ADHB_KOMEU
ID ADHB_KOMEU Reviewed; 468 AA.
AC P0A389; Q03318;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Alcohol dehydrogenase (quinone), cytochrome c subunit {ECO:0000250|UniProtKB:Q47945};
DE Short=ADH {ECO:0000250|UniProtKB:Q47945};
DE EC=1.1.5.5 {ECO:0000250|UniProtKB:Q47945};
DE AltName: Full=Alcohol dehydrogenase (quinone), subunit II {ECO:0000250|UniProtKB:Q47945};
DE AltName: Full=Cytochrome c-553 {ECO:0000250|UniProtKB:Q47945};
DE AltName: Full=Cytochrome c553 {ECO:0000250|UniProtKB:Q47945};
DE AltName: Full=Ethanol:Q2 reductase {ECO:0000250|UniProtKB:Q47945};
DE AltName: Full=G3-ADH subunit II {ECO:0000250|UniProtKB:Q47945};
DE AltName: Full=Quinohemoprotein-cytochrome c complex {ECO:0000250|UniProtKB:Q47945};
DE AltName: Full=Ubiquinol oxidase {ECO:0000250|UniProtKB:Q47945};
DE Flags: Precursor;
GN Name=adhB {ECO:0000250|UniProtKB:Q47945};
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: Cytochrome c 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:Q47945}.
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:Q47945};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:Q47945};
CC Note=Binds 3 heme c groups covalently per subunit.
CC {ECO:0000250|UniProtKB:Q47945};
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:Q47945}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
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DR EMBL; Y09480; CAA70689.1; -; Genomic_DNA.
DR AlphaFoldDB; P0A389; -.
DR STRING; 33995.KOEU_13890; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion 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; -; 3.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR014353; Membr-bd_ADH_cyt_c.
DR Pfam; PF00034; Cytochrom_C; 1.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR PIRSF; PIRSF000018; Mb_ADH_cyt_c; 1.
DR SUPFAM; SSF46626; SSF46626; 3.
DR PROSITE; PS51007; CYTC; 3.
PE 3: Inferred from homology;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Repeat; Respiratory chain; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..468
FT /note="Alcohol dehydrogenase (quinone), cytochrome c
FT subunit"
FT /id="PRO_0000006595"
FT DOMAIN 31..134
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 178..293
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 317..407
FT /note="Cytochrome c 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 45
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 48
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 49
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 193
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 196
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 197
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 330
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 333
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 334
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 468 AA; 49758 MW; 94269A33D7242FBE CRC64;
MINRLKVTFS AAAFSLLAGT ALAQTPDADS ALVQKGAYVA RLGDCVACHT ALHGQSYAGG
LEIKSPIGTI YSTNITPDPT YGIGRYTFAE FDEAVRHGIR KDGSTLYPAM PYPSFSRMTK
EDMQALYAYF MHGVKPVAQP DKQPDISWPL SMRWPLGIWR MMFSPSPKDF TPAPGTDPEI
ARGDYLVTGP GHCGACHTPR GFAMQEKALD AAGGPDFLSG GAPIDNWVAP SLRNDPVVGL
GRWSEDDIYT FLKSGRIDHS AVFGGMGDVV AWSTQYFTDD DLHAIAKYLK SLPPVPPSQG
NYTYDPSTAN MLASGNTASV PGADTYVKEC AICHRNDGGG VARMFPPLAG NPVVVTENPT
SLVNVIAHGG VLPPSNWAPS AVAMPGYSKS LSAQQIADVV NFIRTSWGNK APGTVTAADV
TKLRDTGAPV SSSGWNSVSS GWSVFLPQPY GSGWTFAPQT HTGQDAAQ
