Q8GJ37 (Q8GJ37_CLOSR) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Celloxylanase CelX EMBL CAD48314.1
EC=3.2.1.8 EMBL CAD48314.1

Gene names

Name:

XynC EMBL CAD48314.1

Organism

Clostridium stercorarium EMBL CAD48314.1

Taxonomic identifier

1510 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1032 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family. RuleBase RU003432

Ontologies

Keywords
Biological process	Xylan degradation EMBL CAD48314.1
Molecular function	Glycosidase RuleBase RU003432 EMBL CAD48314.1 Hydrolase
Gene Ontology (GO)
Biological process	carbohydrate catabolic process Inferred from electronic annotation. Source: InterPro xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro endo-1,4-beta-xylanase 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
	Chain	2 – 1032	1031	CelX EMBL CAD48314.1		PRO_5000068843

Sequences

	Sequence		Length	Mass (Da)
	Q8GJ37 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 985733F07F18E99D	FASTA	1,032	115,688
	10 20 30 40 50 60 MNGRNGGKRP IASLLVLTLA FLFIPVTKAE TTVYHETFAE GKGAAVQSGG ATITHVTGKF 70 80 90 100 110 120 FDGNGDGAAL YISNRVNNWD AADFRFSDIG LQDGRIYKIT VKGYVDPDVH VPEGSQIWLQ 130 140 150 160 170 180 TVNSYGWWGS TDIKAGEAFT LTGVYKVDTT NDYALRIQSN DTGAFVPFYI GEILITEETV 190 200 210 220 230 240 PQDDSRNGNK THAEKFTPIT FEDQTTGGFT GRAGTEILTV TDEANHTDGG RYSLKVGGRN 250 260 270 280 290 300 DTWHGPALGV EKYVDQGYEY KVAVYVRLIS PESAQLQLST QIGEGTSASY VNLAKKNVAI 310 320 330 340 350 360 SDGWVLLEGT YRYDNLGGGY LTIYVESPDS PEASFYIDDI NFEPTGMKSE EIEKGLKSLK 370 380 390 400 410 420 DVYKDNFLTG TAISLRDLEG VRFELLKKHF NAVTAENAMK PSELQREKGN FTFDGADRLV 430 440 450 460 470 480 NAAISAGMKV HGHTLVWHQQ TPAWMNIKLD SGGNIVYLSR EEALENMRNH IRTVIEHFGD 490 500 510 520 530 540 KVISWDVVNE AMSDNPSNPS DWRGSLRKSP WYYAIGEDYV EQAFLAAREV LDEHPEWDIK 550 560 570 580 590 600 LYYNDYNLDN QNKALAVYNM VRELNEKYQK THPGKLLIDG IGMQGHYSVN TNPKNVELSL 610 620 630 640 650 660 KRFTELGVEV SISELDIRAG SNYQLTEKEA NAQAYLYAQL FKIFREYSDS IARVTFWGMD 670 680 690 700 710 720 DGTSWRAEES PLLFDRTLKA KPAYYAVADP DEFIEKYKPE TIEANRAYAV YGTPEIDGKT 730 740 750 760 770 780 DEVWNKAPEL KINRYQTAWH GADGTARVLY DENNLYVLIK VNDTQLDKGS PNPWEQDSVE 790 800 810 820 830 840 IFIDENNAKT SFYEEDDGQY RVNFENETSF NPESIAGGFE SAAEVSGTNY TLEVKIPFRT 850 860 870 880 890 900 VKPVSNMQIG FDVQINDGKN GVRQSIATWN DPTGNAWQDT SVFGILTLKS KNPVTRGEAI 910 920 930 940 950 960 VKIMKAYDME PLENWNDNFS DASGSYAGYY PRAKETGFVS GIGDNKIGAE IPLTREMFFT 970 980 990 1000 1010 1020 MIYNIERITG KMQGIDISDA ELTLFSDYND LSEWAEEAVK ALVKSGRIKI NGDLLPKRLM 1030 DAEEVEAFLR LR

References

[1]	"Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes." Adelsberger H., Hertel C., Glawischnig E., Zverlov V.V., Schwarz W.H. Microbiology 150:2257-2266(2004) [PubMed: 15256568] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: NCIMB 11745 EMBL CAD48314.1.
[2]	"Klonierung und Sequenzierung von Genen cellulolytischer Enzyme aus Clostridium stercorarium." Jauris S. Thesis (1990), Department of Microbiology, Technical University, Muenchen, Germany Cited for: NUCLEOTIDE SEQUENCE. Strain: NCIMB 11745 EMBL CAD48314.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ508408 mRNA. Translation: CAD48314.1.
3D structure databases
HSSP	HSSP built from PDB template 1I8A based on UniProtKB Q60037.
ProteinModelPortal	Q8GJ37.
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
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. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.1190. CBD9. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF02018. CBM_4_9. 1 hit. PF06452. DUF1083. 1 hit. PF00331. Glyco_hydro_10. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
SUPFAM	SSF49344. CBD9-like. 1 hit. SSF49785. Gal_bind_like. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q8GJ37_CLOSR

Accession

Primary (citable) accession number: Q8GJ37

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2003
Last sequence update:	March 1, 2003
Last modified:	October 19, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)