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Database: UniProt
Entry: D0IEM8_9VIBR
LinkDB: D0IEM8_9VIBR
Original site: D0IEM8_9VIBR 
ID   D0IEM8_9VIBR            Unreviewed;       442 AA.
AC   D0IEM8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Quino(Hemo)protein alcohol dehydrogenase PQQ-dependent {ECO:0000313|EMBL:EEZ00031.1};
DE            EC=1.1.99.8 {ECO:0000313|EMBL:EEZ00031.1};
GN   ORFNames=VOA_000078 {ECO:0000313|EMBL:EEZ00031.1};
OS   Vibrio sp. RC586.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=675815 {ECO:0000313|EMBL:EEZ00031.1, ECO:0000313|Proteomes:UP000006226};
RN   [1] {ECO:0000313|EMBL:EEZ00031.1, ECO:0000313|Proteomes:UP000006226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC586 {ECO:0000313|EMBL:EEZ00031.1,
RC   ECO:0000313|Proteomes:UP000006226};
RG   Los Alamos National Laboratory (LANL);
RG   National Microbial Pathogen Data Resource (NMPDR);
RA   Chertkov O., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA   Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA   Bartels D., Vonstein V.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR617512-3};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR617512-3};
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000256|PIRSR:PIRSR617512-2};
CC       Note=Binds 1 PQQ group per subunit. {ECO:0000256|PIRSR:PIRSR617512-2};
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008156}.
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DR   EMBL; ADBD01000007; EEZ00031.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0IEM8; -.
DR   eggNOG; COG4993; Bacteria.
DR   Proteomes; UP000006226; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
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   NCBIfam; TIGR03075; PQQ_enz_alc_DH; 1.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   PANTHER; PTHR32303:SF20; QUINOPROTEIN ETHANOL DEHYDROGENASE; 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 4.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR617512-3};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR617512-4};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR617512-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EEZ00031.1};
KW   PQQ {ECO:0000256|ARBA:ARBA00022891, ECO:0000256|PIRSR:PIRSR617512-2};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..442
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003009198"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         85
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         135
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         179
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         197
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         279
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         321
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         418..419
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   DISULFID        129..130
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   442 AA;  48588 MW;  13CCA889EB9E6031 CRC64;
     MKGNPTYLRC TLLSASILTS LTAWAGVTDK DILQDASTPE DVVSYGIGPQ AQRYSSIDLL
     NTENIQELRP VWAFSLGGEK QRGQESQPMI RDGVMYITGS YSRVYAINAK TGDEIWQYDA
     RLPDGIVPCC DVVNRGVAMY DDLVIFGTLD AKLVALDAKT GNVRWKKTVE DYRAGYSITA
     APIVVKGKVI TGVSGGEFGI VGKVRAYDAK TGELVWERPT VEGHMGYVWK DGKRVDNGIS
     GGKAGTTWPA DLWQTGGAAP WLGGTYDPET DLLYFGTGNP APWNSHMRPG DNLFSSSRLA
     IDPDDGKIVW HFQTTPHDGW DFDGVNELIP FDYQQNGKTV QAAASADRNG FFYVLNRTNG
     DFIRGFPFVD KITWAKGLDE KGRPIYIDSN RPGNPQNSKD GKQGQTVVAA PSFLGGKNWM
     PMAFSKHTGY FYVPFVHPYT SL
//
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