ID F3FNK3_PSESX Unreviewed; 791 AA.
AC F3FNK3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Quinoprotein {ECO:0000313|EMBL:EGH31789.1};
GN ORFNames=PSYJA_23583 {ECO:0000313|EMBL:EGH31789.1};
OS Pseudomonas syringae pv. japonica str. M301072.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH31789.1, ECO:0000313|Proteomes:UP000004471};
RN [1] {ECO:0000313|EMBL:EGH31789.1, ECO:0000313|Proteomes:UP000004471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000256|ARBA:ARBA00001931};
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:EGH31789.1}.
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DR EMBL; AEAH01001059; EGH31789.1; -; Genomic_DNA.
DR AlphaFoldDB; F3FNK3; -.
DR PATRIC; fig|629262.5.peg.3923; -.
DR HOGENOM; CLU_018478_1_0_6; -.
DR Proteomes; UP000004471; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR CDD; cd10280; PQQ_mGDH; 1.
DR Gene3D; 2.140.10.10; Quinoprotein alcohol dehydrogenase-like superfamily; 2.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017511; PQQ_mDH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR NCBIfam; TIGR03074; PQQ_membr_DH; 1.
DR PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 1.
DR Pfam; PF01011; PQQ; 2.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 791 AA; 86167 MW; D344B3B1D249F427 CRC64;
MILKVTGIVI AILSLILLFM GAQLVAAGGS PAYSVIALGL LATATLVFLK RKSALTLYAV
MMWAILIWII YEAGLDKWQW IPRGDLFALI GLWLAMPWVV RPLYQARSST DKRRFHPLLG
GTLGAMLLIV IALMFHDPYP QQGRIDNVAT TRSAESAGRD WAAYGGSNAG QRFSSLDQIN
PDNVGKLSVA WEYHTGDLRD EDKDAGEYTF EATPLKINDR VYVCTPHNEV HALNPQTGQL
AWKYTPEKKR SYLQQHQTCR GVSYYSAASS STGQPQQPAQ CAKRIITATA DARLVALDAD
SGNLCSDFGN GGVIDLSVNM GTIRPHALMQ TSAPLIAGDL IVIGSSIMDN GYNDGNPSGV
IRAYDVITGL LVWNFDPQNP DNTQPISADQ NYPQDTPVAW ATLSADVKNG LVYVPFGNAS
PDETGTRRNP DSNTEQFRDA LVALDLKTGA LRWKFQTSNN DLWDRDNPSQ PSLLDLGKDG
NRQPAVVLPT KVGNIFVLDR LTGEPIVPVD QVSVRTEGGV EGERFAPTPP VSRLNFIPPV
LTEKSMWGVT PFDQMACRIA YNTLRYDGNP WTPATESGSL IYPGNIGVFN WGSVAVDPDR
QLLIAAPVRL AYVYNLIKRP AQAQEKRLFT QEGKPYWNEN FDGDYAIRIS RFASSLAIPC
TAPPWGTMVG VDLTTGKTQW MRRVGTTKNL KTSFMQGRFP VGFPMGMVAH GGPMVTAGGL
AFHGATADNF FRAYDVNSGK VLWEHELPAG GQSIPSTYTG NDGKQYVVIA AGGHGSLGTT
LGDSVIAFRV D
//