Q8KIL1 (SLDA_GLUTH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycerol dehydrogenase large subunit
EC=1.1.99.22

Alternative name(s):
D-arabitol dehydrogenase large subunit
Short name=ARDH
D-sorbitol dehydrogenase subunit sldA
Short name=SLDH
Gluconate/polyol dehydrogenase large subunit

Gene names

Name:

sldA

Organism

Gluconobacter thailandicus

Taxonomic identifier

257438 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter

Protein attributes

Sequence length	740 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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.
Sequence similarities	Belongs to the bacterial PQQ dehydrogenase family.
Sequence caution	The sequence BAC02909.1 differs from that shown. Reason: Frameshift at positions 317, 325, 339 and 354.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glycerol dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Ref.2
	Chain	30 – 740	711	Glycerol dehydrogenase large subunit		PRO_0000045858

Sequences

	Sequence		Length	Mass (Da)
	Q8KIL1 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: E7CD78737CDEDF59	FASTA	740	79,499
	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

References

[1]

"Membrane-bound D-sorbitol dehydrogenase of Gluconobacter suboxydans IFO 3255 -- enzymatic and genetic characterization." Hoshino T., Sugisawa T., Shinjoh M., Tomiyama N., Miyazaki T. Biochim. Biophys. Acta 1647:278-288(2003) [PubMed: 12686146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NBRC 3255 / JCM 20465 / IAM 12306 / LMG 1487.

[2]

"5-keto-D-gluconate production is catalyzed by a quinoprotein glycerol dehydrogenase, major polyol dehydrogenase, in gluconobacter species." Matsushita K., Fujii Y., Ano Y., Toyama H., Shinjoh M., Tomiyama N., Miyazaki T., Sugisawa T., Hoshino T., Adachi O. Appl. Environ. Microbiol. 69:1959-1966(2003) [PubMed: 12676670] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-39, CHARACTERIZATION. Strain: NBRC 3255 / JCM 20465 / IAM 12306 / LMG 1487.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB065091 Genomic DNA. Translation: BAC02909.1. Frameshift.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13708.
BRENDA	1.1.1.14. 7280.
Family and domain databases
InterPro	IPR019556. PQQ-dependent_C. IPR019551. PQQ-dependent_N. IPR018391. PQQ_beta_propeller_repeat. IPR002372. PQQ_repeat. IPR011047. Quinonprotein_ADH-like. [Graphical view]
Gene3D	G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 2 hits.
Pfam	PF01011. PQQ. 2 hits. PF10535. PQQ_C. 1 hit. PF10527. PQQ_N. 1 hit. [Graphical view]
SMART	SM00564. PQQ. 4 hits. [Graphical view]
SUPFAM	SSF50998. Quin_alc_DH_like. 1 hit.
PROSITE	PS00363. BACTERIAL_PQQ_1. False negative. PS00364. BACTERIAL_PQQ_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SLDA_GLUTH

Accession

Primary (citable) accession number: Q8KIL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	July 27, 2011
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program