ID   ADHS_GLUOX              Reviewed;         133 AA.
AC   O05544; Q5FSW4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Alcohol dehydrogenase, 15 kDa subunit {ECO:0000303|PubMed:9055427};
DE   AltName: Full=Alcohol dehydrogenase (quinone), subunit III {ECO:0000303|PubMed:9055427};
DE   AltName: Full=G3-ADH subunit III {ECO:0000303|PubMed:9055427};
DE   Flags: Precursor;
GN   Name=adhS {ECO:0000303|PubMed:9055427}; OrderedLocusNames=GOX0756;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-40, FUNCTION,
RP   PYROGLUTAMATE FORMATION AT GLN-25, AND SUBUNIT.
RC   STRAIN=ATCC 621 / DSM 50049 / NBRC 3172 / NCIMB 7069 / NRRL B-72;
RX   PubMed=9055427; DOI=10.1128/aem.63.3.1131-1138.1997;
RA   Kondo K., Horinouchi S.;
RT   "Characterization of the genes encoding the three-component membrane-bound
RT   alcohol dehydrogenase from Gluconobacter suboxydans and their expression in
RT   Acetobacter pasteurianus.";
RL   Appl. Environ. Microbiol. 63:1131-1138(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND SUBUNIT.
RX   PubMed=8617755; DOI=10.1074/jbc.271.9.4850;
RA   Matsushita K., Yakushi T., Toyama H., Shinagawa E., Adachi O.;
RT   "Function of multiple heme c moieties in intramolecular electron transport
RT   and ubiquinone reduction in the quinohemoprotein alcohol dehydrogenase-
RT   cytochrome c complex of Gluconobacter suboxydans.";
RL   J. Biol. Chem. 271:4850-4857(1996).
CC   -!- FUNCTION: Part of the alcohol dehydrogenase multicomponent enzyme
CC       system which is involved in the production of acetic acid and in the
CC       ethanol oxidase respiratory chain. Does not play an obligatory role for
CC       the alcohol dehydrogenase (ADH) activity. {ECO:0000269|PubMed:8617755,
CC       ECO:0000269|PubMed:9055427}.
CC   -!- SUBUNIT: The alcohol dehydrogenase multicomponent enzyme system is
CC       composed of a dehydrogenase subunit I (AdhA), a cytochrome c subunit II
CC       (AdhB) and a subunit III (AdhS). {ECO:0000269|PubMed:8617755,
CC       ECO:0000269|PubMed:9055427}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA19756.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; D86440; BAA19756.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP000009; AAW60532.1; -; Genomic_DNA.
DR   RefSeq; WP_011252329.1; NZ_LT900338.1.
DR   AlphaFoldDB; O05544; -.
DR   STRING; 290633.GOX0756; -.
DR   EnsemblBacteria; AAW60532; AAW60532; GOX0756.
DR   GeneID; 56905074; -.
DR   KEGG; gox:GOX0756; -.
DR   HOGENOM; CLU_1747226_0_0_5; -.
DR   OMA; YTIAMAI; -.
DR   BioCyc; MetaCyc:MON-15244; -.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Membrane;
KW   Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:9055427,
FT                   ECO:0000305|PubMed:8617755"
FT   CHAIN           25..133
FT                   /note="Alcohol dehydrogenase, 15 kDa subunit"
FT                   /id="PRO_0000020626"
FT   REGION          23..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:9055427"
FT   CONFLICT        53..95
FT                   /note="GIMNYCVEQQYVSYDEGNPVLYGLSEKYKATEQTVGNFDYALG -> DITKN
FT                   TAENNNISHKKNKTRPYTRREKNKTTQNTRAKTDNTRA (in Ref. 1; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   133 AA;  14271 MW;  AC90E1C66E35C5CF CRC64;
     MFRRIVPVLG LALGLGLASQ AAMAQEQSPP PPPAVQGTPG KDFTGVSPAN LAGIMNYCVE
     QQYVSYDEGN PVLYGLSEKY KATEQTVGNF DYALGTAGYF DSNGKRFYLV AYTNEDDRRA
     ACHAAVKAAQ PML