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Database: UniProt
Entry: A0A010T661_PSEFL
LinkDB: A0A010T661_PSEFL
Original site: A0A010T661_PSEFL 
ID   A0A010T661_PSEFL        Unreviewed;       591 AA.
AC   A0A010T661;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Quinoprotein ethanol dehydrogenase {ECO:0000313|EMBL:EXF92947.1};
GN   ORFNames=HK44_004385 {ECO:0000313|EMBL:EXF92947.1};
OS   Pseudomonas fluorescens HK44.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF92947.1, ECO:0000313|Proteomes:UP000022611};
RN   [1] {ECO:0000313|EMBL:EXF92947.1, ECO:0000313|Proteomes:UP000022611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK44 {ECO:0000313|EMBL:EXF92947.1,
RC   ECO:0000313|Proteomes:UP000022611};
RX   PubMed=21742869; DOI=10.1128/JB.05530-11;
RA   Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA   Karpinets T.V., Brown S.D., Sayler G.S.;
RT   "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT   genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT   HK44.";
RL   J. Bacteriol. 193:5009-5010(2011).
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:EXF92947.1}.
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DR   EMBL; AFOY02000015; EXF92947.1; -; Genomic_DNA.
DR   RefSeq; WP_019690838.1; NZ_AFOY02000015.1.
DR   AlphaFoldDB; A0A010T661; -.
DR   PATRIC; fig|1042209.11.peg.3234; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_0_0_6; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000022611; 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; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 6.
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   Reference proteome {ECO:0000313|Proteomes:UP000022611};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..591
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001458098"
FT   ACT_SITE        323
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-1"
FT   BINDING         137
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   BINDING         199
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         281
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         323
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-3"
FT   BINDING         417..418
FT                   /ligand="pyrroloquinoline quinone"
FT                   /ligand_id="ChEBI:CHEBI:58442"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-2"
FT   DISULFID        131..132
FT                   /evidence="ECO:0000256|PIRSR:PIRSR617512-4"
SQ   SEQUENCE   591 AA;  64520 MW;  2680F1A1EDE977EE CRC64;
     MTHPVRRQPF ALSVLLSAML LSGSALAAVT DQDILQDPKN PGQVVTNGLG VQGQRYSPLD
     ILNVNNVKEL RPVWAFSFGG EKQRGQQAQP MIKDGVMYMT GSYSRVFAVD AHTGKKLWQY
     DARLPDDIRP CCDVINRGVA LYDDLVIFGT LDAKLVALNK DTGKVVWSKK VADHKEGYSI
     SAAPLVVNGK LITGVAGGEF GVVGKIEAYN PKNGDLLWTR PTVEGHMGYV YKDGKAVENG
     ISGGEAGKTW PGDLWKTGGA APWLGGYYDP ETNLLLFGTG NPAPWNSHLR PGDNLYSSSR
     LALNPDDGTI KWHFQSTPHD GWDFDGVNEL ISFNYKDGGK EIKAAATADR NGFFYVLDRT
     NGKFIRGFPF VDKITWASGL DKDGRPIYNE ASRPGAPGSE EKGSSVFVAP AFLGAKNWMP
     MAYNQDTGLF YVPSNEWGMD IWNEGIAYKK GAAFLGAGFT IKPLNEDYIG VLRAIDPKTG
     KEVWRHKNYA PLWGGVLTTK GNLVFTGTPE GFLQAFNAKT GEKVWEFQTG SGVLGSPITW
     EMDGEQYVSV LSGWGGAVPL WGGEVAKRVK DFNQGGMLWT FKLPKDLVAK H
//
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