GenomeNet

Database: UniProt
Entry: A0A418XFE2_9BURK
LinkDB: A0A418XFE2_9BURK
Original site: A0A418XFE2_9BURK 
ID   A0A418XFE2_9BURK        Unreviewed;       575 AA.
AC   A0A418XFE2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=PQQ-dependent dehydrogenase, methanol/ethanol family {ECO:0000313|EMBL:RJG11182.1};
DE            EC=1.1.2.- {ECO:0000313|EMBL:RJG11182.1};
GN   ORFNames=D3872_21050 {ECO:0000313|EMBL:RJG11182.1};
OS   Massilia cavernae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=2320864 {ECO:0000313|EMBL:RJG11182.1, ECO:0000313|Proteomes:UP000284006};
RN   [1] {ECO:0000313|EMBL:RJG11182.1, ECO:0000313|Proteomes:UP000284006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K1S02-61 {ECO:0000313|EMBL:RJG11182.1,
RC   ECO:0000313|Proteomes:UP000284006};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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}.
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:RJG11182.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QYUP01000153; RJG11182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418XFE2; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000284006; 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   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   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; 7.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 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:RJG11182.1}; PQQ {ECO:0000256|PIRSR:PIRSR617512-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000284006};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..575
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019411659"
FT   ACT_SITE        313
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         77
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         127
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         171
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         189
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         271
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         313
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   DISULFID        121..122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   575 AA;  62037 MW;  8CCBA11E94B622F6 CRC64;
     MIGALLGLAA AAFVQAGDVT DAMLANTEKD PKGVLSFGMG SEGQRYSPLS QINTRNVAKL
     TPAWSFSFGG EKQRGQESQP VIHDGRMFVT ASYSRIFAID MRTGAKLWKY EHRLPEGIMP
     CCDVVNRGAA LYGNLVIFGT LDAQLVALDQ ATGKVVWKEK VDDYAAGYSM TAAPLIARGL
     LLTGVSGGEF GVVGRVEARD PMTGQLVWSR PTVEGHMGYT YDKEGKAIEN GISGTTNKSW
     PGDLWKTGGA STWMGGTYDD STGLAYFGTG NPAPWNSHLR PGDNLYSSST VALDVNTGRI
     KWAYQNTPND AWDFDGSNEF VTFDMDGKRY GGKADRNGFF YVIDAKDGKL QNAFPFVHKI
     TWASSIDLKT GRPNFIAANR PGDPTKGDGT KGSTVFSAPA FLGAKNQMPM AYSPQTKLFY
     VPANEWGMDI WNEPISYKKG GAFLGAGFTI KPLFDDYIGA MRAVDPKTGK IVWEVKNNAP
     LWGGVMSTAG GLVFYGTPEG YLKAVDARTG KELWKFQTGS GVVAPPVTWQ DGDTQYVAVV
     SGWGGAVPLW GGEVAKKVNF LEQGGSVWVF KLPKA
//
DBGET integrated database retrieval system