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Database: UniProt
Entry: A0A1Q7T0J9_9BACT
LinkDB: A0A1Q7T0J9_9BACT
Original site: A0A1Q7T0J9_9BACT 
ID   A0A1Q7T0J9_9BACT        Unreviewed;       526 AA.
AC   A0A1Q7T0J9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AUF67_05760 {ECO:0000313|EMBL:OLD82022.1};
OS   Acidobacteria bacterium 13_1_20CM_58_21.
OC   Bacteria; Acidobacteriota.
OX   NCBI_TaxID=1803438 {ECO:0000313|EMBL:OLD82022.1, ECO:0000313|Proteomes:UP000186215};
RN   [1] {ECO:0000313|EMBL:OLD82022.1, ECO:0000313|Proteomes:UP000186215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000256|ARBA:ARBA00001931};
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008156}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLD82022.1}.
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DR   EMBL; MNIJ01000081; OLD82022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7T0J9; -.
DR   Proteomes; UP000186215; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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   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; 3.
DR   SMART; SM00564; PQQ; 6.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..526
FT                   /note="PQQ-dependent dehydrogenase, methanol/ethanol
FT                   family"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012999885"
FT   REGION          349..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   526 AA;  56890 MW;  98A1470340035247 CRC64;
     MQLASMALLG LGGLASSARA QVTPQRLLDS GKEPQNWLMY SGDYAGHRFS ALDQINAPNA
     AMLVPKWVYQ TMAGGKFETT PLVVDGILYG TGQDNRAFAL DARSGRPIWQ YQRALAADIR
     PCCGRVNRGM AILGDKVFLG TLDAHIIALD AKTGSVVWDA TSADYRNGYS ITLAPLVIKN
     LVLIGVSGGE YGIRGFIDAY DAATGERKWR FYTIPGPGEA GHETWEGESW KIGGAPAWIT
     GTYDPATNTT FWTTGNPSPS NRGEGRAGDN LYSNSLLALD PDTGKLKWYF QFSKHDEHDY
     DATQVPVMVD QGDQHVIVQA NRNGFFYLID RTNGKVVFAN PFAKETWSDS KDASGAPIAR
     KDASPTLEGN RVCPGAAGAT NWMSPTYDPQ TRLFYVTARE QCDVFSTAPQ PYEAGHAFYG
     SAYFPNDDAE PFTGALRAID PHTGKLKWEW KHLSPTWSGV LSTAGGLVFT GDAEGNFIAL
     EAASGKALWH FQCGASVYSS PMSFAIDGKQ YVAVAAGSAL FAFSLP
//
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