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Protein

Extracellular endo-alpha-(1->5)-L-arabinanase 2

Gene

abn2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of the alpha-1,5-L-arabinan to produce arabino-oligosaccharides and L-arabinose. It is also active toward linear branched sugar beet arabinan, and pectin from apple.2 Publications

Catalytic activityi

Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.1 Publication

Cofactori

Ca2+CuratedNote: Binds 1 Ca2+ ion per subunit.Curated

Kineticsi

  1. KM=0.11 mM for linear-alpha-1,5-L-arabinan2 Publications
  2. KM=2 mM for linear-alpha-1,5-L-arabinan (at pH 7.0 and 50 degrees Celsius)2 Publications
  1. Vmax=0.25 mmol/min/mg enzyme for linear-alpha-1,5-L-arabinan (at pH 7.0 and 50 degrees Celsius)2 Publications

pH dependencei

Optimum pH is 7.2 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius. It remains fully active after 30 minutes of preincubation at 50 degrees Celsius, however, after preincubation at 60 degrees Celsius, the residual activity is only 15%.2 Publications

Pathwayi: L-arabinan degradation

This protein is involved in the pathway L-arabinan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway L-arabinan degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei38Proton acceptor1 Publication1
Binding sitei38SubstrateBy similarity1
Binding sitei122Substrate; via amide nitrogenBy similarity1
Sitei171Important for catalytic activity1
Active sitei224Proton donor1 Publication1
Metal bindingi318CalciumSequence analysis1
Sitei318Important for substrate recognition1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU39330-MONOMER.
BRENDAi3.2.1.99. 658.
UniPathwayiUPA00667.

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular endo-alpha-(1->5)-L-arabinanase 2 (EC:3.2.1.99)
Short name:
ABN
Alternative name(s):
Endo-1,5-alpha-L-arabinanase
Gene namesi
Name:abn2
Synonyms:J3A, yxiA
Ordered Locus Names:BSU39330
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Double mutant abn2/abnA induce an almost complete loss of this activity.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi38D → A: Loss of arabinanase activity. 1 Publication1
Mutagenesisi171D → A: Loss of arabinanase activity. 1 Publication1
Mutagenesisi224E → A: Loss of arabinanase activity. 1 Publication1
Mutagenesisi318H → A: Drastic decrease in arabinanase activity. Does not unduly disrupt the calcium cluster. Mutation does not disrupt the calcium cluster, but it relaxes the geometry of the cluster, resulting in a more planar arrangement of the calcium ion with five of the water molecules. 1 Publication1
Mutagenesisi318H → Q: Loss of arabinanase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001220527 – 469Extracellular endo-alpha-(1->5)-L-arabinanase 2Add BLAST443

Proteomic databases

PaxDbiP42293.

Expressioni

Inductioni

Repressed by glucose, and induced by pectin and arabinan.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021221.

Structurei

Secondary structure

1469
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 44Combined sources5
Beta strandi47 – 51Combined sources5
Helixi53 – 55Combined sources3
Beta strandi57 – 65Combined sources9
Beta strandi67 – 70Combined sources4
Helixi83 – 86Combined sources4
Helixi88 – 94Combined sources7
Beta strandi103 – 106Combined sources4
Beta strandi112 – 119Combined sources8
Beta strandi121 – 123Combined sources3
Beta strandi126 – 135Combined sources10
Beta strandi141 – 149Combined sources9
Beta strandi152 – 154Combined sources3
Beta strandi158 – 160Combined sources3
Turni163 – 165Combined sources3
Beta strandi173 – 176Combined sources4
Beta strandi182 – 186Combined sources5
Beta strandi193 – 198Combined sources6
Turni200 – 202Combined sources3
Beta strandi203 – 205Combined sources3
Beta strandi213 – 216Combined sources4
Beta strandi222 – 231Combined sources10
Turni232 – 235Combined sources4
Beta strandi236 – 247Combined sources12
Beta strandi253 – 261Combined sources9
Helixi274 – 276Combined sources3
Helixi287 – 290Combined sources4
Beta strandi293 – 298Combined sources6
Beta strandi300 – 302Combined sources3
Beta strandi306 – 308Combined sources3
Beta strandi312 – 323Combined sources12
Turni325 – 327Combined sources3
Beta strandi330 – 337Combined sources8
Beta strandi346 – 354Combined sources9
Beta strandi360 – 362Combined sources3
Helixi377 – 380Combined sources4
Beta strandi382 – 388Combined sources7
Beta strandi401 – 405Combined sources5
Beta strandi409 – 415Combined sources7
Beta strandi417 – 422Combined sources6
Turni423 – 425Combined sources3
Beta strandi426 – 431Combined sources6
Beta strandi434 – 445Combined sources12
Turni446 – 449Combined sources4
Beta strandi450 – 458Combined sources9
Beta strandi464 – 469Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X8FX-ray1.90A/B1-469[»]
2X8SX-ray1.50A/B1-469[»]
2X8TX-ray1.79A/B1-469[»]
4COTX-ray1.90A1-469[»]
ProteinModelPortaliP42293.
SMRiP42293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni168 – 171Substrate bindingBy similarity4
Regioni188 – 190Substrate binding3
Regioni220 – 224Substrate binding5

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106Z5D. Bacteria.
COG3507. LUCA.
HOGENOMiHOG000292084.
InParanoidiP42293.
KOiK06113.
OMAiYYMYYNA.
PhylomeDBiP42293.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR032291. Abn2_C.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 3 hits.
PfamiPF16369. GH43_C. 1 hit.
PF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42293-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNRLFRVCF LAALIMAFTL PNSVYAQKPI FKEVSVHDPS IIETNGTFYV
60 70 80 90 100
FGSHLASAKS NDLMQWQQLT TSVSNDNPLI PNVYEELKET FEWAQSDTLW
110 120 130 140 150
AADVTQLADG KYYMYYNACR GDSPRSAMGV AVADNIEGPY KNKGIFLKSG
160 170 180 190 200
MEGTSSDGTP YDATKHPNVV DPHTFFDKDG KLWMVYGSYS GGIFILEMNP
210 220 230 240 250
KTGFPLPGQG YGKKLLGGNH SRIEGPYVLY NPDTQYYYLY LSYGGLDATG
260 270 280 290 300
GYNIRVARSK KPDGPYYDAE GNPMLDVRGK GGTFFDDRSI EPYGVKLMGS
310 320 330 340 350
YTFETENEKG TGYVSPGHNS AYYDEKTGRS YLIFHTRFPG RGEEHEVRVH
360 370 380 390 400
QLFMNKDGWP VAAPYRYAGE TLKEVKQKDI TGTYKLIQHG KDISADIKQT
410 420 430 440 450
INIQLNKNHT ISGEMTGTWR KTGKNTADIT LAGKKYNGVF LRQWDSVREK
460
NVMTFSVLNT SGEAVWGSK
Length:469
Mass (Da):52,607
Last modified:July 28, 2009 - v2
Checksum:i1AB8F3D8EF2B3E2E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti175F → S in BAA06646 (PubMed:7704263).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31856 Genomic DNA. Translation: BAA06646.1.
EU373814 Genomic DNA. Translation: ACB06752.1.
AL009126 Genomic DNA. Translation: CAB15969.2.
M20659 Genomic DNA. No translation available.
PIRiE70076.
RefSeqiNP_391812.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15969; CAB15969; BSU39330.
GeneIDi937533.
KEGGibsu:BSU39330.
PATRICi18979926. VBIBacSub10457_4125.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31856 Genomic DNA. Translation: BAA06646.1.
EU373814 Genomic DNA. Translation: ACB06752.1.
AL009126 Genomic DNA. Translation: CAB15969.2.
M20659 Genomic DNA. No translation available.
PIRiE70076.
RefSeqiNP_391812.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2X8FX-ray1.90A/B1-469[»]
2X8SX-ray1.50A/B1-469[»]
2X8TX-ray1.79A/B1-469[»]
4COTX-ray1.90A1-469[»]
ProteinModelPortaliP42293.
SMRiP42293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100021221.

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Proteomic databases

PaxDbiP42293.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15969; CAB15969; BSU39330.
GeneIDi937533.
KEGGibsu:BSU39330.
PATRICi18979926. VBIBacSub10457_4125.

Phylogenomic databases

eggNOGiENOG4106Z5D. Bacteria.
COG3507. LUCA.
HOGENOMiHOG000292084.
InParanoidiP42293.
KOiK06113.
OMAiYYMYYNA.
PhylomeDBiP42293.

Enzyme and pathway databases

UniPathwayiUPA00667.
BioCyciBSUB:BSU39330-MONOMER.
BRENDAi3.2.1.99. 658.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR032291. Abn2_C.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 3 hits.
PfamiPF16369. GH43_C. 1 hit.
PF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEABN2_BACSU
AccessioniPrimary (citable) accession number: P42293
Secondary accession number(s): B3FRL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 28, 2009
Last modified: November 2, 2016
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.