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Database: UniProt
Entry: D8JIW6_ACISD
LinkDB: D8JIW6_ACISD
Original site: D8JIW6_ACISD 
ID   D8JIW6_ACISD            Unreviewed;       809 AA.
AC   D8JIW6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:ADI90579.1};
GN   OrderedLocusNames=AOLE_08450 {ECO:0000313|EMBL:ADI90579.1};
OS   Acinetobacter oleivorans (strain JCM 16667 / KCTC 23045 / DR1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=436717 {ECO:0000313|EMBL:ADI90579.1, ECO:0000313|Proteomes:UP000000392};
RN   [1] {ECO:0000313|EMBL:ADI90579.1, ECO:0000313|Proteomes:UP000000392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16667 / KCTC 23045 / DR1
RC   {ECO:0000313|Proteomes:UP000000392};
RX   PubMed=20639327; DOI=10.1128/JB.00722-10;
RA   Jung J., Baek J.H., Park W.;
RT   "Complete genome sequence of the diesel-degrading Acinetobacter sp. strain
RT   DR1.";
RL   J. Bacteriol. 192:4794-4795(2010).
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; CP002080; ADI90579.1; -; Genomic_DNA.
DR   RefSeq; WP_013197675.1; NC_014259.1.
DR   AlphaFoldDB; D8JIW6; -.
DR   GeneID; 9382112; -.
DR   KEGG; acd:AOLE_08450; -.
DR   PATRIC; fig|436717.3.peg.1680; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_1_0_6; -.
DR   OrthoDB; 9794322at2; -.
DR   Proteomes; UP000000392; Chromosome.
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: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; 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; 4.
DR   SMART; SM00564; PQQ; 5.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS00363; BACTERIAL_PQQ_1; 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   PQQ {ECO:0000256|ARBA:ARBA00022891};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   809 AA;  88072 MW;  FA90C8436D4D7280 CRC64;
     MSESDSKFHI LFKIWCFLLG LVLLATGVFY IVGGGKLVSL GGSWYFLVAG LLITISAFSI
     FRKKALGVWI FAAVFVGTVI WSFVDAGWEF WPLFSRLMFP AGLFAALLFT LPSIRRYQFQ
     TSLASSSYAV GGLVVVGMLI AFYQMFQPHP TVASSGEKLP LVPVDPAKKQ VNWENYGNDA
     GGSRFVALDQ INRDNVHKLK EAWRFRTGDS TTGSGNGAED QMTPLQVGNK VFLCTPHNNI
     FAIDADSGKQ LWKAEVNSKA DAWERCRGVA YFDSTKPLVQ PTLAGANAVT TVATNTACPR
     RLYTNTPDGR LIAVNADNGQ RCADFGVNGT VDLLEGLGAG TKAPRFEVTS APTIAGTTIV
     VGSRIADNVA ADMPGGVIRG YDVITGKLRW AFDARNPDPN YVLKPGETYK RSSANSWAAM
     SYDPQMNTVF LPMGSSSVDI WGGNRNPLDH KYNTSVLALD ATTGKEKWVY QTVHNDLWDF
     DLPMQPSLVD FPLKDGTTKP AVVIGTKSGQ FFVLDRVTGK PLTKVIEQPV KPANIPGEQY
     SATQPRSVEM PQIGNQTLTE SDMWGATPFD QLMCRINFKS MRYEGLFTAP GTDVSLSFPG
     SLGGMNWGSI AFDPTHRYMF VNDMRLGLWV QLMEQTPEDI KIQASGGEKV NTGMGAVPMK
     GTPYKVNKNR FMSALSIPCQ KPPFGTMTAI DMKTRQVAWQ VPLGTVEDTG PMGIKMGLKA
     PIGMPTIGGP MATQGGLVFF AATQDYYLRA FDSSTGKELW KSRMPVGSQG TPISYVSPKT
     GKQFVVVTAG GARQSPDHGD YVIAYSLEQ
//
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