ID   DHET_GLUOX              Reviewed;         757 AA.
AC   O05542; Q5FS09;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   16-JUN-2009, entry version 81.
DE   RecName: Full=Alcohol dehydrogenase [acceptor];
DE            EC=1.1.99.8;
DE   AltName: Full=G3-ADH subunit I;
DE   Flags: Precursor;
GN   Name=adhA; OrderedLocusNames=GOX1068;
OS   Gluconobacter oxydans (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 36-50.
RC   STRAIN=ATCC 621 / IFO 3172 / NCIB 7069;
RX   MEDLINE=97208225; PubMed=9055427;
RA   Kondo K., Horinouchi S.;
RT   "Characterization of the genes encoding the three-component membrane-
RT   bound alcohol dehydrogenase from Gluconobacter suboxydans and their
RT   expression in 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).
CC   -!- FUNCTION: Dehydration of primary alcohols (exception: methanol)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: A primary alcohol + acceptor = an aldehyde +
CC       reduced acceptor.
CC   -!- COFACTOR: Binds 1 PQQ group per subunit. PQQ is inserted between
CC       disulfide Cys-141-Cys-142 and the indole ring of Trp-279 (By
CC       similarity).
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 heme group per subunit (By similarity).
CC   -!- SUBUNIT: Heterotrimer (dehydrogenase, cytochrome and protein
CC       adhS), that forms the alcohol dehydrogenase complex.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Periplasmic side (Potential).
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 cytochrome c domain.
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DR   EMBL; D86375; BAA19753.1; -; Genomic_DNA.
DR   EMBL; CP000009; AAW60837.1; -; Genomic_DNA.
DR   RefSeq; YP_191493.1; -.
DR   HSSP; Q46444; 1KB0.
DR   GeneID; 3250283; -.
DR   GenomeReviews; CP000009_GR; GOX1068.
DR   KEGG; gox:GOX1068; -.
DR   NMPDR; fig|290633.1.peg.1038; -.
DR   HOGENOM; O05542; -.
DR   OMA; O05542; MYVTASW.
DR   BioCyc; GOXY290633:GOX1068-MON; -.
DR   BRENDA; 1.1.99.8; 3050.
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:0018468; F:alcohol dehydrogenase (acceptor) activity; IEA:EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR009056; Cyt_c_monohaem.
DR   InterPro; IPR019556; PQQ-dependent_C.
DR   InterPro; IPR019551; PQQ-dependent_N.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR001479; Quinoprotein_DH_CS.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 1.
DR   Pfam; PF01011; PQQ; 6.
DR   Pfam; PF10535; PQQ_C; 1.
DR   Pfam; PF10527; PQQ_N; 1.
DR   SMART; SM00564; PQQ; 6.
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   1: Evidence at protein level;
KW   Calcium; Cell membrane; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Heme; Iron; Membrane; Metal-binding; Oxidoreductase;
KW   PQQ; Pyrrolidone carboxylic acid; Signal.
FT   SIGNAL        1     34
FT   CHAIN        35    757       Alcohol dehydrogenase [acceptor].
FT                                /FTId=PRO_0000025562.
FT   DOMAIN      637    726       Cytochrome c.
FT   ACT_SITE    342    342       Proton acceptor (Potential).
FT   METAL       215    215       Calcium (By similarity).
FT   METAL       297    297       Calcium (By similarity).
FT   METAL       657    657       Iron (heme axial ligand) (By similarity).
FT   BINDING     653    653       Heme (covalent) (By similarity).
FT   BINDING     656    656       Heme (covalent) (By similarity).
FT   MOD_RES      35     35       Pyrrolidone carboxylic acid.
FT   DISULFID    141    142       By similarity.
FT   CONFLICT    230    230       G -> S (in Ref. 1; BAA19753).
FT   CONFLICT    675    675       A -> R (in Ref. 1; BAA19753).
SQ   SEQUENCE   757 AA;  82853 MW;  56B3940B711BB0CC CRC64;
     MTSGLLTPIK VTKKRLLSCA AALAFSAAVP VAFAQEDTGT AITSSDNGGH PGDWLSYGRS
     YSEQRYSPLD QINTENVGKL KLAWHYDLDT NRGQEGTPLI VNGVMYATTN WSKMKALDAA
     TGKLLWSYDP KVPGNIADRG CCDTVSRGAA YWNGKVYFGT FDGRLIALDA KTGKLVWSVY
     TIPKEAQLGH QRSYTVDGAP RIAKGKVLIG NGGAEFGARG FVSAFDAETG KLDWRFFTVP
     NPENKPDGAA SDDILMSKAY PTWGKNGAWK QQGGGGTVWD SLVYDPVTDL VYLGVGNGSP
     WNYKFRSEGK GDNLFLGSIV AINPDTGKYV WHFQETPMDE WDYTSVQQIM TLDMPVNGEM
     RHVIVHAPKN GFFYIIDAKT GKFITGKPYT YENWANGLDP VTGRPNYVPD ALWTLTGKPW
     LGIPGELGGH NFAAMAYSPK TKLVYIPAQQ IPLLYDGQKG GFKAYHDAWN LGLDMNKIGL
     FDDNDPEHVA AKKDFLKVLK GWTVAWDPEK MAPAFTINHK GPWNGGLLAT AGNVIFQGLA
     NGEFHAYDAT NGNDLYSFPA QSAIIAPPVT YTANGKQYVA VEVGWGGIYP FLYGGVARTS
     GWTVNHSRVI AFSLDGKDSL PPKNELGFTP VKPVPTYDEA RQKDGYFMYQ TFCSACHGDN
     AISGGVLPDL RWSGAPRGRE SFYKLVGRGA LTAYGMDRFD TSMTPEQIED IRNFIVKRAN
     ESYDDEVKAR ENSTGVPNDQ FLNVPQSTAD VPTADHP
//