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P10476

- GUNA_CELJU

UniProt

P10476 - GUNA_CELJU

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Protein

Endoglucanase A

Gene

celA

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei523 – 5231By similarity
Active sitei573 – 5731By similarity
Active sitei582 – 5821By similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

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

Enzyme and pathway databases

BioCyciCJAP498211:GHIT-2463-MONOMER.

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Short name:
EGA
Alternative name(s):
Cellulase
Endo-1,4-beta-glucanase
Gene namesi
Name:celA
Synonyms:cel9A
Ordered Locus Names:CJA_2472
OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri498211 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
ProteomesiUP000001036: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 962930Endoglucanase APRO_0000007957Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi671 ↔ 702By similarity
Disulfide bondi681 ↔ 696By similarity
Disulfide bondi866 ↔ 961By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_2472.

Structurei

3D structure databases

ProteinModelPortaliP10476.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini671 – 69727CBM10Add
BLAST
Domaini859 – 962104CBM2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi608 – 66457Ser-richAdd
BLAST
Compositional biasi823 – 85937Ser-rich (linker)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000245359.
OrthoDBiEOG6QRW4D.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.30.32.30. 1 hit.
2.60.40.10. 1 hit.
2.60.40.290. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR004197. Glyco_hydro_9_Ig-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF02927. CelD_N. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
PF00801. PKD. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
SM01064. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49299. SSF49299. 1 hit.
SSF49384. SSF49384. 1 hit.
SSF57615. SSF57615. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P10476-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MINRSVLKIP ALVKPLVQAL VLVGCTLGVA QAEVGNPRVN QLGYIPNGDR
60 70 80 90 100
IAVYKASNNS AQTWQLTHNG SLIASGQTIP KGSDASSGDN IHHIDLSSVT
110 120 130 140 150
ATGSGFTLTV GGDSSYPFSI SSTTFNAAFY DALKYFYHNR SGIAIETPYT
160 170 180 190 200
GGGRGSYASH SRWSRPAGHL NQGANKGDMN VPCWSGTCNY SLNVTKGWYD
210 220 230 240 250
AGDHGKYVVN GGISVWTLLN LYERAQHITG NLAAVADGSM NIPESGNGVA
260 270 280 290 300
DILDEARWQM EFMLAMQVPQ GQAKAGMAHH KIHDVGWTGL PLAPHEDPQQ
310 320 330 340 350
RALVPPSTAA TLNLAATAAQ AARIWKDIDA GFAALCLTAA ERAWNAAQAN
360 370 380 390 400
PNDIYSGNYD NGGGGYGDRF VADEFYWAAA ELYITTGDSR YLPTINNYTL
410 420 430 440 450
ERTDFGWPDT ELLGVMSLAV VPATHTNSLR IAARNHIQTI ASTHLTTQSA
460 470 480 490 500
SGYPAPLSSL EYYWGSNSVI ANKLVLMGLA YDFSGNQNFA LGVSKGINYL
510 520 530 540 550
FGSNVLSTSF ITGLGTNTVA QPHHRFWAGA LNSNYPWAPP GALSGGPNAG
560 570 580 590 600
LEDSLSASRL SGCTSRPATC WLDSIDAWST NEITINWNAP LAWVLGFYND
610 620 630 640 650
FAATQGGSSS SSSSSSSSVP VSSSSSSSII PSSSSSSIQP SSSSSSMPSS
660 670 680 690 700
SSSSSSVVAS SSSSVSGGLR CNWYGTLYPL CVTTQSGWGW ENSQSCISAS
710 720 730 740 750
TCSAQPAPYG IVGAASSSSQ AANRSPTLQL SANATGFEGG SMVCCTLHIN
760 770 780 790 800
GAASDPDGDN LTYSWQVISG NTVVASGSSS SASIHVSNQR GYEVSMTVSD
810 820 830 840 850
GRGGVATETT FVSVYFSDYF PGSSSSASNI NSSSSSSSSS SSSAIVSSSS
860 870 880 890 900
SVVSSSSSSA ASGGNCQYVV TNQWNNGFTA VIRVRNNGSS AINGWSVNWS
910 920 930 940 950
YSDGSRITNS WNANVTGNNP YAASALGWNA NIQPGQTAEF GFQGTKGAGS
960
AQVPAVTGSV CQ
Length:962
Mass (Da):100,109
Last modified:April 20, 2010 - v2
Checksum:i95212655950CB52A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141K → T in CAA31082. (PubMed:2851699)Curated
Sequence conflicti25 – 251C → G in CAA31082. (PubMed:2851699)Curated
Sequence conflicti503 – 5031S → I in CAA31082. (PubMed:2851699)Curated
Sequence conflicti507 – 5071S → P in CAA31082. (PubMed:2851699)Curated
Sequence conflicti555 – 5551L → F in CAA31082. (PubMed:2851699)Curated
Sequence conflicti894 – 8941G → R in CAA31082. (PubMed:2851699)Curated
Sequence conflicti951 – 9511A → R in CAA31082. (PubMed:2851699)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12570 Genomic DNA. Translation: CAA31082.1.
CP000934 Genomic DNA. Translation: ACE85757.1.
RefSeqiYP_001982933.1. NC_010995.1.

Genome annotation databases

EnsemblBacteriaiACE85757; ACE85757; CJA_2472.
GeneIDi6416717.
KEGGicja:CJA_2472.
PATRICi21328310. VBICelJap122165_2424.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12570 Genomic DNA. Translation: CAA31082.1 .
CP000934 Genomic DNA. Translation: ACE85757.1 .
RefSeqi YP_001982933.1. NC_010995.1.

3D structure databases

ProteinModelPortali P10476.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 498211.CJA_2472.

Protein family/group databases

CAZyi CBM10. Carbohydrate-Binding Module Family 10.
CBM2. Carbohydrate-Binding Module Family 2.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACE85757 ; ACE85757 ; CJA_2472 .
GeneIDi 6416717.
KEGGi cja:CJA_2472.
PATRICi 21328310. VBICelJap122165_2424.

Phylogenomic databases

HOGENOMi HOG000245359.
OrthoDBi EOG6QRW4D.

Enzyme and pathway databases

BioCyci CJAP498211:GHIT-2463-MONOMER.

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
2.30.32.30. 1 hit.
2.60.40.10. 1 hit.
2.60.40.290. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR002883. CBM10/Dockerin_dom.
IPR018366. CBM2_CS.
IPR009031. CBM_fam10.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR004197. Glyco_hydro_9_Ig-like.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR000601. PKD_dom.
[Graphical view ]
Pfami PF02013. CBM_10. 1 hit.
PF00553. CBM_2. 1 hit.
PF02927. CelD_N. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
PF00801. PKD. 1 hit.
[Graphical view ]
SMARTi SM00637. CBD_II. 1 hit.
SM01064. CBM_10. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF49299. SSF49299. 1 hit.
SSF49384. SSF49384. 1 hit.
SSF57615. SSF57615. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of a carboxymethylcellulase gene from Pseudomonas fluorescens subsp. cellulosa."
    Hall J., Gilbert H.J.
    Mol. Gen. Genet. 213:112-117(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
    DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
    J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ueda107.

Entry informationi

Entry nameiGUNA_CELJU
AccessioniPrimary (citable) accession number: P10476
Secondary accession number(s): B3PKK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 20, 2010
Last modified: October 29, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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