ADHA_KOMEU
ID ADHA_KOMEU Reviewed; 739 AA.
AC Q44002; O07952;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Alcohol dehydrogenase (quinone), dehydrogenase subunit {ECO:0000250|UniProtKB:O05542};
DE Short=ADH {ECO:0000250|UniProtKB:O05542};
DE EC=1.1.5.5 {ECO:0000250|UniProtKB:O05542};
DE AltName: Full=Alcohol dehydrogenase (quinone), acceptor subunit {ECO:0000250|UniProtKB:O05542};
DE AltName: Full=Alcohol dehydrogenase (quinone), subunit I {ECO:0000250|UniProtKB:O05542};
DE AltName: Full=Ethanol:Q2 reductase {ECO:0000250|UniProtKB:O05542};
DE AltName: Full=G3-ADH subunit I {ECO:0000250|UniProtKB:O05542};
DE AltName: Full=Quinohemoprotein alcohol dehydrogenase {ECO:0000250|UniProtKB:O05542};
DE AltName: Full=Quinohemoprotein-cytochrome c complex {ECO:0000250|UniProtKB:O05542};
DE AltName: Full=Ubiquinol oxidase {ECO:0000250|UniProtKB:O05542};
DE Flags: Precursor;
GN Name=adhA {ECO:0000250|UniProtKB:O05542}; Synonyms=adh;
OS Komagataeibacter europaeus (Gluconacetobacter europaeus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=33995;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51845 / DSM 6160 / JCM 16395 / LMG 18890 / DES 11;
RA Thurner C.A.K.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dehydrogenase component of the alcohol dehydrogenase
CC multicomponent enzyme system which is involved in the production of
CC acetic acid and in the ethanol oxidase respiratory chain.
CC Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of
CC ethanol to acetaldehyde by transferring electrons to the ubiquinone
CC embedded in the membrane phospholipids. The electrons transfer from
CC ethanol to membranous ubiquinone occurs from pyrroloquinoline quinone
CC (PQQ) to one heme c in subunit I (AdhA), and finally to two heme c in
CC subunit II (AdhB). Besides ubiquinone reduction, ADH also has a
CC ubiquinol (QH2) oxidation reaction which mediates electron transfer
CC from ubiquinol to the non-energy generating bypass oxidase system. The
CC electrons transfer occurs from ubiquinol (QH2) to the additional heme c
CC within subunit II (AdhB). {ECO:0000250|UniProtKB:O05542}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + ethanol = a ubiquinol + acetaldehyde;
CC Xref=Rhea:RHEA:26442, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC ChEBI:CHEBI:15343, ChEBI:CHEBI:16236, ChEBI:CHEBI:16389,
CC ChEBI:CHEBI:17976; EC=1.1.5.5;
CC Evidence={ECO:0000250|UniProtKB:O05542};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000250|UniProtKB:O05542};
CC Note=Binds 1 PQQ group per subunit. {ECO:0000250|UniProtKB:O05542};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:O05542};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GR64};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:O05542};
CC Note=Binds 1 heme c group covalently per subunit.
CC {ECO:0000250|UniProtKB:O05542};
CC -!- SUBUNIT: The alcohol dehydrogenase multicomponent enzyme system is
CC composed of a dehydrogenase subunit I (AdhA) and a cytochrome c subunit
CC II (AdhB). {ECO:0000250|UniProtKB:P28036}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X82894; CAA58066.1; -; Genomic_DNA.
DR EMBL; Y09480; CAA70688.1; -; Genomic_DNA.
DR AlphaFoldDB; Q44002; -.
DR SMR; Q44002; -.
DR STRING; 33995.KOEU_13900; -.
DR BRENDA; 1.1.5.5; 40.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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; PS00363; BACTERIAL_PQQ_1; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Calcium; Cell membrane; Disulfide bond; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; PQQ; Respiratory chain; Signal;
KW Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..739
FT /note="Alcohol dehydrogenase (quinone), dehydrogenase
FT subunit"
FT /id="PRO_0000025560"
FT DOMAIN 635..739
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 344
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 97
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 149
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 279
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 299
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 371
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 585
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 651
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 654
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
FT BINDING 655
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:0000250|UniProtKB:Q8GR64"
FT BINDING 694
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:0000250|UniProtKB:Q8GR64"
FT DISULFID 143..144
FT /evidence="ECO:0000250|UniProtKB:Q8GR64"
SQ SEQUENCE 739 AA; 80945 MW; E681BB237ACB91F4 CRC64;
MISAVFGKRR SLSRTLTAGT ICAALISGYA TMASADDGQG ATGEAIIHAD DHPGNWMTYG
RTYSEQRYSP LDQINRSNVG NLKLAWYLDL DTNRGQEGTP LVIDGVMYAT TNWSMMKAVD
AATGKLLWSY DPRVPGNIAD KGCCDTVNRG AAYWNGKVYF GTFDGRLIAL DAKTGKLVWS
VNTIPPEAEL GKQRSYTVDG APRIAKGRVI IGNGGSEFGA RGFVTAFDAE TGKVDWRFFT
APNPKNEPDH TASDSVLMNK AYQTWSPTGA WTRQGGGGTV WDSIVYDPVA DLVYLGVGNG
SPWNYKYRSE GKGDNLFLGS IVALKPETGE YVWHFQETPM DQWDFTSVQQ IMTLDLPING
ETRHVIVHAP KNGFFYIIDA KTGEFISGKN YVYVNWASGL DPKTGRPIYN PDALYTLTGK
EWYGIPGDLG GHNFAAMAFS PKTGLVYIPA QQVPFLYTNQ VGGFTPHPDS WNLGLDMNKV
GIPDSPEAKQ AFVKDLKGWI VAWDPQKQAE AWRVDHKGPW NGGILATGGD LLFQGLANGE
FHAYDATNGS DLFHFAADSG IIAPPVTYLA NGKQYVAVEV GWGGIYPFFL GGLARTSGWT
VNHSRIIAFS LDGKSGPLPK QNDQGFLPVK PPAQFDSKRT DNGYFQFQTY CAACHGDNAE
GAGVLPDLRW SGSIRHEDAF YNVVGRGALT AYGMDRFDGN MNPTEIEDIR QFLIKRANET
YQREVDARKN ADGIPEQLP
