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Protein

Endoglucanase D

Gene

celD

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Caution

The sequence shown here has been extracted from PDB entry 1CLC.Curated

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei177Nucleophile1
Active sitei4921 Publication1
Active sitei5221 Publication1
Active sitei531Proton donorPROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase D (EC:3.2.1.4)
Short name:
EGD
Alternative name(s):
Cellulase D
Endo-1,4-beta-glucanase
Gene namesi
Name:celD
OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
Taxonomic identifieri1515 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi41H → A: 79% of wild-type activity. 1
Mutagenesisi143H → A: 104% of wild-type activity. 1
Mutagenesisi146H → A: 77% of wild-type activity. 1
Mutagenesisi150H → A: 2% of wild-type activity. 1
Mutagenesisi163H → A: 124% of wild-type activity. 1
Mutagenesisi173H → A: 8% of wild-type activity. 1
Mutagenesisi174D → A: 0.08% of wild-type activity. 1
Mutagenesisi177D → A: 0.2% of wild-type activity. 1
Mutagenesisi198H → S: 17% of wild-type activity. 1
Mutagenesisi222D → A: 72% of wild-type activity. 1
Mutagenesisi245H → A: 90% of wild-type activity. 1
Mutagenesisi262H → A: 19% of wild-type activity. 1
Mutagenesisi293D → A: 98% of wild-type activity. 1
Mutagenesisi337D → A: 86% of wild-type activity. 1
Mutagenesisi421H → S: 32% of wild-type activity. 1
Mutagenesisi468H → A: 9% of wild-type activity. 1
Mutagenesisi492H → S: 25% of wild-type activity. 1
Mutagenesisi493D → A: 0.8% of wild-type activity. 1
Mutagenesisi499D → A: 224% of wild-type activity. 1
Mutagenesisi503E → A: 127% of wild-type activity. 1
Mutagenesisi519D → A: 91% of wild-type activity. 1
Mutagenesisi522D → A: 1% of wild-type activity. 1
Mutagenesisi525D → A: 118% of wild-type activity. 1
Mutagenesisi531E → A: 0.3% of wild-type activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei‹1 – 17Add BLAST›17
ChainiPRO_000000794918 – 625Endoglucanase DAdd BLAST608

Structurei

Secondary structure

1625
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 37Combined sources4
Beta strandi44 – 47Combined sources4
Beta strandi53 – 58Combined sources6
Beta strandi61 – 68Combined sources8
Beta strandi70 – 74Combined sources5
Turni75 – 78Combined sources4
Beta strandi79 – 85Combined sources7
Beta strandi93 – 99Combined sources7
Turni100 – 102Combined sources3
Beta strandi108 – 110Combined sources3
Turni112 – 115Combined sources4
Helixi116 – 128Combined sources13
Beta strandi135 – 139Combined sources5
Beta strandi142 – 146Combined sources5
Helixi157 – 160Combined sources4
Beta strandi175 – 177Combined sources3
Helixi182 – 198Combined sources17
Helixi200 – 203Combined sources4
Turni211 – 214Combined sources4
Beta strandi215 – 217Combined sources3
Helixi219 – 231Combined sources13
Helixi232 – 234Combined sources3
Beta strandi243 – 248Combined sources6
Helixi258 – 260Combined sources3
Beta strandi266 – 270Combined sources5
Helixi272 – 289Combined sources18
Turni290 – 292Combined sources3
Helixi294 – 313Combined sources20
Helixi336 – 350Combined sources15
Helixi353 – 363Combined sources11
Beta strandi367 – 370Combined sources4
Helixi380 – 389Combined sources10
Helixi397 – 420Combined sources24
Turni426 – 429Combined sources4
Helixi435 – 452Combined sources18
Helixi456 – 469Combined sources14
Beta strandi483 – 486Combined sources4
Helixi494 – 498Combined sources5
Helixi527 – 530Combined sources4
Helixi534 – 545Combined sources12
Turni546 – 549Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CLCX-ray1.90A1-625[»]
4CJ0X-ray1.10A1-625[»]
4CJ1X-ray1.63A1-625[»]
ProteinModelPortaliP0C2S4
SMRiP0C2S4
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2S4

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini555 – 625DockerinPROSITE-ProRule annotationAdd BLAST71

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E08 Bacteria
ENOG410XNTA LUCA

Family and domain databases

CDDicd02850 E_set_Cellulase_N, 1 hit
Gene3Di1.50.10.10, 1 hit
2.60.40.10, 1 hit
InterProiView protein in InterPro
IPR008928 6-hairpin_glycosidase_sf
IPR012341 6hp_glycosidase-like_sf
IPR004197 Cellulase_Ig-like
IPR002105 Dockerin_1_rpt
IPR016134 Dockerin_dom
IPR036439 Dockerin_dom_sf
IPR001701 Glyco_hydro_9
IPR033126 Glyco_hydro_9_Asp/Glu_AS
IPR018221 Glyco_hydro_9_His_AS
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
PfamiView protein in Pfam
PF02927 CelD_N, 1 hit
PF00404 Dockerin_1, 2 hits
PF00759 Glyco_hydro_9, 1 hit
SUPFAMiSSF48208 SSF48208, 1 hit
SSF63446 SSF63446, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS00448 CLOS_CELLULOSOME_RPT, 2 hits
PS51766 DOCKERIN, 1 hit
PS00018 EF_HAND_1, 2 hits
PS00592 GLYCOSYL_HYDROL_F9_1, 1 hit
PS00698 GLYCOSYL_HYDROL_F9_2, 1 hit

Sequencei

Sequence statusi: Fragment.

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

P0C2S4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SLTGVFPSGL IETKVSAAKI TENYQFDSRI RLNSIGFIPN HSKKATIAAN
60 70 80 90 100
CSTFYVVKED GTIVYTGTAT SMFDNDTKET VYIADFSSVN EEGTYYLAVP
110 120 130 140 150
GVGKSVNFKI AMNVYEDAFK TAMLGMYLLR CGTSVSATYN GIHYSHGPCH
160 170 180 190 200
TNDAYLDYIN GQHTKKDSTK GWHDAGDYNK YVVNAGITVG SMFLAWEHFK
210 220 230 240 250
DQLEPVALEI PEKNNSIPDF LDELKYEIDW ILTMQYPDGS GRVAHKVSTR
260 270 280 290 300
NFGGFIMPEN EHDERFFVPW SSAATADFVA MTAMAARIFR PYDPQYAEKC
310 320 330 340 350
INAAKVSYEF LKNNPANVFA NQSGFSTGEY ATVSDADDRL WAAAEMWETL
360 370 380 390 400
GDEEYLRDFE NRAAQFSKKI EADFDWDNVA NLGMFTYLLS ERPGKNPALV
410 420 430 440 450
QSIKDSLLST ADSIVRTSQN HGYGRTLGTT YYWGCNGTVV RQTMILQVAN
460 470 480 490 500
KISPNNDYVN AALDAISHVF GRNYYNRSYV TGLGINPPMN PHDRRSGADG
510 520 530 540 550
IWEPWPGYLV GGGWPGPKDW VDIQDSYQTN EIAINWNAAL IYALAGFVNY
560 570 580 590 600
NSPQNEVLYG DVNDDGKVNS TDLTLLKRYV LKAVSTLPSS KAEKNADVNR
610 620
DGRVNSSDVT ILSRYLIRVI EKLPI
Length:625
Mass (Da):69,707
Last modified:April 17, 2007 - v1
Checksum:i6BFD88E2BDF1BD8F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

PIRiA25535 CZCLDM

Similar proteinsi

Entry informationi

Entry nameiGUND_CLOTM
AccessioniPrimary (citable) accession number: P0C2S4
Secondary accession number(s): P04954
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: April 17, 2007
Last modified: March 28, 2018
This is version 55 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
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Main funding by: National Institutes of Health