AltName: Full=PQQ-containing alcohol dehydrogenase {ECO:0000303|PubMed:11714714};
DE AltName: Full=PQQ-dependent ADH {ECO:0000303|PubMed:11714714};
DE AltName: Full=Quinohaemoprotein ethanol dehydrogenase type I {ECO:0000303|PubMed:8654419};
DE Short=QH-EDHI {ECO:0000303|PubMed:8654419};
DE Flags: Precursor;
GN Name=qheDH {ECO:0000303|PubMed:8654419};
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 32-54, AND COFACTOR.
RC STRAIN=ATCC 15667 / IAM 12408 / JCM 13048 / LMG 7106 / NCIMB 9682;
RX PubMed=8654419; DOI=10.1111/j.1432-1033.1996.00690.x;
RA Stoorvogel J., Kraayveld D.E., van Sluis C.A., Jongejan J.A., De Vries S.,
RA Duine J.A.;
RT "Characterization of the gene encoding quinohaemoprotein ethanol
RT dehydrogenase of Comamonas testosteroni.";
RL Eur. J. Biochem. 235:690-698(1996).
RN [2]
RP PROTEIN SEQUENCE OF 32-54 AND 477-490, FUNCTION, AND COFACTOR.
RC STRAIN=ATCC 15667 / IAM 12408 / JCM 13048 / LMG 7106 / NCIMB 9682;
RX PubMed=7601151; DOI=10.1111/j.1432-1033.1995.tb20634.x;
RA de Jong G.A.H., Geerlof A., Stoorvogel J., Jongejan J.A., De Vries S.,
RA Duine J.A.;
RT "Quinohaemoprotein ethanol dehydrogenase from Comamonas testosteroni.
RT Purification, characterization, and reconstitution of the apoenzyme with
RT pyrroloquinoline quinone analogues.";
RL Eur. J. Biochem. 230:899-905(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBUNIT, SUBSTRATE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 15667 / IAM 12408 / JCM 13048 / LMG 7106 / NCIMB 9682;
RX PubMed=3521592; DOI=10.1042/bj2340611;
RA Groen B.W., van Kleef M.A., Duine J.A.;
RT "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas
RT testosteroni.";
RL Biochem. J. 234:611-615(1986).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=11679760; DOI=10.1107/s0907444901013002;
RA Oubrie A., Huizinga E.G., Rozeboom H.J., Kalk K.H., de Jong G.A.H.,
RA Duine J.A., Dijkstra B.W.;
RT "Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas
RT testosteroni: crystals with unique optical properties.";
RL Acta Crystallogr. D 57:1732-1734(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) IN COMPLEX WITH HEME C,
RP PYRROLOQUINOLINE QUINONE AND CALCIUM IONS, COFACTOR, ACTIVE SITE, DISULFIDE
RP BOND, AND REACTION MECHANISM.
RX PubMed=11714714; DOI=10.1074/jbc.m109403200;
RA Oubrie A., Rozeboom H.J., Kalk K.H., Huizinga E.G., Dijkstra B.W.;
RT "Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas
RT testosteroni: structural basis for substrate oxidation and electron
RT transfer.";
RL J. Biol. Chem. 277:3727-3732(2002).
CC -!- FUNCTION: Catalyzes the dye-linked oxidation of primary alcohols to the
CC corresponding aldehydes and the (subsequent) oxidation of the aldehydes
CC to carboxylic acids. Methanol is not a substrate.
CC {ECO:0000269|PubMed:3521592, ECO:0000305|PubMed:7601151}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + 2 oxidized [azurin] = an aldehyde + 2 H(+)
CC + 2 reduced [azurin]; Xref=Rhea:RHEA:51148, Rhea:RHEA-COMP:11034,
CC Rhea:RHEA-COMP:11035, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552; EC=1.1.9.1;
CC Evidence={ECO:0000269|PubMed:3521592};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:11714714, ECO:0000269|PubMed:3521592,
CC ECO:0000305|PubMed:7601151, ECO:0000305|PubMed:8654419};
CC Note=Binds 1 PQQ group per subunit (PubMed:3521592, PubMed:11714714).
CC PQQ is inserted between disulfide Cys-147-Cys-148 and the plane of Trp-
CC 276 (PubMed:11714714). {ECO:0000269|PubMed:11714714,
CC ECO:0000269|PubMed:3521592};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11714714, ECO:0000269|PubMed:3521592,
CC ECO:0000305|PubMed:7601151, ECO:0000305|PubMed:8654419};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11714714};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:11714714, ECO:0000269|PubMed:3521592,
CC ECO:0000305|PubMed:7601151, ECO:0000305|PubMed:8654419};
CC Note=Binds 1 heme c group per subunit. {ECO:0000269|PubMed:11714714,
CC ECO:0000269|PubMed:3521592};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for benzyl alcohol {ECO:0000269|PubMed:3521592};
CC KM=5 uM for butan-1-ol {ECO:0000269|PubMed:3521592};
CC KM=5 uM for pentan-1-ol {ECO:0000269|PubMed:3521592};
CC KM=5 uM for octan-1-ol {ECO:0000269|PubMed:3521592};
CC KM=40 uM for octanal {ECO:0000269|PubMed:3521592};
CC KM=60 uM for propan-1-ol {ECO:0000269|PubMed:3521592};
CC KM=100 uM for butyraldehyde {ECO:0000269|PubMed:3521592};
CC KM=200 uM for 6-aminohexan-1-ol {ECO:0000269|PubMed:3521592};
CC KM=280 uM for butan-1,3-diol {ECO:0000269|PubMed:3521592};
CC KM=900 uM for acetaldehyde {ECO:0000269|PubMed:3521592};
CC KM=3 mM for formaldehyde {ECO:0000269|PubMed:3521592};
CC KM=5 mM for ethanol {ECO:0000269|PubMed:3521592};
CC pH dependence:
CC Optimum pH is 7.7. {ECO:0000269|PubMed:3521592};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3521592}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:3521592}.
CC -!- INDUCTION: By ethanol and butanol. {ECO:0000305|PubMed:8654419}.
CC -!- PTM: In the crystallographic structures Trp-543 is oxidized to 2'-
CC hydroxytryptophan. {ECO:0000269|PubMed:11714714}.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
CC -!- CAUTION: The oxidation form of Trp-543 is subject of controversy and
CC could be the artifactual result of sample handling.
CC {ECO:0000305|PubMed:11714714}.
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DR EMBL; X81880; CAA57464.1; -; Genomic_DNA.
DR PIR; S62366; S52317.
DR PDB; 1KB0; X-ray; 1.44 A; A=32-708.
DR PDBsum; 1KB0; -.
DR AlphaFoldDB; Q46444; -.
DR SMR; Q46444; -.
DR DrugBank; DB03051; (S)-2-Tetrahydrofuroic acid.
DR DrugBank; DB03679; 2-Hydroxy-Tryptophan.
DR DrugBank; DB03317; Ferroheme C.
DR DrugBank; DB03205; Pyrroloquinoline Quinone.
DR KEGG; ag:CAA57464; -.
DR BioCyc; MetaCyc:MON-15520; -.
DR BRENDA; 1.1.9.1; 1590.
DR EvolutionaryTrace; Q46444; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
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; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; Heme;
KW Iron; Metal-binding; Oxidoreductase; Periplasm; PQQ; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:7601151,
FT ECO:0000269|PubMed:8654419"
FT CHAIN 32..708
FT /note="Quinohemoprotein alcohol dehydrogenase"
FT /id="PRO_0000025563"
FT DOMAIN 619..708
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 339
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:11714714"
FT BINDING 101
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 153
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 198
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 214..215
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 274
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 366
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 425..426
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 575
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 635
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 638
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 639
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT BINDING 678
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT DISULFID 147..148
FT /evidence="ECO:0000269|PubMed:11714714,
FT ECO:0007744|PDB:1KB0"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 140..145
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 187..190
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 380..387
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 437..444
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 487..494
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 499..509
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 521..525
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 529..535
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 541..546
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 563..570
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 574..579
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 624..634
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 642..644
FT /evidence="ECO:0007829|PDB:1KB0"
FT STRAND 648..650
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 653..655
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 658..662
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 664..668
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 674..676
FT /evidence="ECO:0007829|PDB:1KB0"
FT TURN 682..684
FT /evidence="ECO:0007829|PDB:1KB0"
FT HELIX 689..704
FT /evidence="ECO:0007829|PDB:1KB0"
SQ SEQUENCE 708 AA; 76823 MW; 99AB54BDD6ACCAB3 CRC64;
MERLIDNSHG WPGRMVWLLA ACLGSAAAFA QTGPAAQAAA AVQRVDGDFI RANAARTPDW
PTIGVDYAET RYSRLDQINA ANVKDLGLAW SYNLESTRGV EATPVVVDGI MYVSASWSVV
HAIDTRTGNR IWTYDPQIDR STGFKGCCDV VNRGVALWKG KVYVGAWDGR LIALDAATGK
EVWHQNTFEG QKGSLTITGA PRVFKGKVII GKRGAEYGVR GYITAYDAET GERKWRWFSV
PGDPSKPFED ESMKRAARTW DPSGKWWEAG GGGTMWDSMT FDAELNTMYV GTGNGSPWSH
KVRSPKGGDN LYLASIVALD PDTGKYKWHY QETPGDNWDY TSTQPMILAD IKIAGKPRKV
ILHAPKNGFF FVLDRTNGKF ISAKNFVPVN WASGYDKHGK PIGIAAARDG SKPQDAVPGP
YGAHNWHPMS FNPQTGLVYL PAQNVPVNLM DDKKWEFNQA GPGKPQSGTG WNTAKFFNAE
PPKSKPFGRL LAWDPVAQKA AWSVEHVSPW NGGTLTTAGN VVFQGTADGR LVAYHAATGE
KLWEAPTGTG VVAAPSTYMV DGRQYVSVAV GWGGVYGLAA RATERQGPGT VYTFVVAGKA
RMPEFVAQRT GQLLQGVKYD PAKVEAGTML YVANCVFCHG VPGVDRGGNI PNLGYMDASY
IENLPNFVFK GPAMVRGMPD FTGKLSGDDV ESLKAFIQGT ADAIRPKP
