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Protein

Putative endo-1,4-beta-xylanase

Gene
N/A
Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Could be a xylanase.By similarity

Catalytic activityi

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

Pathway:ixylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041Proton donorBy similarity
Active sitei216 – 2161NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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

CAZyiGH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
ORF4
OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifieri44001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 312312Putative endo-1,4-beta-xylanasePRO_0000184068Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi351627.Csac_2405.

Structurei

3D structure databases

ProteinModelPortaliP23557.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 301301GH10PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR031158. Glyco_hydro_10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23557-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQQYLLDYE ATKASKNGMP VCKFDSCIPA LQFCKENGIK MRGHVLVWHN
60 70 80 90 100
QTPEWFFHKD YDVSKPLVDA ATMERRLESY IKQVIEFCQK NYPGVVYCWD
110 120 130 140 150
VVNEAILDDG SWREINNNWY TIMKEKYVEK AFYYARKYAK KDVALFYNDY
160 170 180 190 200
NVFLPAKREA IYNLAQKLKE KGLIDGLGLQ PTVGLNYPEL DSDDIDSFKT
210 220 230 240 250
TLETFAKLGL QIHITELNFE IKGDESNRTP ENLKKQADRY YEMMKLLLKE
260 270 280 290 300
DTDNGGPCNI TCVTVFGICD DYPLYKNFKQ CMYLWDKNCN PKPCFYSFLQ
310
AGLDWKASLL SK
Length:312
Mass (Da):36,494
Last modified:November 1, 1991 - v1
Checksum:i6C2A049212F9CB6E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34459 Genomic DNA. Translation: AAA23062.1.
PIRiD37202.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34459 Genomic DNA. Translation: AAA23062.1.
PIRiD37202.

3D structure databases

ProteinModelPortaliP23557.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351627.Csac_2405.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR031158. Glyco_hydro_10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. 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'."
    Luethi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D.J., Bergquist P.L.
    Appl. Environ. Microbiol. 56:1017-1024(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiXYN4_CALSA
AccessioniPrimary (citable) accession number: P23557
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: July 22, 2015
This is version 71 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. 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.