Reviewed, UniProtKB/Swiss-Prot O31411 (SACC_BACL7)

Names and origin

Protein names	Recommended name:     Levanase     EC=3.2.1.65 Alternative name(s):     Endo-levanase     2,6-beta-D-fructan fructanohydrolase
Organism	Bacillus sp. (strain L7)
Taxonomic identifier	62626 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	921 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the hydrolysis of levan with endo-type specificity. The products of levan hydrolysis are a mixture of fructose and a series of fructooligosaccharides up to 12-mer, with levantriose being the major oligosaccharide obtained. Is not active towards sucrose. Ref.1
Catalytic activity	Random hydrolysis of (2->6)-beta-D-fructofuranosidic linkages in (2->6)-beta-D-fructans (levans) containing more than 3 fructose units.
Enzyme regulation	Is completely inhibited by low concentrations of heavy metal ions, while Ca2+ and Mg2+ or chelating agents such as EDTA neither inhibit nor activate the enzyme to any signicant extent. Ref.1
Subcellular location	Secreted Ref.1.
Sequence similarities	Belongs to the glycosyl hydrolase 32 family.
Caution	Functional characterization has been done on a chimeric protein carrying at its C-terminus a fragment of the cloning vector instead of the levanase sequence.
Biophysicochemical properties	pH dependence: Optimum pH is about 5.5 at 50 degrees Celsius and shows an apparent shift towards higher pH values at higher temperatures.
Sequence caution	The sequence CAA73180.1 differs from that shown. Reason: Frameshift at position 728. The exact location of the frameshift is not clear.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro levanase 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 – 23	23	Potential
	Chain	24 – ›921	›898	Levanase		PRO_0000344252
Regions
	Region	409 – 412	4	Substrate binding By similarity
	Region	460 – 461	2	Substrate binding By similarity
	Region	539 – 540	2	Substrate binding By similarity
Sites
	Active site	412	1	By similarity
	Binding site	428	1	Substrate By similarity
	Binding site	591	1	Substrate By similarity
	Binding site	679	1	Substrate By similarity
Experimental info
	Non-terminal residue	921	1

Sequences

	Sequence		Length	Mass (Da)
	O31411-1 [UniParc]. Last modified July 22, 2008. Version 2. Checksum: 24B04DE96067DC44	FASTA	921	101,206
	10 20 30 40 50 60 MMKWFAKLIL SLSLAVVMAA SSAAISFGAS NSSLDTHASL VTQLDSAASE AAEGKSAMIN 70 80 90 100 110 120 ESAINSNVTG WKLHGKGRME VTGEGLRLTS DPQENVMAIS ETVADDFIYE ADVMVTDPQA 130 140 150 160 170 180 DATLLFRSGE DGWSSYMLQL ALGAGVIRLK DASGGEGVLN VERKVEAKPG DIYHLRVKAE 190 200 210 220 230 240 GTRLQVYWGQ QYEPVIDTEA AAHRTGRLGL HVWNGSALFQ NIRVSDMSGN TLEPISSQGL 250 260 270 280 290 300 WQPDLKGLKG TGEDGLEAKK VFRNHEADVV LEGDLILNGQ GSAGLLFRSN AQGTEGYAAV 310 320 330 340 350 360 LQGEGERVRV YLKKADGTIL HESRVTYPSQ RESRHHLEVK AIGERIQIFV DGYEPAAIDM 370 380 390 400 410 420 VDTAFPSGYH GVMASSGIAY FQDVYITPYA SYYTEKYRPQ YHYSPIRGSA SDPNGLVYFE 430 440 450 460 470 480 GEYHLFHQDG GQWAHAVSRD LIHWKRLPIA LPWNDLGHVW SGSAVADTTN ASGLFGSSGG 490 500 510 520 530 540 KGLIAYYTSY NPDRHNGNQK IGLAYSTDRG RTWKYSEEHP VVIENPGKTG EDPGGWDFRD 550 560 570 580 590 600 PKVVRDEANN RWVMVVSGGD HIRLFTSTNL LNWTLTDQFG YGAYIRGGVW ECPDLFQLPV 610 620 630 640 650 660 EGSKKRKWVL MISTGANPNT QGSDAEYFIG DLTPEGKFIN DNPAGTVLKT DWGKEYYASM 670 680 690 700 710 720 SFSDMPDGRR IMLAWMTNWD YPFSFPTTGW KGQLSIPRQV SLKETEEGIR MHQTPIEELA 730 740 750 760 770 780 QLRSPVLTSP TARWGTSGEN LLKGITSGAY EIEAELELPP TGAASEFGFR LREGDGQRTL 790 800 810 820 830 840 VGYRAAGSKM FVDRSASGMT DFSDLFSTLH EAPLKPEGNR IKLRILVDES SVEVFGNDGR 850 860 870 880 890 900 VVFSDVIFPD PASRGMSFYS EGGKVKVVSL QVHALQHIWR EDEAKEPRVV MDTETLELSL 910 920 GQTKPLFASI DNGQGKGADG I

References

[1]	"Characterization of a novel endo-levanase and its gene from Bacillus sp. L7." Miasnikov A.N. FEMS Microbiol. Lett. 154:23-28(1997) [PubMed: 9297817] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PH DEPENDENCE, ENZYME REGULATION, SUBCELLULAR LOCATION.
[2]	"Levanase gene sequence from strain Bacillus sp. L7." Naumoff D.G. FEMS Microbiol. Lett. 164:227-228(1998) [PubMed: 9675868] [Abstract] Cited for: IDENTIFICATION OF FRAMESHIFT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y12619 Genomic DNA. Translation: CAA73180.1. Frameshift.
3D structure databases
HSSP	HSSP built from PDB template 1UYP based on UniProtKB O33833.
SMR	O31411. Positions 393-879.
ModBase	Search...
Protein family/group databases
CAZy	GH32. Glycoside Hydrolase Family 32.
Family and domain databases
InterPro	IPR008985. ConA-like_lec_gl. IPR010496. DUF1080. IPR001362. Glyco_hydro_32. IPR013189. Glyco_hydro_32_C. IPR013148. Glyco_hydro_32_N. [Graphical view]
Pfam	PF06439. DUF1080. 1 hit. PF08244. Glyco_hydro_32C. 1 hit. PF00251. Glyco_hydro_32N. 1 hit. [Graphical view]
SMART	SM00640. Glyco_32. 1 hit. [Graphical view]
PROSITE	PS00609. GLYCOSYL_HYDROL_F32. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SACC_BACL7

Accession

Primary (citable) accession number: O31411

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	July 22, 2008
Last modified:	January 19, 2010
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)