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P38535

- XYNX_CLOTM

UniProt

P38535 - XYNX_CLOTM

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Protein

Exoglucanase XynX

Gene

xynX

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei347 – 3471Proton donorBy similarity
Active sitei389 – 3891By similarity
Active sitei452 – 4521NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

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:
Exoglucanase XynX (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase
Gene namesi
Name:xynX
OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 10871057Exoglucanase XynXPRO_0000007982Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP38535.
SMRiP38535. Positions 711-895.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 188152CBM-cenCAdd
BLAST
Domaini903 – 96664SLH 1PROSITE-ProRule annotationAdd
BLAST
Domaini967 – 102559SLH 2PROSITE-ProRule annotationAdd
BLAST
Domaini1028 – 108760SLH 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 SLH (S-layer homology) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
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. 1 hit.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P38535-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKNNLSKFVS IFTAFIMIFG TSLFFPHVSA FADDNNANLV SNGDFESGTI
60 70 80 90 100
DGWIKQGNPT LAATTEEAIG QYSMKVAGRT QTYEGPAYSF LGKMQKGQSY
110 120 130 140 150
NVSLKVRLVS GQNSSNPLIT VTMFREDDNG KHYDTIVWQK QVSEDSWTTV
160 170 180 190 200
NGTYTLDYTG TLKTLYMYVE SPDPTLEYYI DDVVVTPQNP IQVGEISNNQ
210 220 230 240 250
ITIQNDIPDL SSVFKDYFPI GVAVDPSRLN DTDPHAQLTA KHFNMLVAEN
260 270 280 290 300
AMKPESLQPT EGNFTFDNAD RIVDYAIAHN MKMRGHTLLW HNQVPDWFFQ
310 320 330 340 350
DPSDPTKPAS RDLLLQRLKT HITTVLDHFK TKYGAQNPII GWDVVNEVLD
360 370 380 390 400
DNGSLRNSKW LQIIGPDYIE KAFEYAHEAD PSMKLFINDY NIENNGVKTQ
410 420 430 440 450
AMYDLVKKLK SEGVPISGIG MQMHININSN IDNIKASIEK LASLGVEIQV
460 470 480 490 500
TELDMNMNGN VSNEALLKQA RLYKQLFDLF KAEKQYITAV VFWGVSDDVT
510 520 530 540 550
WLSKPNAPLL FDSKLQAKPA YWAIADPSKA IPDIQSAKAL EGSPTIGANV
560 570 580 590 600
DSSWKLVKPL YANTYVEGTV GATATVKSMW DTKNLYLLVQ VSDNTPSSND
610 620 630 640 650
GIEIFVDKND NKSTSYETDD EHYTIKSDGT GSSDITKYVT SNADGYIVQL
660 670 680 690 700
AIPIEDISPT LNDKIGLDVR LNDDKGSGSI DTVTVWNDYT NSQDTNTSYF
710 720 730 740 750
GDIVLSKPAQ VATAIYGTPV IDGKIDDIWN KVDAITTNTW VLGSDGATAT
760 770 780 790 800
AKMMWDDKYL YVLADVTDSN LNKSSVNPYE QDSVEVFVDQ NNDKTSYYES
810 820 830 840 850
DDGQYRVNYD NEQSFGGSTN SNGFKSATSL TQSGYIVEEA IPWTSITLLN
860 870 880 890 900
GTIIGFDLQV NDADENGKRT GIVTWCDPSG NSWQDTSGFG NLLLTGKPSG
910 920 930 940 950
VLKKSVTFND IKDNWAKDVI EVLASRHIVE GMTDTQYEPS KTVTRAEFTA
960 970 980 990 1000
MILKLLNIKE EAYNGEFSDV KNGDWYANAI EAAYKAGIIE GDGKNMRPND
1010 1020 1030 1040 1050
SITREEMTSI AMRAYEMLTS YKEENIGATS FNDDKSISDW AKNVVANAAK
1060 1070 1080
LGIINGEPSN VFAPKGIATR AEAAAIIYGL LEKSNNL
Length:1,087
Mass (Da):120,358
Last modified:October 1, 1994 - v1
Checksum:i88077FC27AC83F51
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M67438 Genomic DNA. Translation: AAA23227.1.
PIRiS41797.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M67438 Genomic DNA. Translation: AAA23227.1 .
PIRi S41797.

3D structure databases

ProteinModelPortali P38535.
SMRi P38535. Positions 711-895.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProi IPR010502. 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 ]
Pfami PF02018. CBM_4_9. 1 hit.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Pack M.Y., Jung K.H.
    Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiXYNX_CLOTM
AccessioniPrimary (citable) accession number: P38535
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 1, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3