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Protein

Endoglucanase A

Gene

celCCA

Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Miscellaneous

The C-terminus (AA 411-475) may play a role in organizing the cellulosome complex.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei147Curated1
Active sitei195Proton donor1
Active sitei332Nucleophile1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciCCEL394503:G1GUL-1122-MONOMER

Protein family/group databases

CAZyiGH5 Glycoside Hydrolase Family 5

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase A (EC:3.2.1.4)
Alternative name(s):
Cellulase A
EGCCA
Endo-1,4-beta-glucanase A
Gene namesi
Name:celCCA
Ordered Locus Names:Ccel_1099
OrganismiClostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Taxonomic identifieri394503 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
Proteomesi
  • UP000001349 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi104R → K: Small loss of activity. 1 Publication1
Mutagenesisi104R → S or V: Large decrease of activity. 1 Publication1
Mutagenesisi147H → S, E, G or F: Total loss of activity. 1 Publication1
Mutagenesisi148H → V: Large decrease of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 261 PublicationAdd BLAST26
ChainiPRO_000000784527 – 475Endoglucanase AAdd BLAST449

Proteomic databases

PRIDEiP17901

Interactioni

Protein-protein interaction databases

STRINGi394503.Ccel_1099

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 31Combined sources3
Helixi46 – 54Combined sources9
Beta strandi56 – 59Combined sources4
Helixi75 – 77Combined sources3
Helixi78 – 81Combined sources4
Helixi89 – 98Combined sources10
Beta strandi102 – 105Combined sources4
Helixi110 – 112Combined sources3
Turni115 – 118Combined sources4
Helixi122 – 136Combined sources15
Turni137 – 139Combined sources3
Beta strandi141 – 145Combined sources5
Turni152 – 154Combined sources3
Helixi160 – 162Combined sources3
Helixi163 – 180Combined sources18
Turni181 – 183Combined sources3
Beta strandi188 – 191Combined sources4
Turni202 – 205Combined sources4
Helixi212 – 234Combined sources23
Helixi237 – 240Combined sources4
Beta strandi244 – 247Combined sources4
Helixi249 – 251Combined sources3
Helixi253 – 257Combined sources5
Beta strandi274 – 279Combined sources6
Helixi284 – 287Combined sources4
Helixi291 – 293Combined sources3
Helixi304 – 320Combined sources17
Helixi322 – 324Combined sources3
Beta strandi328 – 333Combined sources6
Helixi341 – 357Combined sources17
Beta strandi361 – 364Combined sources4
Beta strandi371 – 374Combined sources4
Turni382 – 385Combined sources4
Beta strandi386 – 389Combined sources4
Helixi390 – 399Combined sources10
Beta strandi418 – 420Combined sources3
Helixi424 – 435Combined sources12
Helixi443 – 445Combined sources3
Helixi455 – 465Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EDGX-ray1.60A27-401[»]
2VN5X-ray1.90B/D410-475[»]
2VN6X-ray1.49B410-472[»]
ProteinModelPortaliP17901
SMRiP17901
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17901

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini409 – 474DockerinPROSITE-ProRule annotationAdd BLAST66

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108K2F Bacteria
COG2730 LUCA
HOGENOMiHOG000027405
KOiK01179
OMAiYVILNTH
OrthoDBiPOG091H14IK

Family and domain databases

InterProiView protein in InterPro
IPR002105 Dockerin_1_rpt
IPR016134 Dockerin_dom
IPR036439 Dockerin_dom_sf
IPR001547 Glyco_hydro_5
IPR018087 Glyco_hydro_5_CS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00150 Cellulase, 1 hit
PF00404 Dockerin_1, 2 hits
SUPFAMiSSF51445 SSF51445, 1 hit
SSF63446 SSF63446, 1 hit
PROSITEiView protein in PROSITE
PS00448 CLOS_CELLULOSOME_RPT, 2 hits
PS51766 DOCKERIN, 1 hit
PS00018 EF_HAND_1, 1 hit
PS00659 GLYCOSYL_HYDROL_F5, 1 hit

Sequencei

Sequence statusi: Complete.

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

P17901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTTAFLLC FLMIFTALLP MQNANAYDAS LIPNLQIPQK NIPNNDGMNF
60 70 80 90 100
VKGLRLGWNL GNTFDAFNGT NITNELDYET SWSGIKTTKQ MIDAIKQKGF
110 120 130 140 150
NTVRIPVSWH PHVSGSDYKI SDVWMNRVQE VVNYCIDNKM YVILNTHHDV
160 170 180 190 200
DKVKGYFPSS QYMASSKKYI TSVWAQIAAR FANYDEHLIF EGMNEPRLVG
210 220 230 240 250
HANEWWPELT NSDVVDSINC INQLNQDFVN TVRATGGKNA SRYLMCPGYV
260 270 280 290 300
ASPDGATNDY FRMPNDISGN NNKIIVSVHA YCPWNFAGLA MADGGTNAWN
310 320 330 340 350
INDSKDQSEV TWFMDNIYNK YTSRGIPVII GECGAVDKNN LKTRVEYMSY
360 370 380 390 400
YVAQAKARGI LCILWDNNNF SGTGELFGFF DRRSCQFKFP EIIDGMVKYA
410 420 430 440 450
FEAKTDPDPV IVYGDYNNDG NVDALDFAGL KKYIMAADHA YVKNLDVNLD
460 470
NEVNAFDLAI LKKYLLGMVS KLPSN
Length:475
Mass (Da):53,625
Last modified:November 1, 1990 - v1
Checksum:i1AF20EA2C0A132F9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93096 Genomic DNA Translation: AAA51444.1
M32362 Genomic DNA Translation: AAA23221.1
CP001348 Genomic DNA Translation: ACL75458.1
RefSeqiWP_015924614.1, NC_011898.1

Genome annotation databases

EnsemblBacteriaiACL75458; ACL75458; Ccel_1099
KEGGicce:Ccel_1099

Similar proteinsi

Entry informationi

Entry nameiGUNA_CLOCE
AccessioniPrimary (citable) accession number: P17901
Secondary accession number(s): B8HZV8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 23, 2018
This is version 134 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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