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Protein

Endo-1,4-beta-xylanase

Gene

xynU

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei122NucleophilePROSITE-ProRule annotation1
Active sitei212Proton donorPROSITE-ProRule annotation1
Metal bindingi255CalciumCombined sources1
Metal bindingi257CalciumCombined sources1
Metal bindingi277Calcium; via carbonyl oxygenCombined sources1
Metal bindingi369CalciumCombined sources1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidasePROSITE-ProRule annotationImported, Hydrolase
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradationPROSITE-ProRule annotationImported
LigandCalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BRENDAi3.2.1.8. 1530.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM6. Carbohydrate-Binding Module Family 6.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11U_CLOTH.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanasePROSITE-ProRule annotation (EC:3.2.1.8PROSITE-ProRule annotation)
Gene namesi
Name:xynUImported
OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)Imported
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_500415890229 – 683Endo-1,4-beta-xylanaseSequence analysisAdd BLAST655

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GMMX-ray2.00A248-380[»]
1UXXX-ray1.60X248-380[»]
ProteinModelPortaliO52780.
SMRiO52780.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO52780.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 225GH11InterPro annotationAdd BLAST195
Domaini252 – 374CBM6InterPro annotationAdd BLAST123
Domaini388 – 456DockerinInterPro annotationAdd BLAST69
Domaini480 – 658NodB homologyInterPro annotationAdd BLAST179

Sequence similaritiesi

Belongs to the glycosyl hydrolase 11 (cellulase G) family.PROSITE-ProRule annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG4107T94. Bacteria.
COG0726. LUCA.
COG5498. LUCA.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 1 hit.
InterProiView protein in InterPro
IPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR036439. Dockerin_dom_sf.
IPR018247. EF_Hand_1_Ca_BS.
IPR008979. Galactose-bd-like.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR002509. NODB_dom.
PfamiView protein in Pfam
PF03422. CBM_6. 1 hit.
PF00404. Dockerin_1. 2 hits.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
PRINTSiPR00911. GLHYDRLASE11.
SMARTiView protein in SMART
SM00606. CBD_IV. 1 hit.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 1 hit.
SSF63446. SSF63446. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEiView protein in PROSITE
PS51175. CBM6. 1 hit.
PS00448. CLOS_CELLULOSOME_RPT. 1 hit.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
PS51677. NODB. 1 hit.

Sequencei

Sequence statusi: Complete.

O52780-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQKLLVTFL ILITFTVSLT LFPVNVRADV VITSNQTGTH GGYNFEYWKD
60 70 80 90 100
TGNGTMVLKD GGAFSCEWSN INNILFRKGF KYDETKRHDQ LGYITVTYSC
110 120 130 140 150
NYQPNGNSYL GVYGWTSNPL VEYYIIESWG TWRPPGATPK GTITVDGGTY
160 170 180 190 200
EIYETTRVNQ PSIKGTATFQ QYWSVRTSKR TSGTISVTEH FKAWERLGMK
210 220 230 240 250
MGKMYEVALV VEGYQSSGKA DVTSMTITVG NAPSTSSPPG PTPEPTPRSA
260 270 280 290 300
FSKIESEEYN SLKSSTIQTI GTSDGGSGIG YIESGDYLVF NKINFGNGAN
310 320 330 340 350
SFKARVASGA DTPTNIQLRL GSPTGTLIGT LTVASTGGWN NYEEKSCSIT
360 370 380 390 400
NTTGQHDLYL VFSGPVNIDY FIFDSNGVNP TPTSQPQQGQ VLGDLNGDKQ
410 420 430 440 450
VNSTDYTALK RHLLNITRLS GTALANADLN GDGKVDSTDL MILHRYLLGI
460 470 480 490 500
ISSFPRSNPQ PSSNPQPSSN PQPTINPNAK LVALTFDDGP DNVLTARVLD
510 520 530 540 550
KLDKYNVKAT FMVVGQRVND STAAIIRRMV NSGHEIGNHS WSYSGMANMS
560 570 580 590 600
PDQIRKSIAD TNAVIQKYAG TTPKFFRAPN LETSPTLFNN VDLVFVGGLT
610 620 630 640 650
ANDWIPSTTA EQRAGAVING VRDGTIILLH DVQPEPHPTP EALDIIIPTL
660 670 680
KSRGYEFVTL TELFTLKGVP IDPSVKRMYN SVP
Length:683
Mass (Da):74,530
Last modified:June 1, 1998 - v1
Checksum:i714BB16E0C9820A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047761 Genomic DNA. Translation: AAC04579.1.

Similar proteinsi

Entry informationi

Entry nameiO52780_CLOTM
AccessioniPrimary (citable) accession number: O52780
Entry historyiIntegrated into UniProtKB/TrEMBL: June 1, 1998
Last sequence update: June 1, 1998
Last modified: October 25, 2017
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources