ADHB_GLUPO
ID ADHB_GLUPO Reviewed; 468 AA.
AC P0A388; Q03318;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Alcohol dehydrogenase (quinone), cytochrome c subunit {ECO:0000303|PubMed:2001402};
DE Short=ADH {ECO:0000303|PubMed:2001402};
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:0000303|PubMed:2001402};
OS Gluconacetobacter polyoxogenes (Acetobacter polyoxogenes).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=439;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=NBI1028;
RX PubMed=2001402; DOI=10.1016/0167-4781(91)90066-u;
RA Tamaki T., Fukaya M., Takemura H., Tayama K., Okumura H., Kawamura Y.,
RA Nishiyama M., Horinouchi S., Beppu T.;
RT "Cloning and sequencing of the gene cluster encoding two subunits of
RT membrane-bound alcohol dehydrogenase from Acetobacter polyoxogenes.";
RL Biochim. Biophys. Acta 1088:292-300(1991).
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 (By
CC similarity). Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the
CC oxidation of ethanol to acetaldehyde by transferring electrons to the
CC ubiquinone embedded in the membrane phospholipids (PubMed:2001402). The
CC electrons transfer from ethanol to membranous ubiquinone occurs from
CC pyrroloquinoline quinone (PQQ) to one heme c in subunit I (AdhA), and
CC finally to two heme c in subunit II (AdhB) (By similarity). Besides
CC ubiquinone reduction, ADH also has a ubiquinol (QH2) oxidation reaction
CC which mediates electron transfer from ubiquinol to the non-energy
CC generating bypass oxidase system (By similarity). The electrons
CC transfer occurs from ubiquinol (QH2) to the additional heme c within
CC subunit II (AdhB) (By similarity). {ECO:0000250|UniProtKB:Q47945,
CC ECO:0000269|PubMed:2001402}.
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:0000305|PubMed:2001402}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
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DR EMBL; D00635; BAA00529.1; -; Genomic_DNA.
DR PIR; S14271; S14271.
DR AlphaFoldDB; P0A388; -.
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 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Repeat; Respiratory chain; Signal;
KW 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_0000006596"
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
