NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=IFO 3255 / IAM 12306 / LMG 1487;
DOI=10.1016/S1570-9639(03)00071-2; PubMed=12686146 [NCBI, ExPASy, EBI, Israel, Japan]
Hoshino T., Sugisawa T., Shinjoh M., Tomiyama N., Miyazaki T.;
"Membrane-bound D-sorbitol dehydrogenase of Gluconobacter suboxydans IFO 3255 -- enzymatic and genetic characterization.";
Biochim. Biophys. Acta 1647:278-288(2003).

[2]

PROTEIN SEQUENCE OF 30-39, AND CHARACTERIZATION.
STRAIN=IFO 3257 / LMG 1489;
DOI=10.1128/AEM.69.4.1959-1966.2003; PubMed=12676670 [NCBI, ExPASy, EBI, Israel, Japan]
Matsushita K., Fujii Y., Ano Y., Toyama H., Shinjoh M., Tomiyama N., Miyazaki T., Sugisawa T., Hoshino T., Adachi O.;
"5-keto-D-gluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in gluconobacter species.";
Appl. Environ. Microbiol. 69:1959-1966(2003).

Comments

FUNCTION: Catalyzes the oxidation of glycerol to glycerone. Also acts, more slowly, on a number of other polyols including D-sorbitol, D-arabinitol, D-mannitol, meso-erythritol, adonitol and propylene glycol.
CATALYTIC ACTIVITY: Glycerol + acceptor = glycerone + reduced acceptor.
COFACTOR: PQQ.
SUBCELLULAR LOCATION: Secreted (Probable).
SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
SEQUENCE CAUTION:
- Sequence=BAC02909.1; Type=Frameshift; Positions=317, 325, 339, 354;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB065091; BAC02909.1; ALT_FRAME; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q8KIL1.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13708; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0047955;	Molecular function: glycerol dehydrogenase (acceptor) activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002372; PQQ_repeat.
IPR011047; Quino_AlcDHase-like.
IPR001479; Quinoprotein_DHase_PQQ_bac_CS.
Graphical view of domain structure.

Gene3D

G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 1.

Pfam

PF01011; PQQ; 2.
Pfam graphical view of domain structure.

SMART

SM00564; PQQ; 4.
SMART graphical view of domain structure.

PROSITE

PS00363; BACTERIAL_PQQ_1; FALSE_NEG.
PS00364; BACTERIAL_PQQ_2; FALSE_NEG.

ProtoNet

Q8KIL1.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Oxidoreductase; Secreted; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 29`	`29`
`CHAIN`	`30 740`	`711`	`Glycerol dehydrogenase large subunit.`	`PRO_0000045858`

Sequence information

Length: 740 AA [This is the length of the unprocessed precursor]

Molecular weight: 79499 Da [This is the MW of the unprocessed precursor]

CRC64: E7CD78737CDEDF59 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRRPYLLATA AGLALACSPL IAHAQFAPAG AGGEPSSSVP GPGNASEPTE NSPKSQSYFA 

        70         80         90        100        110        120 
GPSPYAPQAP GVNAANLPDI ESIDPSQVPA MAPQQSANPA RGDWVAYGRD DHQTRYSPLS 

       130        140        150        160        170        180 
EITPENASKL KVAFVYHTGS YPRPGQVNKW AAETTPIKVG DGLYTCSAMN DIIKLDPATG 

       190        200        210        220        230        240 
KQIWRRNVDV KYHSIPYTAA CKGVTYFTSS VVPEGQPCHN RLIEGTLDMR LIAVDAETGD 

       250        260        270        280        290        300 
FCPNFGHGGQ VNLMQGLGES VPGFVSMTAP PPVINGVVVV NHEVLDGQRR WAPSGVIRGY 

       310        320        330        340        350        360 
DAESGKFVWA WDVNNSDDHS QPTGNRHYSR GTPNSWATMT GDNEEGLVYV PTGNSAADYY 

       370        380        390        400        410        420 
SALRSDAENK VSSAVVAIDV KTGSPRWVFQ TAHKDVWDYD IGSQATLMDM PGPDGQTVPA 

       430        440        450        460        470        480 
LIMPTKRGQT FVLDRRTGKP ILPVEERPAP SPGVIPGDPR SPTQPWSVGM PALRVPDLKE 

       490        500        510        520        530        540 
TDMWGMSPID QLFCRIKFRR ANYVGEFTPP SVDKPWIEYP GYNGGSDWGS MSYDPQSGIL 

       550        560        570        580        590        600 
IANWNITPMY DQLVTRKKAD SLGLMPIDDP NFKPGGGGAE GNGAMDGTPY GIVVTPFWDQ 

       610        620        630        640        650        660 
YTGMMCNRPP YGMITAIDMK HGQKVLWQHP LGTARANGPW GLPTGLPWEI GTPNNGGSVV 

       670        680        690        700        710        720 
TGGGLIFIGA ATDNQIRAID EHTGKVVWSA VLPGGGQANP MTYEANGHQY VAIMAGGHHF 

       730        740 
MMTPVSDQLV VYALPDAIKQ

Q8KIL1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools