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Entry: A0A4Q7LFW5_9BURK
LinkDB: A0A4Q7LFW5_9BURK
Original site: A0A4Q7LFW5_9BURK 
ID   A0A4Q7LFW5_9BURK        Unreviewed;       610 AA.
AC   A0A4Q7LFW5;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=PQQ-dependent dehydrogenase (Methanol/ethanol family) {ECO:0000313|EMBL:RZS52218.1};
GN   ORFNames=EV685_3409 {ECO:0000313|EMBL:RZS52218.1};
OS   Sphaerotilus mobilis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=47994 {ECO:0000313|EMBL:RZS52218.1, ECO:0000313|Proteomes:UP000293433};
RN   [1] {ECO:0000313|EMBL:RZS52218.1, ECO:0000313|Proteomes:UP000293433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10617 {ECO:0000313|EMBL:RZS52218.1,
RC   ECO:0000313|Proteomes:UP000293433};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (FEB-2019) 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:RZS52218.1}.
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DR   EMBL; SGWV01000011; RZS52218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q7LFW5; -.
DR   Proteomes; UP000293433; 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; cd10278; PQQ_MDH; 1.
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:SF22; METHANOL DEHYDROGENASE LARGE SUBUNIT-LIKE PROTEIN; 1.
DR   PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR   Pfam; PF13360; PQQ_2; 1.
DR   SMART; SM00564; PQQ; 4.
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:UP000293433};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..610
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5020293307"
FT   ACT_SITE        332
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         87
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         140
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         184
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         270
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         290
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         332
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   DISULFID        134..135
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   610 AA;  66577 MW;  5FE79D53990EF3B8 CRC64;
     MTSTGNTAGK TGQWLIRGAC VALLGMPALT MANADVEKHI ANPKNWAMQA GDMYNQRYSQ
     LKQINKSNVG KMQVAWTFST GVLRGHEGSP LVVDGTMYLH SPFPNKVFAI DLDTQKILWK
     YEPKQDPAVI PQMCCDTVNR GLAYAEGKVF LQQADSNLIA LDAKSGKLVW TVKNGDPKLG
     AVNTNAPHVF KDKVITGISG GEWGVRGFLA AYDIKTGKQV WKGYSVGPDS EMLMDPDKTT
     TWADGKVTPV GRDSSLKTWQ GDQWKIGGGT TWGWYSYDKA TNAVYYGTGN PSTWNPAQRP
     GDNKWTMSIW SRDVDSGKVN WVYQMTPYDE WDFDGINEMI LADINVKGKL TKALVHFDRN
     GFAYTLDRVS GALLVAEKYD PKVNWATHVD MKSGRPQVVS KYSTAQNGPD VNTKGICPAA
     LGSKDQQPAS YDPETKLFYV PTNHVCMDYE PFKVEYTAGQ PYVGATLSMF PAPGSHGGMG
     NYITWDAGTG KIVQSKAEKF SVWSGSLNTA GGLSCYGTLE GYLKCVDKND INKELFKFKT
     PSGIIGNVFT YEHKGKQYLG VFSGIGGWAG IGMAAGLEKD TDGLGAVGGY RELNQYTELG
     GSLTVFALPN
//
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