microglycodb_gene_00058
Gene Number | BLLJ_0211 |
---|---|
UniProt ID | E8MGH8 |
NCBI Protein ID | BAK79118.1 |
Protein Name | |
Enzyme Name | β-L-arabinofuranosidase |
CAZy Family | GH127 |
Reviewed | true |
Organism | Bifidobacterium longum |
sequence
functions
publications
reaction
Data not found
Beta-L-arabinofuranosidase that removes the beta-L-arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue.
kcat is 2.0 sec(-1) with beta-Ara2. kcat is 0.013 sec(-1) with Ara-Hyp. kcat is 6.3 sec(-1) with Ara(2)-Hyp.
Data not found
Data not found
10 20 30 40 50
MNVTITSPFW KRRRDQIVES VIPYQWGVMN DEIDTTVPDD PAGNQLADSK
60 70 80 90 100
SHAVANLKVA AGELDDEFHG MVFQDSDVYK WLEEAAYALA YHPDPELKAL
110 120 130 140 150
CDRTVDLIAR AQQSDGYLDT PYQIKSGVWA DRPRFSLIQQ SHEMYVMGHY
160 170 180 190 200
IEAAVAYHQV TGNEQALEVA KKMADCLDAN FGPEEGKIHG ADGHPEIELA
210 220 230 240 250
LAKLYEETGE KRYLTLSQYL IDVRGQDPQF YAKQLKAMNG DNIFHDLGFY
260 270 280 290 300
KPTYFQAAEP VRDQQTADGH AVRVGYLCTG VAHVGRLLGD QGLIDTAKRF
310 320 330 340 350
WKNIVTRRMY VTGAIGSTHV GESFTYDYDL PNDTMYGETC ASVAMSMFAQ
360 370 380 390 400
QMLDLEPKGE YADVLEKELF NGSIAGISLD GKQYYYVNAL ETTPDGLDNP
410 420 430 440 450
DRHHVLSHRV DWFGCACCPA NIARLIASVD RYIYTERDGG KTVLSHQFIA
460 470 480 490 500
NTAEFASGLT VEQRSNFPWD GHVEYTVSLP ASATDSSVRF GLRIPGWSRG
510 520 530 540 550
SYTLTVNGKP AVGSLEDGFV YLVVNAGDTL EIALELDMSV KFVRANSRVR
560 570 580 590 600
SDAGQVAVMR GPLVYCAEQV DNPGDLWNYR LADGVTGADA AVAFQADLLG
610 620 630 640 650
GVDTVDLPAV REHADEDDAP LYVDADEPRA GEPATLRLVP YYSWANREIG
660
EMRVFQRR
1. Bifidobacteria can protect from enteropathogenic infection through production of acetate.
PubMed: 21270894
doi:10.1038/nature09646
2. Characterization of a novel beta-L-Arabinofuranosidase in Bifidobacterium longum: functional elucidation of A DUF1680 family member.
PubMed: 21914802
doi:10.1074/jbc.m111.248690
3. Characterization of a novel beta-L-arabinofuranosidase in Bifidobacterium longum: functional elucidation of a DUF1680 protein family member.
PubMed: 24385433
doi:10.1074/jbc.m113.528711
4. Crystal structure of glycoside hydrolase family 127 beta-l-arabinofuranosidase from Bifidobacterium longum.
PubMed: 24680821
doi:10.1016/j.bbrc.2014.03.096
5. Crystallization and preliminary X-ray diffraction analysis of a novel beta-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum.
PubMed: 24817727
doi:10.1107/s2053230x14001812
6. Structure and catalytic mechanism of a glycoside hydrolase family-127 beta-L-arabinofuranosidase (HypBA1).
doi:10.4172/2155-9821.1000171