P46336 (IOLS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein IolS
EC=1.1.1.-

Alternative name(s):
AKR11A
Vegetative protein 147
Short name=VEG147

Gene names

Name:	iolS
Synonyms:	yxbF
Ordered Locus Names:	BSU39780
ORF Names:	SS92ER

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	310 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Pathway	Polyol metabolism; myo-inositol degradation into acetyl-CoA.
Induction	Inositol.
Sequence similarities	Belongs to the aldo/keto reductase 2 family.

Ontologies

Keywords
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular function	oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 310

310

Protein IolS

PRO_0000070382

Regions

Nucleotide binding

204 – 214

11

NADP

Sites

Active site

53

1

Active site

58

1

Proton donor

Active site

84

1

Secondary structure

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310

Helix Strand Turn

Details...

Turn

26 – 28

3

Helix

34 – 46

13

Beta strand

51 – 53

3

Turn

56 – 61

6

Helix

62 – 71

10

Helix

76 – 78

3

Beta strand

80 – 85

6

Beta strand

87 – 90

4

Beta strand

93 – 96

4

Helix

100 – 114

15

Beta strand

119 – 124

6

Beta strand

129 – 131

3

Helix

133 – 145

13

Beta strand

148 – 150

3

Beta strand

152 – 156

5

Helix

159 – 165

7

Turn

166 – 168

3

Beta strand

173 – 177

5

Helix

184 – 186

3

Helix

189 – 196

8

Beta strand

199 – 204

6

Turn

205 – 209

5

Helix

210 – 212

3

Helix

226 – 229

4

Helix

231 – 233

3

Helix

235 – 246

12

Helix

249 – 254

6

Helix

259 – 269

11

Helix

283 – 290

8

Helix

291 – 294

4

Helix

299 – 308

10

Sequences

	Sequence		Length	Mass (Da)
	P46336 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: A870F226F8684867	FASTA	310	35,168
	10 20 30 40 50 60 MKKAKLGKSD LQVFPIGLGT NAVGGHNLYP NLNEETGKEL VREAIRNGVT MLDTAYIYGI 70 80 90 100 110 120 GRSEELIGEV LREFNREDVV IATKAAHRKQ GNDFVFDNSP DFLKKSVDES LKRLNTDYID 130 140 150 160 170 180 LFYIHFPDEH TPKDEAVNAL NEMKKAGKIR SIGVSNFSLE QLKEANKDGL VDVLQGEYNL 190 200 210 220 230 240 LNREAEKTFF PYTKEHNISF IPYFPLVSGL LAGKYTEDTT FPEGDLRNEQ EHFKGERFKE 250 260 270 280 290 300 NIRKVNKLAP IAEKHNVDIP HIVLAWYLAR PEIDILIPGA KRADQLIDNI KTADVTLSQE 310 DISFIDKLFA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons." Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y. DNA Res. 2:61-69(1995) [PubMed: 7584049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / BGSC1A1.
[2]	"Organization and transcription of the myo-inositol operon, iol, of Bacillus subtilis." Fujita Y., Shibayama T., Ishio I., Aoyama D., Yoshida K. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / BGSC1A1.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis." Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M. Electrophoresis 18:1451-1463(1997) [PubMed: 9298659] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-20. Strain: 168 / IS58.
[5]	"Structural and catalytic diversity in the two family 11 aldo-keto reductases." Ehrensberger A.H., Wilson D.K. J. Mol. Biol. 337:661-673(2004) [PubMed: 15019785] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB005554 Genomic DNA. Translation: BAA21607.1.
AL009126 Genomic DNA. Translation: CAB16014.1.

PIR

D69646.

RefSeq

NP_391857.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PYF	X-ray	1.80	A	1-310	[»]
1PZ0	X-ray	2.35	A	1-310	[»]

ProteinModelPortal

P46336.

SMR

P46336. Positions 2-310.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000003249; EBBACP00000003249; EBBACG00000003242.

GeneID

937636.

GenomeReviews

Gene locus BSU39780 in contig AL009126_GR.

KEGG

bsu:BSU39780.

NMPDR

fig|224308.1.peg.3983.

PATRIC

18980020. VBIBacSub10457_4172.

Organism-specific databases

GenoList

BSU39780. [Micado]

Phylogenomic databases

GeneTree

EBGT00070000031909.

HOGENOM

HBG605727.

OMA

GEYNLLN.

PhylomeDB

P46336.

ProtClustDB

CLSK888176.

Enzyme and pathway databases

BioCyc

BSUB:BSU39780-MONOMER.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]

Gene3D

G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.

KO

K06607.

PANTHER

PTHR11732. Aldo/ket_red. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

ProtoNet

Search...

Entry information

Entry name

IOLS_BACSU

Accession

Primary (citable) accession number: P46336

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program