ID A0A0Q5MJG9_9BURK Unreviewed; 875 AA.
AC A0A0Q5MJG9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:KQR60311.1};
GN ORFNames=ASF94_17945 {ECO:0000313|EMBL:KQR60311.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR60311.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR60311.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR60311.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR60311.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR60311.1,
RC ECO:0000313|Proteomes:UP000051403};
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=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:KQR60311.1}.
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DR EMBL; LMOV01000007; KQR60311.1; -; Genomic_DNA.
DR RefSeq; WP_056662596.1; NZ_LMOV01000007.1.
DR AlphaFoldDB; A0A0Q5MJG9; -.
DR STRING; 1736280.ASF94_17945; -.
DR OrthoDB; 9794322at2; -.
DR Proteomes; UP000051403; 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 PANTHER; PTHR32303; QUINOPROTEIN ALCOHOL DEHYDROGENASE (CYTOCHROME C); 1.
DR PANTHER; PTHR32303:SF4; QUINOPROTEIN GLUCOSE DEHYDROGENASE; 1.
DR Pfam; PF01011; PQQ; 4.
DR SMART; SM00564; PQQ; 6.
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 Reference proteome {ECO:0000313|Proteomes:UP000051403};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 33..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 160..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 92325 MW; 5E0FBDD42129DD52 CRC64;
MAGIARTTGI AVGVIGALLA AGGVWLVALG GSFYYLIAGV VLVGCGVLLA RRRVEALWLY
AVLLAASVVW ALWEVGLDWW PLAARLDVLA VIGLWLLMPW VRRALVVRSP SAPRSRVPQG
TDGPIATPVT ALTITLAATV AIAVVAMFRQ PHDMAGQLTG AAQAPGAAPS ATPPGAAGAV
PDGEWHAYGR TGYGQRFSPL TQITPANASQ LKMAWEYRTG DVRGKDGDPE ETTYEVTPLK
IDNRLFLCTP HQSVIALDAT TGQQLWRYDP KIENKLALQH LTCRGLSYQP PQSGAAPAAT
AATAPASAPA SAPAIAASSP VAAVSAGAAR AEPASHASPT TTQPEAPATQ AADQRQPPIA
ARSGPTDPAC RAKLFMPTAD GRVIALNPES GAVCTNFGGG TGQIDLWQRM PNLRPGAYYS
TSPVVVTQRY VIVGGTVLDN ASVKEQSGVI RAFDIDTGAL VWNWDSGNPD DTAPLPPGRT
YTPNSPNSWS ISSVDEALGM VYVPMGNQPP DQWGGNRSPA VEKYSSSVVA LDVATGRVRW
VFQTVHHDLW DYDVPAQPTL VDLQVRGQTV PALVQPTKQG ELFVLDRRTG TPVLPVTEHP
APQGAAAGDR TAPTQPKSAL SFDPPPLRER NMWGATLFDQ LACRIAFHRL RYEGRFTPPS
EQGSIIYPGN FGVFNWGGIA VDPQRQIVFT TPTYLAFVSK LVPRKDDTSL LVQSGGPPKG
SLPALNENFG APFAASMKPF MSPVGLPCQA PPWGYVAGVD LRTGEVAWKH RNGTVRDLSP
LPLPFRMGVP GIGGPMVTAG GVAFYSGALD NYVRAYDVNS GNRLWEDRLP AGGQATPMSY
TGADGRQYVV VVAGGHGSTG TKAGDAVRAY AVPGN
//
