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Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Thermoanaerobacterium saccharolyticum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endo-acting enzyme that randomly cleaves the internal xylosidic linkages of the xylan backbone, yielding xylooligosaccharides of various lengths which are further hydrolyzed to xylose molecules by beta-xylosidase (EC 3.2.1.37). Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.

pH dependencei

Optimum pH is 5.5.

Temperature dependencei

Optimum temperature is 70 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei495 – 4951Proton donorBy similarity
Active sitei537 – 53711 Publication
Active sitei600 – 6001NucleophilePROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene namesi
Name:xynA
OrganismiThermoanaerobacterium saccharolyticum
Taxonomic identifieri28896 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi537 – 5371D → N: Loss of activity. 1 Publication
Mutagenesisi600 – 6001E → Q: Loss of activity. 1 Publication
Mutagenesisi602 – 6021D → N: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 PublicationAdd
BLAST
Chaini34 – 11571124Endo-1,4-beta-xylanase APRO_0000007980Add
BLAST

Expressioni

Inductioni

By xylan and xylose.

Structurei

3D structure databases

ProteinModelPortaliP36917.
SMRiP36917. Positions 859-1043.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 189152CBM-cenC 1Add
BLAST
Domaini195 – 343149CBM-cenC 2Add
BLAST
Domaini1051 – 111464SLH 1PROSITE-ProRule annotationAdd
BLAST
Domaini1115 – 115743SLH 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni413 – 649237CatalyticSequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 2 SLH (S-layer homology) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. S-layer_homology_dom.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 2 hits.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P36917-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKNNVDRIV SIVTALIMIF GASLFSPPIR VFADDTNINL VSNGDFESGT
60 70 80 90 100
IDGWIKQGNP TLAVTTEQAI GQYSMKVTGR TQTYEGPAYS FLGKMQKGES
110 120 130 140 150
YSVSLKVRLV SGQNSSNPLI TVTMFREDDN GKHYDTIVWQ KQVSEDSWTT
160 170 180 190 200
VSGTYTLDYI GTLKTLYMYV ESPDPTLEYY IDDVVVTTQN PIQVGNVIAN
210 220 230 240 250
ETFENGNTSG WIGTGSSVVK AVYGVAHSGD YSLLTTGRTA NWNGPSYDLT
260 270 280 290 300
GKIVPGQQYN VDFWVKFVNG NDTEQIKATV KATSDKDNYI QVNDFANVNK
310 320 330 340 350
GEWTEIKGSF TLPVADYSGI SIYVESQNPT LEFYIDDFSV IGEISNNQIT
360 370 380 390 400
IQNDIPDLYS VFKDYFPIGV AVDPSRLNDA DPHAQLTAKH FNMLVAENAM
410 420 430 440 450
KPESLQPTEG NFTFDNADKI VDYAIAHNMK MRGHTLLWHN QVPDWFFQDP
460 470 480 490 500
SDPSKSASRD LLLQRLKTHI TTVLDHFKTK YGSQNPIIGW DVVNEVLDDN
510 520 530 540 550
GNLRNSKWLQ IIGPDYIEKA FEYAHEADPS MKLFINDYNI ENNGVKTQAM
560 570 580 590 600
YDLVKKLKSE GVPIDGIGMQ MHININSNID NIKASIEKLA SLGVEIQVTE
610 620 630 640 650
LDMNMNGNIS NEALLKQARL YKQLFDLFKA EKQYITAVVF WGVSDDVTWL
660 670 680 690 700
SKPNAPLLFD SKLQAKPAFW AVVDPSKAIP DIQSAKALEG SPTIGANVDS
710 720 730 740 750
SWKLVKPLYV NTYVEGTVGA TATVKSMWDT KNLYLLVQVS DNTPSNNDGI
760 770 780 790 800
EIFVDKNDDK STSYETDDER YTIKRDGTGS SDITKYVTSN ADGYVAQLAI
810 820 830 840 850
PIEDISPAVN DKIGFDIRIN DDKGNGKIDA ITVWNDYTNS QNTNTSYFGD
860 870 880 890 900
IVLSKSAQIA TAIYGTPVID GKVDDIWNNV EPISTNTWIL GSNGATATQK
910 920 930 940 950
MMWDDKYLYV LADVTDSNLN KSSINPYEQD SVEVFVDQNN DKTTYYENDD
960 970 980 990 1000
GQYRVNYDNE QSFGGSTNSN GFKSATSLTQ SGYIVEEAIP WTSITPSNGT
1010 1020 1030 1040 1050
IIGFDLQVNN ADENGKRTGI VTWCDPSGNS WQDTSGFGNL LLTGKPSGAL
1060 1070 1080 1090 1100
KKGVTFDDIK NSWAKDAIEV LASRHIVEGM TDTQYEPNKT VTRAEFTAMI
1110 1120 1130 1140 1150
LRLLNIKEEQ YSGEFSDVNS GDWYANAIEA AYKAGIIEGD GKNARPNDSI

TREEMTQ
Length:1,157
Mass (Da):128,380
Last modified:June 1, 1994 - v1
Checksum:i51FA6004497EC58B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97882 Genomic DNA. Translation: AAA21812.1. Sequence problems.
PIRiA48490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97882 Genomic DNA. Translation: AAA21812.1. Sequence problems.
PIRiA48490.

3D structure databases

ProteinModelPortaliP36917.
SMRiP36917. Positions 859-1043.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. S-layer_homology_dom.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 2 hits.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Gene cloning, sequencing, and biochemical characterization of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI."
    Lee Y.-E., Lowe S.E., Zeikus J.G.
    Appl. Environ. Microbiol. 59:3134-3137(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-41.
    Strain: ATCC 49915 / DSM 7060 / B6A-RI.
  2. "Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI."
    Lee Y.-E., Lowe S.E., Henrissat B., Zeikus J.G.
    J. Bacteriol. 175:5890-5898(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, MUTAGENESIS.

Entry informationi

Entry nameiXYNA_THESA
AccessioniPrimary (citable) accession number: P36917
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 1, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.