Q7Z9M8 (XG74_HYPJQ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Xyloglucanase
Short name=XG
EC=3.2.1.155

Alternative name(s):
Cel74a

Gene names

Name:	cel74a
ORF Names:	TRIREDRAFT_49081

Organism

Hypocrea jecorina (strain QM6a) (Trichoderma reesei) [Complete proteome]

Taxonomic identifier

431241 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea

Protein attributes

Sequence length	838 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)

Function	Hydrolyzes the glucosidic bonds of unbranched Glc residues in tamarind seed xyloglucan, producing XXXG, XLXG, XXLG and XLLG. Has a low activity against beta-glucan and carboxymethylcellulose. Not active against Avicel, laminarin, xylan, galactomannan, linear and branched arabinans, galactan, polygalacturonic acid, starch, beta-D-Glcp, beta-D-cellobiose, beta-D-Galp, beta-D-Xylp, alpha-D-Xylp, alpha-L-Araf and alpha-L-Arap. Ref.3
Catalytic activity	Hydrolysis of (1->4)-D-glucosidic linkages in xyloglucans so as to successively remove oligosaccharides from the chain end. Ref.3
Sequence similarities	Belongs to the glycosyl hydrolase 74 family. Ref.3 Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.
Biophysicochemical properties	pH dependence: Optimum pH is 5.3. Ref.3 Temperature dependence: Has a half life of 15 minutes at 60 degrees Celsius. Ref.3

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	cellulose binding Inferred from electronic annotation. Source: InterPro xyloglucan-specific exo-beta-1,4-glucanase 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 – 19	19	Potential
	Chain	20 – 838	819	Xyloglucanase		PRO_0000395871
Regions
	Domain	802 – 838	37	CBM1
	Compositional bias	673 – 753	81	Gly-rich
	Compositional bias	755 – 794	40	Ser-rich
Sites
	Active site	53	1	Nucleophile By similarity UniProtKB Q70DK5
	Active site	469	1	Proton donor By similarity UniProtKB Q70DK5
Amino acid modifications
	Glycosylation	232	1	N-linked (GlcNAc...) Potential
	Glycosylation	436	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q7Z9M8 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: FBE3D08F2A74FA84	FASTA	838	87,133
	10 20 30 40 50 60 MKVSRVLALV LGAVIPAHAA FSWKNVKLGG GGGFVPGIIF HPKTKGVAYA RTDIGGLYRL 70 80 90 100 110 120 NADDSWTAVT DGIADNAGWH NWGIDAVALD PQDDQKVYAA VGMYTNSWDP SNGAIIRSSD 130 140 150 160 170 180 RGATWSFTNL PFKVGGNMPG RGAGERLAVD PANSNIIYFG ARSGNGLWKS TDGGVTFSKV 190 200 210 220 230 240 SSFTATGTYI PDPSDSNGYN SDKQGLMWVT FDSTSSTTGG ATSRIFVGTA DNITASVYVS 250 260 270 280 290 300 TNAGSTWSAV PGQPGKYFPH KAKLQPAEKA LYLTYSDGTG PYDGTLGSVW RYDIAGGTWK 310 320 330 340 350 360 DITPVSGSDL YFGFGGLGLD LQKPGTLVVA SLNSWWPDAQ LFRSTDSGTT WSPIWAWASY 370 380 390 400 410 420 PTETYYYSIS TPKAPWIKNN FIDVTSESPS DGLIKRLGWM IESLEIDPTD SNHWLYGTGM 430 440 450 460 470 480 TIFGGHDLTN WDTRHNVSIQ SLADGIEEFS VQDLASAPGG SELLAAVGDD NGFTFASRND 490 500 510 520 530 540 LGTSPQTVWA TPTWATSTSV DYAGNSVKSV VRVGNTAGTQ QVAISSDGGA TWSIDYAADT 550 560 570 580 590 600 SMNGGTVAYS ADGDTILWST ASSGVQRSQF QGSFASVSSL PAGAVIASDK KTNSVFYAGS 610 620 630 640 650 660 GSTFYVSKDT GSSFTRGPKL GSAGTIRDIA AHPTTAGTLY VSTDVGIFRS TDSGTTFGQV 670 680 690 700 710 720 STALTNTYQI ALGVGSGSNW NLYAFGTGPS GARLYASGDS GASWTDIQGS QGFGSIDSTK 730 740 750 760 770 780 VAGSGSTAGQ VYVGTNGRGV FYAQGTVGGG TGGTSSSTKQ SSSSTSSASS STTLRSSVVS 790 800 810 820 830 TTRASTVTSS RTSSAAGPTG SGVAGHYAQC GGIGWTGPTQ CVAPYVCQKQ NDYYYQCV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Transcriptional regulation of biomass-degrading enzymes in the filamentous fungus Trichoderma reesei." Foreman P.K., Brown D., Dankmeyer L., Dean R., Diener S., Dunn-Coleman N.S., Goedegebuur F., Houfek T.D., England G.J., Kelley A.S., Meerman H.J., Mitchell T., Mitchinson C., Olivares H.A., Teunissen P.J.M., Yao J., Ward M. J. Biol. Chem. 278:31988-31997(2003) [PubMed: 12788920] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: QM6a.
[2]	"Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)." Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E., Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G., Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I., Larrondo L.F. , de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B., Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N., Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A., Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S., Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S. Nat. Biotechnol. 26:553-560(2008) [PubMed: 18454138] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: QM6a.
[3]	"Specific xyloglucanases as a new class of polysaccharide-degrading enzymes." Grishutin S.G., Gusakov A.V., Markov A.V., Ustinov B.B., Semenova M.V., Sinitsyn A.P. Biochim. Biophys. Acta 1674:268-281(2004) [PubMed: 15541296] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY281371 mRNA. Translation: AAP57752.1. GL985067 Genomic DNA. Translation: EGR47596.1.
3D structure databases
ProteinModelPortal	Q7Z9M8.
SMR	Q7Z9M8. Positions 804-838.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7Z9M8.
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH74. Glycoside Hydrolase Family 74.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
PhylomeDB	Q7Z9M8.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16608.
BRENDA	3.2.1.155. 6451.
Family and domain databases
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR015943. WD40/YVTN_repeat-like_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
Pfam	PF00734. CBM_1. 1 hit. [Graphical view]
ProDom	PD001821. CBD_fun. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00236. fCBD. 1 hit. [Graphical view]
SUPFAM	SSF57180. CBD_fun. 1 hit.
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XG74_HYPJQ

Accession

Primary (citable) accession number: Q7Z9M8
Secondary accession number(s): G0RLY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 10, 2010
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program