ID A0A0Q7CXS3_9BURK Unreviewed; 618 AA.
AC A0A0Q7CXS3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Quinonprotein alcohol dehydrogenase {ECO:0000313|EMBL:KQW65640.1};
GN ORFNames=ASC67_14890 {ECO:0000313|EMBL:KQW65640.1};
OS Methylibium sp. Root1272.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1736441 {ECO:0000313|EMBL:KQW65640.1, ECO:0000313|Proteomes:UP000053968};
RN [1] {ECO:0000313|EMBL:KQW65640.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW65640.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW65640.1, ECO:0000313|Proteomes:UP000053968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1272 {ECO:0000313|EMBL:KQW65640.1,
RC ECO:0000313|Proteomes:UP000053968};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQW65640.1}.
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DR EMBL; LMDY01000017; KQW65640.1; -; Genomic_DNA.
DR RefSeq; WP_056324528.1; NZ_LMDY01000017.1.
DR AlphaFoldDB; A0A0Q7CXS3; -.
DR STRING; 1736441.ASC67_14890; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000053968; 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 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..618
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006304477"
FT REGION 237..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT BINDING 89
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 139
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 183
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT BINDING 450..451
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT DISULFID 133..134
FT /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ SEQUENCE 618 AA; 67675 MW; DD5AEE344B1FB231 CRC64;
MSKHPVRHVL SIAAALAVLG LSQGAHAVKN VTWEDISNDD RTSTDVLSYG LGLKAQRYSP
LKQITTVNVQ KLVPAWSHSF GGEKQRGQEG QVLVHDGVIY ATSSYSRFTA IDAKTGRQLW
TYEHRLPDDI RPCCDVVNRG PAIYGDKVYF GTLDARIVAL DRATGKVVWN EKFGDHKVGY
TMTGAPFIVK DKKSGRVLLI HGSSGDEFGV VGWLFARDPD TGAEVWARPM VEGHMGRLNG
KDSTVTGDAK APSWPRDKDG KLVEAWNQGG GAPWQTASFD AENNTIVIGT GNPAPWNTWK
RTKEGDDPRN WDSLFTSGQA YVDASTGELK GFFQHTPNDA WDFSGNNSIV LFEYKDPKSG
KLVKAGAHAD RNGFFFVTDR EKLATGAGYP NKPTALIGAW PFVDGITWAK GFDLKTGKPI
ENNNRPPAPK PGADKGESIF VSPPFLGGTN WMPMSYSPDT GLFYIPANHW AMDYWTENLT
YKAGSAYLGQ GFRIKRLYED HVGTLRAIDP VTGKIAWEHK EKLPLWAGTM TTAGGLLFTG
TSDGYVKAFD SKTGKELWKF QTGSGVVSVP VTWELDGEQY VGIQSGYGGA VPLWGGDMAE
MTKKVTQGGS MWVFRLPK
//
