Reviewed, UniProtKB/Swiss-Prot P23659 (GUNZ_CLOSR)

Names and origin

Protein names

Recommended name:
    Endoglucanase Z
    EC=3.2.1.4
Alternative name(s):
    Endo-1,4-beta-glucanase
    Thermoactive cellulase
    Avicelase I

Gene names

Name:

celZ

Organism

Clostridium stercorarium

Taxonomic identifier

1510 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	986 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence similarities	Belongs to the glycosyl hydrolase 9 (cellulase E) family. Contains 2 CBM3 (carbohydrate binding type-3) domains.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cellulase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Ref.1
	Chain	26 – 986	961	Endoglucanase Z		PRO_0000007948
Regions
	Domain	481 – 642	162	CBM3 1
	Repeat	651 – 738	88	Domain B
	Repeat	744 – 831	88	Domain B'
	Domain	836 – 986	151	CBM3 2
Sites
	Active site	400	1	By similarity
	Active site	438	1	By similarity
	Active site	447	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23659-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 1802E09B22923690	FASTA	986	109,512
	10 20 30 40 50 60 MRKFYSFAII ISLLVTGLFI HTPKAEAAGY NYGEALQKAI MFYEFQRSGK LPENKRDNWR 70 80 90 100 110 120 GDSGLNDGAD VGLDLTGGWY DAGDHVKFNL PMAYSQTMLA WAAYEAEEAL ERSGQMGYLL 130 140 150 160 170 180 DAIKWVSDYL IKCHPSPNVF YYQVGDGHLD HSWWGPAEVM QMDRPAYKVD LANPGSTVVA 190 200 210 220 230 240 EAAAALASAA VVFADRDPAY AATCIQHAKE LYNFAEITKS DSGYTAASGF YDSHSGFYDE 250 260 270 280 290 300 LSWAGVWLYL ATGDETYLNK AEQYVAYWGT EPQTNIISYK WAHCWDDVHY GACLLLAKIT 310 320 330 340 350 360 GKQIYKEAIE RHLDYWSVGY NGERVHYTPK GLAWLDSWGS LRYATTTAFL ASVYADWEGC 370 380 390 400 410 420 SREKAAIYND FAKQQIDYAL GSSGRSYVVG FGVNPPKRPH HRTAHSSWAD SMSVPDYHRH 430 440 450 460 470 480 VLIGALVGGP GKDDSYTDDI NNYINNEVAC DYNAGFVGAL AKMYEDYGGS PIPDLNAFEE 490 500 510 520 530 540 ITNDEFFVMA GINASGQNFI EIKALLHNQS GWPARVADKL SFRYFVDLTE LIEAGYSASD 550 560 570 580 590 600 VTITTNYNAG AKVTGLHPWN EAENIYYVNV DFTGTKIYPG GQSAYRKEVQ FRIAAPQNTN 610 620 630 640 650 660 FWNNDNDYSF RDIKGVTSGN TVKTVYIPVY DDGVLVFGVE PEGGSGENNS SISITNATFD 670 680 690 700 710 720 KNPAKQENIQ VVMNLNGNTL NGIKYGNTYL REGTDYTVSG DTVTILKSFL NSFDTSTVQL 730 740 750 760 770 780 IFDFSAGRDP VLTVNIIDTT TSASIVPTTA DFDKNPDASR DVKVKLVPNG NTLLAVKKDG 790 800 810 820 830 840 EALVLGRDYS IDGDEVTIFR EYLADQPVGR VTLTFDFDRG TDPVLTINIT DSRQVETGVI 850 860 870 880 890 900 QIQMFNGNTS DKTNGIMPRY RLTNTGTTPI RLSDVKIRYY YTIDGEKDQN FWCDWSSVGS 910 920 930 940 950 960 NNITGTFVKM AEPKEGADYY LETGFTDGAG YLQPNQSIEV QNRFSKADWT DYIQTNDYSF 970 980 STNTSYGSND RITVYISGVL VSGIEP

References

[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: 2250652] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-36 AND 475-486. Strain: NCIB 11745.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X55299 Genomic DNA. Translation: CAA39010.1. Sequence problems.
PIR	S12021.
3D structure databases
HSSP	HSSP built from PDB template 1G87 based on UniProtKB P37700.
ModBase	Search...
Protein family/group databases
CAZy	CBM3. Carbohydrate-Binding Module Family 3. GH9. Glycoside Hydrolase Family 9.
Enzyme and pathway databases
BRENDA	3.2.1.4. 16695.
Family and domain databases
InterPro	IPR012341. 6hp_glycosidase. IPR001956. CBD_3. IPR005102. DUF291. IPR001701. Glyco_hydro_9. IPR018221. Glyco_hydro_9_AS. IPR013783. Ig-like_fold. [Graphical view]
Gene3D	G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PANTHER	PTHR22298:SF3. Glyco_hydro_9. 1 hit.
Pfam	PF00942. CBM_3. 2 hits. PF03442. DUF291. 2 hits. PF00759. Glyco_hydro_9. 1 hit. [Graphical view]
ProDom	PD001947. CBD_3. 2 hits. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS51172. CBM3. 2 hits. PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit. PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUNZ_CLOSR

Accession

Primary (citable) accession number: P23659

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 5, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)