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P23659

- GUNZ_CLOSR

UniProt

P23659 - GUNZ_CLOSR

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Protein

Endoglucanase Z

Gene

celZ

Organism
Clostridium stercorarium
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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 sitei400 – 4001By similarity
Active sitei438 – 4381By similarity
Active sitei447 – 4471By 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

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase Z (EC:3.2.1.4)
Alternative name(s):
Avicelase I
Endo-1,4-beta-glucanase
Thermoactive cellulase
Gene namesi
Name:celZ
OrganismiClostridium stercorarium
Taxonomic identifieri1510 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – 986961Endoglucanase ZPRO_0000007948Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP23659.
SMRiP23659. Positions 30-641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini481 – 642162CBM3 1PROSITE-ProRule annotationAdd
BLAST
Repeati651 – 73888Domain BAdd
BLAST
Repeati744 – 83188Domain B'Add
BLAST
Domaini836 – 986151CBM3 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 CBM3 (carbohydrate binding type-3) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 2 hits.
2.60.40.710. 2 hits.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR005102. Carbo-bd_X2.
IPR001956. CBD_3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF00942. CBM_3. 2 hits.
PF03442. CBM_X2. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
SMARTiSM01067. CBM_3. 2 hits.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 2 hits.
SSF81296. SSF81296. 2 hits.
PROSITEiPS51172. CBM3. 2 hits.
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.

P23659-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRKFYSFAII ISLLVTGLFI HTPKAEAAGY NYGEALQKAI MFYEFQRSGK
60 70 80 90 100
LPENKRDNWR GDSGLNDGAD VGLDLTGGWY DAGDHVKFNL PMAYSQTMLA
110 120 130 140 150
WAAYEAEEAL ERSGQMGYLL DAIKWVSDYL IKCHPSPNVF YYQVGDGHLD
160 170 180 190 200
HSWWGPAEVM QMDRPAYKVD LANPGSTVVA EAAAALASAA VVFADRDPAY
210 220 230 240 250
AATCIQHAKE LYNFAEITKS DSGYTAASGF YDSHSGFYDE LSWAGVWLYL
260 270 280 290 300
ATGDETYLNK AEQYVAYWGT EPQTNIISYK WAHCWDDVHY GACLLLAKIT
310 320 330 340 350
GKQIYKEAIE RHLDYWSVGY NGERVHYTPK GLAWLDSWGS LRYATTTAFL
360 370 380 390 400
ASVYADWEGC SREKAAIYND FAKQQIDYAL GSSGRSYVVG FGVNPPKRPH
410 420 430 440 450
HRTAHSSWAD SMSVPDYHRH VLIGALVGGP GKDDSYTDDI NNYINNEVAC
460 470 480 490 500
DYNAGFVGAL AKMYEDYGGS PIPDLNAFEE ITNDEFFVMA GINASGQNFI
510 520 530 540 550
EIKALLHNQS GWPARVADKL SFRYFVDLTE LIEAGYSASD VTITTNYNAG
560 570 580 590 600
AKVTGLHPWN EAENIYYVNV DFTGTKIYPG GQSAYRKEVQ FRIAAPQNTN
610 620 630 640 650
FWNNDNDYSF RDIKGVTSGN TVKTVYIPVY DDGVLVFGVE PEGGSGENNS
660 670 680 690 700
SISITNATFD KNPAKQENIQ VVMNLNGNTL NGIKYGNTYL REGTDYTVSG
710 720 730 740 750
DTVTILKSFL NSFDTSTVQL IFDFSAGRDP VLTVNIIDTT TSASIVPTTA
760 770 780 790 800
DFDKNPDASR DVKVKLVPNG NTLLAVKKDG EALVLGRDYS IDGDEVTIFR
810 820 830 840 850
EYLADQPVGR VTLTFDFDRG TDPVLTINIT DSRQVETGVI QIQMFNGNTS
860 870 880 890 900
DKTNGIMPRY RLTNTGTTPI RLSDVKIRYY YTIDGEKDQN FWCDWSSVGS
910 920 930 940 950
NNITGTFVKM AEPKEGADYY LETGFTDGAG YLQPNQSIEV QNRFSKADWT
960 970 980
DYIQTNDYSF STNTSYGSND RITVYISGVL VSGIEP
Length:986
Mass (Da):109,512
Last modified:November 1, 1991 - v1
Checksum:i1802E09B22923690
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55299 Genomic DNA. Translation: CAA39010.1. Sequence problems.
PIRiS12021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55299 Genomic DNA. Translation: CAA39010.1 . Sequence problems.
PIRi S12021.

3D structure databases

ProteinModelPortali P23659.
SMRi P23659. Positions 30-641.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM3. Carbohydrate-Binding Module Family 3.
GH9. Glycoside Hydrolase Family 9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
2.60.40.10. 2 hits.
2.60.40.710. 2 hits.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR005102. Carbo-bd_X2.
IPR001956. CBD_3.
IPR001701. Glyco_hydro_9.
IPR018221. Glyco_hydro_9_AS.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF00942. CBM_3. 2 hits.
PF03442. CBM_X2. 2 hits.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view ]
SMARTi SM01067. CBM_3. 2 hits.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF49384. SSF49384. 2 hits.
SSF81296. SSF81296. 2 hits.
PROSITEi PS51172. CBM3. 2 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence analysis of the Clostridium stercorarium celZ gene encoding a thermoactive cellulase (Avicelase I): identification of catalytic and cellulose-binding domains."
    Jauris S., Ruecknagel K.P., Schwarz W.H., Kratzsch P., Bronnenmeier K., Staudenbauer W.L.
    Mol. Gen. Genet. 223:258-267(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-36 AND 475-486.
    Strain: NCIB 11745.

Entry informationi

Entry nameiGUNZ_CLOSR
AccessioniPrimary (citable) accession number: P23659
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 1, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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