P38535 (XYNX_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exoglucanase XynX
EC=3.2.1.91

Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase

Gene names

Name:

xynX

Organism

Clostridium thermocellum

Taxonomic identifier

1515 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1087 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family. Contains 1 CBM-cenC (cenC-type cellulose-binding) domain. Contains 3 SLH (S-layer homology) domains.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
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 cellulose 1,4-beta-cellobiosidase 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 – 30	30	Potential
	Chain	31 – 1087	1057	Exoglucanase XynX		PRO_0000007982
Regions
	Domain	37 – 188	152	CBM-cenC
	Domain	903 – 966	64	SLH 1
	Domain	967 – 1025	59	SLH 2
	Domain	1028 – 1087	60	SLH 3
Sites
	Active site	347	1	Proton donor By similarity
	Active site	389	1	By similarity
	Active site	452	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	P38535 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 88077FC27AC83F51	FASTA	1,087	120,358
	10 20 30 40 50 60 MKNNLSKFVS IFTAFIMIFG TSLFFPHVSA FADDNNANLV SNGDFESGTI DGWIKQGNPT 70 80 90 100 110 120 LAATTEEAIG QYSMKVAGRT QTYEGPAYSF LGKMQKGQSY NVSLKVRLVS GQNSSNPLIT 130 140 150 160 170 180 VTMFREDDNG KHYDTIVWQK QVSEDSWTTV NGTYTLDYTG TLKTLYMYVE SPDPTLEYYI 190 200 210 220 230 240 DDVVVTPQNP IQVGEISNNQ ITIQNDIPDL SSVFKDYFPI GVAVDPSRLN DTDPHAQLTA 250 260 270 280 290 300 KHFNMLVAEN AMKPESLQPT EGNFTFDNAD RIVDYAIAHN MKMRGHTLLW HNQVPDWFFQ 310 320 330 340 350 360 DPSDPTKPAS RDLLLQRLKT HITTVLDHFK TKYGAQNPII GWDVVNEVLD DNGSLRNSKW 370 380 390 400 410 420 LQIIGPDYIE KAFEYAHEAD PSMKLFINDY NIENNGVKTQ AMYDLVKKLK SEGVPISGIG 430 440 450 460 470 480 MQMHININSN IDNIKASIEK LASLGVEIQV TELDMNMNGN VSNEALLKQA RLYKQLFDLF 490 500 510 520 530 540 KAEKQYITAV VFWGVSDDVT WLSKPNAPLL FDSKLQAKPA YWAIADPSKA IPDIQSAKAL 550 560 570 580 590 600 EGSPTIGANV DSSWKLVKPL YANTYVEGTV GATATVKSMW DTKNLYLLVQ VSDNTPSSND 610 620 630 640 650 660 GIEIFVDKND NKSTSYETDD EHYTIKSDGT GSSDITKYVT SNADGYIVQL AIPIEDISPT 670 680 690 700 710 720 LNDKIGLDVR LNDDKGSGSI DTVTVWNDYT NSQDTNTSYF GDIVLSKPAQ VATAIYGTPV 730 740 750 760 770 780 IDGKIDDIWN KVDAITTNTW VLGSDGATAT AKMMWDDKYL YVLADVTDSN LNKSSVNPYE 790 800 810 820 830 840 QDSVEVFVDQ NNDKTSYYES DDGQYRVNYD NEQSFGGSTN SNGFKSATSL TQSGYIVEEA 850 860 870 880 890 900 IPWTSITLLN GTIIGFDLQV NDADENGKRT GIVTWCDPSG NSWQDTSGFG NLLLTGKPSG 910 920 930 940 950 960 VLKKSVTFND IKDNWAKDVI EVLASRHIVE GMTDTQYEPS KTVTRAEFTA MILKLLNIKE 970 980 990 1000 1010 1020 EAYNGEFSDV KNGDWYANAI EAAYKAGIIE GDGKNMRPND SITREEMTSI AMRAYEMLTS 1030 1040 1050 1060 1070 1080 YKEENIGATS FNDDKSISDW AKNVVANAAK LGIINGEPSN VFAPKGIATR AEAAAIIYGL LEKSNNL

References

[1]	Pack M.Y., Jung K.H. Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	M67438 Genomic DNA. Translation: AAA23227.1.
PIR	S41797.
3D structure databases
ProteinModelPortal	P38535.
SMR	P38535. Positions 711-895.
ModBase	Search...
Protein family/group databases
CAZy	CBM22. Carbohydrate-Binding Module Family 22. CBM9. Carbohydrate-Binding Module Family 9. GH10. Glycoside Hydrolase Family 10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	2.60.40.1190. 2 hits. 3.20.20.80. 1 hit.
InterPro	IPR010502. Carb-bd_dom_fam9. IPR008960. Carb-bd_dom_fam9-like. IPR015922. Carb-bd_dom_fam9-like_subgr. IPR003305. CenC_carb-bd. IPR008979. Galactose-bd-like. IPR001000. Glyco_hydro_10. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. IPR001119. S-layer_homology_dom. [Graphical view]
Pfam	PF02018. CBM_4_9. 1 hit. PF06452. DUF1083. 2 hits. PF00331. Glyco_hydro_10. 1 hit. PF00395. SLH. 3 hits. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
SUPFAM	SSF49344. CBD9-like. 2 hits. SSF49785. Gal_bind_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. 1 hit. PS00659. GLYCOSYL_HYDROL_F5. 1 hit. PS51272. SLH. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNX_CLOTM

Accession

Primary (citable) accession number: P38535

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program