Reviewed, UniProtKB/Swiss-Prot P94522 (ABNA_BACSU)

Names and origin

Protein names

Recommended name:
    Arabinan endo-1,5-alpha-L-arabinosidase
    EC=3.2.1.99
Alternative name(s):
    Endo-1,5-alpha-L-arabinanase
      Short name=ABN
    Endo-arabinanase

Gene names

Name:	abnA
Ordered Locus Names:	BSU28810

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	323 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 hydrolysis of the alpha-1,5-linked L-arabinofuranoside backbone. Its preferred substrate is linear 1,5-alpha-L-arabinan. It is also active towards branched sugar beet arabinan, but inactive towards larch wood arabinogalactan, wheat arabinoxylan and p-nitrophenyl-alpha-L-arabinofuranoside. The enzyme activity is progressively reduced as 1,5-alpha-chains become shorter or more highly substituted. Ref.4
Catalytic activity	Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.
Pathway	Glycan metabolism; L-arabinan degradation.
Subcellular location	Secreted Potential.
Induction	Induced by arabinose and arabinan and repressed by glucose. Ref.4
Sequence similarities	Belongs to the glycosyl hydrolase 43 family.
biophysicochemical properties	Kinetic parameters: KM=3.5 mM for arabinotetraose (at 27 degrees Celsius and pH 7) KM=5.92 mM for linear 1,5-alpha-L-arabinan (at 37 degrees Celsius and pH 6.6) Vmax=1.31 mmol/min/mg enzyme (at 37 degrees Celsius and pH 6.6) pH dependence: Optimum pH is 6.0. At pH 4.0 the arabinosidase retains about 8% of activity. Temperature dependence: Optimum temperature is 60 degrees Celsius. At 80 degrees Celsius retains about 2% of activity.
Sequence caution	The sequence CAA99586.1 differs from that shown. Reason: Frameshift at position 308. The sequence CAB14841.1 differs from that shown. Reason: Frameshift at position 308.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	arabinan endo-1,5-alpha-L-arabinosidase 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 – 32	32	Potential
	Chain	33 – 323	291	Arabinan endo-1,5-alpha-L-arabinosidase		PRO_0000360437
Experimental info
	Mutagenesis	43	1	H → A: Decrease in binding affinity. Ref.5
	Mutagenesis	44	1	D → A: Loss of arabinosidase activity. Ref.5
	Mutagenesis	104	1	W → A: Significantly less active (10000-fold) than the wild-type arabinosidase against both linear arabinan and arabinooligosaccharides. Ref.5
	Mutagenesis	124	1	F → A: Increase in binding affinity. Ref.5
	Mutagenesis	163	1	D → A: Loss of arabinosidase activity. Ref.5
	Mutagenesis	181	1	F → A: Significantly less active than the wild-type arabinosidase against both linear arabinan (50-fold) and the arabinooligosaccharides (1000-fold). Ref.5
	Mutagenesis	182	1	W → A: Same binding affinity as wild-type. Ref.5
	Mutagenesis	215	1	E → A: Loss of arabinosidase activity. Ref.5 Ref.2
	Sequence conflict	172	1	D → G in AAV87172. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P94522-1 [UniParc]. Last modified January 20, 2009. Version 2. Checksum: 7C1A1B1B0E808C5B	FASTA	323	35,504
	10 20 30 40 50 60 MKKKKTWKRF LHFSSAALAA GLIFTSAAPA EAAFWGASNE LLHDPTMIKE GSSWYALGTG 70 80 90 100 110 120 LTEERGLRVL KSSDAKNWTV QKSIFTTPLS WWSNYVPNYG QNQWAPDIQY YNGKYWLYYS 130 140 150 160 170 180 VSSFGSNTSA IGLASSTSIS SGGWKDEGLV IRSTSSNNYN AIDPELTFDK DDNPWLAFGS 190 200 210 220 230 240 FWSGIKLTKL DKSTMKPTGS LYSIAARPNN GGALEAPTLT YQNGYYYLMV SFDKCCDGVN 250 260 270 280 290 300 STYKIAYGRS KSITGPYLDK SGKSMLEGGG TILDSGNDQW KGPGGQDIVN GNILVRHAYD 310 320 ANDNGIPKLL INDLNWSSGW PSY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism." Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R. Microbiology 142:3067-3078(1996) [PubMed: 8969504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Purification, characterization and functional analysis of an endo-arabinanase (AbnA) from Bacillus subtilis." Leal T.F., de Sa-Nogueira I. FEMS Microbiol. Lett. 241:41-48(2004) [PubMed: 15556708] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-37, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-215. Strain: 168.
[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]	"Transcriptional regulation of genes encoding arabinan-degrading enzymes in Bacillus subtilis." Raposo M.P., Inacio J.M., Mota L.J., de Sa-Nogueira I. J. Bacteriol. 186:1287-1296(2004) [PubMed: 14973026] [Abstract] Cited for: FUNCTION, INDUCTION. Strain: 168.
[5]	"Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A." Proctor M.R., Taylor E.J., Nurizzo D., Turkenburg J.P., Lloyd R.M., Vardakou M., Davies G.J., Gilbert H.J. Proc. Natl. Acad. Sci. U.S.A. 102:2697-2702(2005) [PubMed: 15708971] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 31-323, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-43; ASP-44; TRP-104; PHE-124; ASP-163; PHE-181; TRP-182 AND GLU-215.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z75208 Genomic DNA. Translation: CAA99586.1. Frameshift.
AY669857 Genomic DNA. Translation: AAV87172.1.
Z99118 Genomic DNA. Translation: CAB14841.1. Frameshift.

PIR

E69580.

RefSeq

NP_390759.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UV4	X-ray	1.50	A	31-323	[»]

SMR

P94522. Positions 33-309.

ModBase

Search...

Protein family/group databases

CAZy

GH43. Glycoside Hydrolase Family 43.

Genome annotation databases

GeneID

937430.

GenomeReviews

Gene locus BSU28810 in contig AL009126_GR.

KEGG

bsu:BSU28810.

NMPDR

fig|224308.1.peg.2884.

Organism-specific databases

SubtiList

BG11901. abnA. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

P94522.

Enzyme and pathway databases

BioCyc

BSUB224308:BSU2877-MON.

Family and domain databases

InterPro

IPR006710. Glyco_hydro_43.
[Graphical view]

Pfam

PF04616. Glyco_hydro_43. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ABNA_BACSU

Accession

Primary (citable) accession number: P94522
Secondary accession number(s): Q5MPF4, Q795W7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 20, 2009
Last sequence update:	January 20, 2009
Last modified:	June 16, 2009
This is version 51 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)