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Protein

Beta-xylanase

Gene

XynE

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationImported

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
Gene namesi
Name:XynEImported
OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)Imported
Taxonomic identifieri44001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3636Sequence analysisAdd
BLAST
Chaini37 – 700664Beta-xylanaseSequence analysisPRO_5004158101Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi351627.Csac_2410.

Structurei

3D structure databases

ProteinModelPortaliO30427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini349 – 678330GH10 (glycosyl hydrolase family 10)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 10 (cellulase F) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG4105D9F. Bacteria.
COG3693. LUCA.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O30427-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRTFKSVT LLAVAIVFLV SGVFLKAFPV MQNAKAQSSS VTVINFEGKD
60 70 80 90 100
TLTFFAYGNA KIATDQSSAI EGKKSIKVTN RKSIWDSLAI DVKDVLKRGK
110 120 130 140 150
TWVISSYIKH VGKKPIAFSI TALYDDGKGL KYVQLGEKIV MPSKWEKIAV
160 170 180 190 200
KWKPTLKNPS NLIIAIHPTV DKTTAYNVDS IQVMTEETYL SQAIIYKDTF
210 220 230 240 250
ENNTTNWRPR GEGVKIKLDN SKFHEGNESL YVSGRTAFWH GAKIPIIKYV
260 270 280 290 300
VPGKRYKFSI WVYHTSMDLK RFSILVQRKM ADEAQYRYDW ITSKEVAGDG
310 320 330 340 350
WEEISGSYVV PDNGKIEELE FYIESPDPTL SFWVDDFTIS DTMKLQQPNY
360 370 380 390 400
SLPSLKEKYK NDFKVGVAIG YGELINSIDK QFIKKHFNSI TPGNEMKPES
410 420 430 440 450
LLRGPDKYDF TIADAFVEFA TKNNISIRGH TLVWHNQTPD WFFKDSNGNF
460 470 480 490 500
LKKDELLKRL KKHIYTVVGR YKGKIYAWDV VNEAIDETQP DGYRRSNWYK
510 520 530 540 550
ICGPEYIEKA FIWAHEADPQ AKLFYNDYNT EVPQKRMFIY NMIKNMKSKG
560 570 580 590 600
IPIHGVGLQC HINVDSPSVE EIEETIKLFS TIPGLEIQIT ELDMSFYQWG
610 620 630 640 650
SSVYYVEPSR EMLLRQAKKY YELFNLFRKY KKIIKSVTFW GLKDDYSWLR
660 670 680 690 700
GVFNKPDFPL LFDEYYDGKP AFWALIDYSV IPQNINLPAP PAIPKLNTKK
Length:700
Mass (Da):80,853
Last modified:January 1, 1998 - v1
Checksum:i407562F85B2B5699
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005383 Genomic DNA. Translation: AAB87372.1.
PIRiT30910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005383 Genomic DNA. Translation: AAB87372.1.
PIRiT30910.

3D structure databases

ProteinModelPortaliO30427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351627.Csac_2410.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105D9F. Bacteria.
COG3693. LUCA.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile 'Caldocellum saccharolyticum'."
    Luthi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D., Bergquist P.L.
    Appl. Environ. Microbiol. 56:1017-1024(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "A cluster of genes involved in xylan degradation cloned from the extreme thermophile Caldicellulosiruptor saccharolyticus."
    Te'o V.S.Jr., Gibbs M.D., Saul D.J., Bergquist P.L.
    Appl. Environ. Microbiol. 0:0-0(1997)
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiO30427_CALSA
AccessioniPrimary (citable) accession number: O30427
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: April 13, 2016
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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 one 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.