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Protein
Submitted name:

Endoglucanase cel5A

Gene

cel5A

Organism
Eubacterium cellulosolvens
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Enzyme and pathway databases

BRENDAi3.2.1.4. 8385.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Submitted name:
Endoglucanase cel5AImported
Gene namesi
Name:cel5AImported
OrganismiEubacterium cellulosolvensImported
Taxonomic identifieri29322 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YPJX-ray2.35A581-713[»]
4AEKX-ray1.75A37-170[»]
4AEMX-ray2.10A37-170[»]
4AFDX-ray1.34A40-170[»]
4AFMX-ray1.25A37-170[»]
4BA6X-ray1.42A581-713[»]
5AFEX-ray2.60A581-713[»]
ProteinModelPortaliQ3LHN3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 5 family.UniRule annotation

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.

Sequencei

Sequence statusi: Complete.

Q3LHN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGNWLKDVL RRFAVIAMML VMVFTLLPAT AQGTEAASGD IVLFSGSKHV
60 70 80 90 100
EFTDWGGTDW PSAYELQPPY QTMPFDLNKN FEIKVDYSGA DIVLIFARWE
110 120 130 140 150
HGSKPQIWAQ ISPYYVVDGT AVFTKEQIAK AYGSDDFSDL DYIGVKPLPS
160 170 180 190 200
ADGMTVTKIV ASYTSGSSDD VDINLKGIAG EWANGVNIGW NLGNTLDAYD
210 220 230 240 250
TNRFKSSKGH NNPADIETCW GNPVTTKAMI DDIKAQGFNA VRVPVTWDFE
260 270 280 290 300
IDDNDGYKVN EAWMARVKEV VDYVMDNDLY CILNVHHDTG EQGWLKASTA
310 320 330 340 350
NYNKNVKKFK ALWKQIAAEF KNYDNKLAFE GFNEMLDEKN SWNYPGTDAG
360 370 380 390 400
DAINLYNQAF VDVVRASGGK NGKRPLICNT YAGCTEAGAL NSFKIPNDTV
410 420 430 440 450
DNAIIAQVHF YQPTGYCFDM NPNQGQNMDV DYKTCGGESA ADTLAMMLYK
460 470 480 490 500
RFTEKGIPCI VGEFAASHKK NDDNRAEWVD YVVRKTGTYG VKCFWWDNGG
510 520 530 540 550
TFTPNYSTGL DYYNSMGIYN RNTMQFEYPK VADALVNAAN GGAKPTTAPT
560 570 580 590 600
KKPTSTPKPT ATLKPTTKPT TKPTTKPNPT SGADSGEIIL FSGSNHADFK
610 620 630 640 650
AWGGDDWPSA FEISPKYEPM KLDLNKNFEI KVDYNGADIV LIFARWDKDI
660 670 680 690 700
WAQISPYYVV DGTAVFTKEQ IAKAYGSDDF SGLDYIAVKP LPSEEGVTVT
710 720 730 740 750
KVSGIYTNGG SEDVDINLKG IAGEWANGVN IGWNLGNTLD AYDTNRFTRT
760 770 780 790 800
KGHNNPADIE TCWGNPVTTK AMIDDIKAQG FNAVRVPVTW DYEIDDNDGY
810 820 830 840 850
KVNEAWMARV KEVVDYVMDN DMYCIVNVHH DTGEQGWLKA STANYAKNEK
860 870 880 890 900
KFKALWKQIA AEFKNYDHKL AFEGFNEMLD EKNSWNYPGA DAGEAINLYN
910 920 930 940 950
QAFVDVVRAS GGKNSDRPLI CNTYAGCTEA GALNSFEIPN DTVENAIIAQ
960 970 980 990 1000
VHFYQPTGYC FDMNPNQGQN MDVDYKTCGG ESAADTLAMM LYKRFTEKGI
1010 1020 1030 1040 1050
PCIVGEFAAS HKQNDDNRAA WVDYVVSKTG KYGVKCFWWD NGGTFTPNYS
1060 1070 1080 1090 1100
TGLDYYNSMG IYNRNTMKFE YPKVADALVK AANGGTMPTV APTKKPTATP
1110 1120 1130 1140
TPTKKPTSTP KPTVKPTQTP KPTRKPGKRV KYSALDLDGN VSSGNLIP
Length:1,148
Mass (Da):127,127
Last modified:November 8, 2005 - v1
Checksum:i0DBCB73BDB1BB578
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB179780 Genomic DNA. Translation: BAE46390.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB179780 Genomic DNA. Translation: BAE46390.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YPJX-ray2.35A581-713[»]
4AEKX-ray1.75A37-170[»]
4AEMX-ray2.10A37-170[»]
4AFDX-ray1.34A40-170[»]
4AFMX-ray1.25A37-170[»]
4BA6X-ray1.42A581-713[»]
5AFEX-ray2.60A581-713[»]
ProteinModelPortaliQ3LHN3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.4. 8385.

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 2 hits.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing, and expression of a Eubacterium cellulosolvens 5 gene encoding an endoglucanase (Cel5A) with novel carbohydrate-binding modules, and properties of Cel5A."
    Yoda K., Toyoda A., Mukoyama Y., Nakamura Y., Minato H.
    Appl. Environ. Microbiol. 71:5787-5793(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Understanding how noncatalytic carbohydrate binding modules can display specificity for xyloglucan."
    Luis A.S., Venditto I., Temple M.J., Rogowski A., Basle A., Xue J., Knox J.P., Prates J.A., Ferreira L.M., Fontes C.M., Najmudin S., Gilbert H.J.
    J. Biol. Chem. 288:4799-4809(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 37-170.
  3. "Understanding How Noncatalytic Carbohydrate Binding Modules Can Display Specificity for Xyloglucan."
    Luis A.S., Venditto I., Basle A., Prates J.A.M., Ferreira L.M.A., Temple M., Rogowski A., Xue J., Knox J.P., Fontes C.M.G.A., Gilbert H.J., Najmudin S.
    Submitted (DEC-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 581-713.

Entry informationi

Entry nameiQ3LHN3_EUBCE
AccessioniPrimary (citable) accession number: Q3LHN3
Entry historyi
Integrated into UniProtKB/TrEMBL: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 1, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.