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Information on EC 3.2.1.8 - endo-1,4-beta-xylanase and Organism(s) Bacillus sp. 41M-1 and UniProt Accession Q9RC94

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Bacillus sp. 41M-1
UNIPROT: Q9RC94 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus sp. 41M-1
The enzyme appears in selected viruses and cellular organisms
Synonyms
endoxylanase, xylanase a, endo-xylanase, xyn11a, xyn10a, beta-xylanase, endo-1,4-beta-xylanase, gh11 xylanase, xylanase b, xynii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(1--> 4)-beta-xylan 4-xylanohydrolase
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1,4-beta-D-xylan xylanohydrolase
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1,4-beta-D-xylan xylanohydrolase 22
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1,4-beta-xylan xylanohydrolase
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34 kDa xylanase
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beta-1,4-D-xylanase
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beta-1,4-xylan xylanohydrolase
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beta-1,4-xylanase
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beta-D-xylanase
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beta-xylanase
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endo-(1--> 4)-beta-xylanase
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endo-1,4-beta-D-xylanase
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endo-1,4-beta-xylanase
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endo-1,4-xylanase
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endo-beta-1,4-xylanase
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endoxylanase
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FIA-xylanase
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ORF4
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TAXI
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X34
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XYLA
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xylanase
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Xylanase 22
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xylanase J
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xylanase, endo-1,4-
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XYLD
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XYLY
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-xylan xylanohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-57-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
birchwood xylan + H2O
?
show the reaction diagram
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
wild-type DELTAXBD
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
wild-type DELTAXBD
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9RC94_9BACI
354
0
39000
TrEMBL
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
DELTAXBD, consists of the catalytic domain only and corresponds to ALa1-Pro222 of XynJ. Mutants DELTAXBDR5 and DELTAXBDK51R/R5 show about 50% activity of that of DELTAXBD and have optima of pH 9.0 and 9.5, respectively. Reinforcing the characteristic salt bridge in the catalytic cleft and introducing excess Arg residues on the protein surface shift the optimum pH of the wild-type enzyme from 8.5 to 9.5. Mutant DELTAXBDK51R exhibit almost the same temperature profile and temperature optimum as DELTAXBD. The temperature optima of mutants DELTAXBDR5 and DELTAXBDK51R/R5 are both 60°C. Mutants show lower specific activity than DELTAXBD at 37-60°C, but they show apparently higher activity at 65°C. Introduction of excess Arg residues on the protein surface increase the thermostability of DELTAXBD
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
plasmids pET-DELTAXBD, pET-DELTAXBDR5 and pET-DELTAXBDK51R/R5 expressed in Escherichia coli BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Umemoto, H.; Ihsanawati, H.; Inami, M.; Yatsunami, R.; Fukui, T.; Kumasaka, T.; Tanaka, N.; Nakamura, S.
Improvement of alkaliphily of Bacillus alkaline xylanase by introducing amino acid substitutions both on catalytic cleft and protein surface
Biosci. Biotechnol. Biochem.
73
965-967
2009
Bacillus sp. 41M-1 (Q9RC94)
Manually annotated by BRENDA team