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Database: UniProt
Entry: A0A1C3K556_9BURK
LinkDB: A0A1C3K556_9BURK
Original site: A0A1C3K556_9BURK 
ID   A0A1C3K556_9BURK        Unreviewed;       806 AA.
AC   A0A1C3K556;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Quinate/shikimate dehydrogenase [Pyrroloquinoline-quinone] {ECO:0000313|EMBL:SBT26507.1};
DE            EC=1.1.5.8 {ECO:0000313|EMBL:SBT26507.1};
GN   ORFNames=ODI_04280 {ECO:0000313|EMBL:SBT26507.1}, ODI_R0482
GN   {ECO:0000313|EMBL:SOE46815.1};
OS   Orrella dioscoreae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Orrella.
OX   NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT26507.1, ECO:0000313|Proteomes:UP000078558};
RN   [1] {ECO:0000313|EMBL:SBT26507.1, ECO:0000313|Proteomes:UP000078558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT26507.1};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SOE46815.1, ECO:0000313|Proteomes:UP000078558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE46815.1};
RA   de Groot N.N.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FLRC01000033; SBT26507.1; -; Genomic_DNA.
DR   EMBL; LT907988; SOE46815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C3K556; -.
DR   STRING; 1851544.ODI_04280; -.
DR   KEGG; odi:ODI_R0482; -.
DR   Proteomes; UP000078558; Chromosome i.
DR   Proteomes; UP000078558; Unassembled WGS sequence.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047519; F:quinate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
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; 1.
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   InterPro; IPR001479; Quinoprotein_DH_CS.
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; 3.
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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:SBT26507.1}; PQQ {ECO:0000256|ARBA:ARBA00022891};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078558};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          389..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   806 AA;  86111 MW;  C91E6D462573A9A4 CRC64;
     MLATAWRLVL AFLILATGAF FTYYGFQLVT LSGSPYFLIA GILLLLSGIQ IARRKTSGAW
     LYALTFAGTL IWAVADAGLD FWPLVSRLMV LAGLGILVSL SYPLLRTDKQ QDSTPTKRSA
     SKVVAAVLAV ACVATVAGMF MPHAPVSKGE QLALKPVDPA KEQKNWSHYG NTEGGTRFAA
     LDQITRDNVK DLEVAWTYRT GDTPVSPGGG GAEDQQTPLQ IGNRVFLCTP HNNVIALDAT
     TGKELWKTEI NAKQKKWMRC RGLAYFDVAE PLAQPNTEGA SLVLPVSVPA GAICQRRILM
     NSVAPELIAL DADTGAFCPD FGVNGRVDLR AGMGKGADKG EYYPTSAPTL AGTTIVIGGR
     VADNVSTDMP GGVVRGFDVI TGAQRWAFDP GKPQDQAAPA DGQTYTRSTP NVWAPMSYDS
     TSNTVFMPVG SAAVDLWGVK HTALDRKYGA SMLAVDATTG KEKWVYQTVH DDLWDFDVPM
     QPTFADFPNG QGGTTPALIF GTKAGQIFVL DRLTGKPLTQ VEERPVPAGN IQGETYSPTQ
     PFSVGMPSIG ADDLTESDMW GATPFDQLLC RIHFKSKRYT GLFTPPGTDA SLNLPGSLGG
     MNWGGLSIDP VNGLLFVNDM RVGLEVQLVE VSPNVQARKS DGNEAAAISG PVALSGTPYA
     INAKVRFMSQ LEIPCQKPPF GTLSAIDLKT QQMLWQVPVG TVKDTGPFGV KMGLPIPIGM
     PTIGGTMATQ GGLVFIAATQ DYYLRAYDSG TGKEVWKGRL PVGSQATPIS YKSTEDGRQY
     IVISAGGARN SPDRGDYVIA YALPKQ
//
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