ID A0A1C2H3I8_9RHOB Unreviewed; 704 AA.
AC A0A1C2H3I8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:OCX58152.1};
GN ORFNames=BFP70_19015 {ECO:0000313|EMBL:OCX58152.1};
OS Thioclava sp. SK-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX58152.1, ECO:0000313|Proteomes:UP000094269};
RN [1] {ECO:0000313|EMBL:OCX58152.1, ECO:0000313|Proteomes:UP000094269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-1 {ECO:0000313|EMBL:OCX58152.1,
RC ECO:0000313|Proteomes:UP000094269};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Thioclava sp. strain SK-1.";
RL Submitted (AUG-2016) 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:OCX58152.1}.
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DR EMBL; MDHA01000089; OCX58152.1; -; Genomic_DNA.
DR RefSeq; WP_066013630.1; NZ_MDHA01000089.1.
DR AlphaFoldDB; A0A1C2H3I8; -.
DR STRING; 1889770.BFP70_19015; -.
DR Proteomes; UP000094269; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000094269};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..704
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008662667"
FT REGION 26..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 76107 MW; 7622FBA9161BFDBB CRC64;
MIRYSFPLAV AILGLVPLHG HAQDTAMPEP AAPATAVDTP PAASEAGAVA QTDTASNTGA
QSDPADLLPG VADPILNPEG RTRSDIPLVP ETATWDGFHG QLNAQKYSPL TQITVDNVKD
LEKVWDIHTG DVSDGSGDLA ATVWSATPVF ANDTLYLGTP FYRILALDPA TGAEKWHFNT
DSALEPLTQP ALKNRGVAYW ENPTPVEGAT CQKIVYIGTM DAQLFAVDAD DGQPCTDFGN
NGVLDVNQWN TVNDRFPFSV LQPPTVAGNH VVLGWAGKDW EYAEAPPGAV FSVDPQTGEL
QWSFETLPEE IRRQTGTANV WTAMSVDEGL NLIYLPVASP SPNYWGGNRV EEIPYATSTT
ALDLDTGEVV WSRQWVHHDI WDYDINSAPT LMDITVDGEE IPALMQATKM GFLFVVNRET
GEDVWPIEER PVPQGDGTID GEYYAPTQPF PTKPAPLLDQ SQKPKVWPIA DIVGMGSCSK
LFDDLWYEGM YTPPTTEGEG VLTYPDSAGG VQWGGVAFDP ETQTAVVNTS HIVQYIKLWS
REDYDANAGG SGNENGFYPQ EGAPYGMSLM NALNWLGMPC WEPPFGELVA LDMHTGDVKW
RKPLGSSQQY GFFMPESMGS PTIGGPAVTK GGLVFIGATM DGKARAYDLA TGKELWSDQM
EAPVVANPAI YEYQGKQYVA FVSGGNSILK PAVGDQVAVY ALPN
//
