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Database: UniProt
Entry: A0A1V4CD95_9BURK
LinkDB: A0A1V4CD95_9BURK
Original site: A0A1V4CD95_9BURK 
ID   A0A1V4CD95_9BURK        Unreviewed;       555 AA.
AC   A0A1V4CD95;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Quinonprotein alcohol dehydrogenase {ECO:0000313|EMBL:OPF62843.1};
GN   ORFNames=BC358_11625 {ECO:0000313|EMBL:OPF62843.1};
OS   Hydrogenophaga sp. H7.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1882399 {ECO:0000313|EMBL:OPF62843.1, ECO:0000313|Proteomes:UP000189907};
RN   [1] {ECO:0000313|Proteomes:UP000189907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H7 {ECO:0000313|Proteomes:UP000189907};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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:OPF62843.1}.
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DR   EMBL; MCIC01000016; OPF62843.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4CD95; -.
DR   STRING; 1882399.BC358_11625; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000189907; 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; 2.
DR   SMART; SM00564; PQQ; 6.
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   PQQ {ECO:0000256|PIRSR:PIRSR617512-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189907};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..555
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011985365"
FT   ACT_SITE        300
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         79
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         130
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         174
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         258
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         300
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         389..390
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         531
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   DISULFID        124..125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   555 AA;  60284 MW;  B5707119BC02B635 CRC64;
     MQQTTRWAGA AALALLATSL HAQSLDDLKR DSATPGDVLT YGMGYNNQRY SPLKQINTGN
     AAKLRPVWAY SLNNPQGQES QPIVHNGVMY VTTHNTTVAI DPATGKQIWK QEIELPQDVF
     KMACCGILNR GAAIYDGKLF RSTLDAHVMA MDAKTGKQLW KSKAADYQNG QAMTSAPLIA
     NGVVLTGIAG GEYGTRGFID GWDPATGKQL WRFYTTAAPD QKGGDTWPGD THLKGGAPTW
     LTGAYDPDLD LVYWGTGNGG PWNPNARKGD NLYIASVVAI RPKTGELVWH YQFSPNDPYD
     YDATEVGMLV DMKIGGKDRK VLAQANRNGF FYVLDRASGE LLAANPYVKV NWAERIDLKT
     GRPVPTETDK KARAGEDVEI FPSVLGGKNW TPMSWNPSTG LAYANTLNIS WPYQLAKPEY
     KKGEWYLGVN FRGVNMPKNE PHGYLSAIDP MTGKSKWQMA WPGQPSMAGT LSTGGGLVFT
     GAATGEFIAV DANNGKKLYE FQTSSGIIGL PVTFEHKGKQ YVTIVSGAGG VWALMGDERM
     SQVPAGGSVW TFAVD
//
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