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Database: UniProt
Entry: A0A1X7DPY7_9PROT
LinkDB: A0A1X7DPY7_9PROT
Original site: A0A1X7DPY7_9PROT 
ID   A0A1X7DPY7_9PROT        Unreviewed;       637 AA.
AC   A0A1X7DPY7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Alcohol dehydrogenase (Cytochrome c) {ECO:0000313|EMBL:SMF19305.1};
GN   ORFNames=SAMN02982917_0792 {ECO:0000313|EMBL:SMF19305.1};
OS   Azospirillum oryzae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF19305.1, ECO:0000313|Proteomes:UP000192936};
RN   [1] {ECO:0000313|EMBL:SMF19305.1, ECO:0000313|Proteomes:UP000192936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2P {ECO:0000313|EMBL:SMF19305.1,
RC   ECO:0000313|Proteomes:UP000192936};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FXAK01000001; SMF19305.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7DPY7; -.
DR   STRING; 286727.SAMN02982917_0792; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000192936; 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   CDD; cd10277; PQQ_ADH_I; 1.
DR   Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 1.
DR   InterPro; IPR034119; ADHI.
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; PF01011; PQQ; 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 5.
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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR617512-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   PQQ {ECO:0000256|ARBA:ARBA00022891, ECO:0000256|PIRSR:PIRSR617512-2}.
FT   REGION          255..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        354
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         108
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         158
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         202
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         226
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         311
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         354
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         462..463
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   DISULFID        152..153
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   637 AA;  69079 MW;  266C2CF8D341586E CRC64;
     MTLSSYSTSA GSTNSGTKPR RRVHLAGVAG VIAALFLAAA PAGPALASEV TWDAIANDAK
     NTGDVLMYGM GVEGKRFSPL KQINAESVSR LVPAWSFSFG DEKQRGQETQ ALVHDGVIYV
     TASYSRMFAL DAKTGKRLWS YAHRLPDDIR PCCDVVNRGA AIYGDKLFFG TLDASIVALN
     KDTGKVVWKK KFADHKVGYT MTGAPTIVKD QKTGKVLLIH GSSGDEFGVV GRLFARDPDT
     GEEIWMRPLV EGHMGRLNGK DSTPTGSDKA PSWPRDKDGN LVEAWNHGGG APWQSATFDV
     ETNTIVIGTG NPAPWNGWAR WPGDSLYTSG QAYVDPTTGE LKGFYQHTPN DTWDFSGNNE
     LVLFDYTDAA GKTVKATAHA DRNGFFYVTD RTKLATAGGE PNKPNSVIAA YPFVDGITWA
     KGIDLKTGRP IENEGQRPPL PAEGEKRGKP VEVSPPFLGG KNWNPMSYSE DTKLFYIAAN
     HWKEDYWTEH VGYNPGSAYL GMGFRIHKMF DDHVGSLRAL DPKTGKIVWE HKEELPLWAG
     TLATAGNLVF TGTGDGFVKA FNAKTGEELW HFQTGSGIVS SPVTWEQDGV QYVGITTGYG
     GAVPLWGGDL ADLTTRVTQG GSFWVFKLAD VKVSSTK
//
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