Endo-1,4-beta-xylanase A precursor - Paenibacillus sp. (strain JDR-2)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Endo-1,4-beta-xylanase A
EC=3.2.1.8

Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A

Gene names

Name:	xynA1
Synonyms:	xynA
Ordered Locus Names:	Pjdr2_0221

Organism

Paenibacillus sp. (strain JDR-2) [Complete proteome] [HAMAP]

Taxonomic identifier

324057 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Paenibacillaceae › Paenibacillus

Protein attributes

Sequence length	1462 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	Catalyzes the depolymerization of methylglucuronoxylan (MeGAXn), a beta-1,4 xylan in which 10% to 20% of the xylose residues are substituted with alpha-1,2-4-O-methylglucuronate (MeGA) residues, which is predominant in hemicellulose fractions of hardwood and crop residues. Generates xylobiose (X2) and aldotetrauronate (MeGAX3) as the predominant products of MeGAXn hydrolysis; these products are then directly assimilated by the bacterium for subsequent metabolism. Thus, allows the bacterium to efficiently use polymeric MeGAXn as a growth substrate. Ref.1
Catalytic activity	Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.1
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted › cell wall Ref.1.
Sequence similarities	Belongs to the glycosyl hydrolase 10 (cellulase F) family. Contains 3 CBM-cenC (cenC-type cellulose-binding) domains. Contains 3 SLH (S-layer homology) domains.
Biophysicochemical properties	Kinetic parameters: V_max=8.0 µmol/min/mg enzyme with sweet gum methylglucuronoxylan as substrate Ref.1 pH dependence: Optimum pH is 6.5 with sweet gum methylglucuronoxylan as substrate. Temperature dependence: Optimum temperature is 45 degrees Celsius with sweet gum methylglucuronoxylan as substrate.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation Xylan degradation
Cellular component	Cell wall Secreted
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW xylan catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	cell wall Inferred from direct assay Ref.1. Source: UniProtKB extracellular region 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 direct assay Ref.1. Source: UniProtKB
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 – 1462

1432

Endo-1,4-beta-xylanase A

PRO_5000484609

Regions

Domain

64 – 165

102

CBM-cenC 1

Domain

207 – 319

113

CBM-cenC 2

Domain

360 – 490

131

CBM-cenC 3

Domain

1279 – 1342

64

SLH 1

Domain

1345 – 1404

60

SLH 2

Domain

1407 – 1462

56

SLH 3

Compositional bias

186 – 191

6

Poly-Thr

Sites

Active site

651

1

Proton donor By similarity

Active site

706

1

By similarity

Active site

775

1

Nucleophile By similarity

Experimental info

Sequence conflict

313

1

S → T in CAI79477. Ref.1

Sequence conflict

454 – 461

8

SLASKTIT → TPTTQAWQARRLP in CAI79477. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

C6CRV0 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: AE29664CDEA3BF3E
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FASTA

1,462

157,322

        10         20         30         40         50         60 
MSRSLKKFVS ILLAAALLIP IGRLAPVAEA AENPTIVYHE DFAIDKGKAI QSGGASLTQV 

        70         80         90        100        110        120 
TGKVFDGNND GSALYVSNRA NTWDAADFKF ADIGLQNGKT YTVTVKGYVD QDATVPSGAQ 

       130        140        150        160        170        180 
AFLQAVDSNN YGFLASANFA AGTAFTLTKE FTVDTSVSTQ LRVQSSEEGK AVPFYIGDIL 

       190        200        210        220        230        240 
ITANPTTTTN TVYHEDFATD KGKAVQSGGA NLAQVADKVF DGNDDGKALY VSNRANTWDA 

       250        260        270        280        290        300 
ADFKFADIGL QNGKTYTVTV KGYVDQDATV PSGAQAFLQA VDSNNYGFLA SANFAARSAF 

       310        320        330        340        350        360 
TLTKEFTVDT SVSTQLRVQS SEEGKAVPFY IGDILITETV NSGGGQEDPP RPPALPFNTI 

       370        380        390        400        410        420 
TFEDQTAGGF TGRAGTETLT VTNESNHTAD GSYSLKVEGR TTSWHGPSLR VEKYVDKGYE 

       430        440        450        460        470        480 
YKVTAWVKLL SPETSTKLEL ASQVGDGGSA NYPSLASKTI TAADGWVQLQ GNYRYNSVGG 

       490        500        510        520        530        540 
EYLTIYVQSS NATASYYIDD ISFESTGSGP VGIQKDLAPL KDVYKNDFLI GNAISAEDLE 

       550        560        570        580        590        600 
GTRLELLKMH HDVVTAGNAM KPDALQPTKG NFTFTAADAM IDKVLAEGMK MHGHVLVWHQ 

       610        620        630        640        650        660 
QSPAWLNTKK DDNNNTVPLG RDEALDNLRT HIQTVMKHFG NKVISWDVVN EAMNDNPSNP 

       670        680        690        700        710        720 
ADYKASLRQT PWYQAIGSDY VEQAFLAARE VLDENPSWNI KLYYNDYNED NQNKATAIYN 

       730        740        750        760        770        780 
MVKDINDRYA AAHNGKLLID GVGMQGHYNI NTNPDNVKLS LEKFISLGVE VSVSELDVTA 

       790        800        810        820        830        840 
GNNYTLPENL AVGQAYLYAQ LFKLYKEHAD HIARVTFWGM DDNTSWRAEN NPLLFDKNLQ 

       850        860        870        880        890        900 
AKPAYYGVID PDKYMEEHAP ESKDANQAEA QYGTPVIDGT VDSIWSNAQA MPVNRYQMAW 

       910        920        930        940        950        960 
QGATGTAKAL WDDQNLYVLI QVSDSQLNKA NENAWEQDSV EVFLDQNNGK TTFYQNDDGQ 

       970        980        990       1000       1010       1020 
YRVNFDNETS FSPASIAAGF ESQTKKTANS YTVELKIPLT AVTPANQKKL GFDVQINDAT 

      1030       1040       1050       1060       1070       1080 
DGARTSVAAW NDTTGNGYQD TSVYGELTLA GKGTGGTGTV GTTVPQTGNV VKNPDGSTTL 

      1090       1100       1110       1120       1130       1140 
KPEVKTTNGN AVGTVTGDDL KKALDQAAPA AGGKKQVIID VPLQANAATY AVQLPTQSLK 

      1150       1160       1170       1180       1190       1200 
SQDGYQLTAK IANAFIQIPS NMLANTNVTT DQVSIRVAKA SLDNVDAATR ELIGNRPVID 

      1210       1220       1230       1240       1250       1260 
LSLVAGGNVI AWNNPTAPVT VAVPYAPTAE ELKHPEHILI WYIDGSGKAT PVPNSRYDAA 

      1270       1280       1290       1300       1310       1320 
LGAVVFQTTH FSTYAAVSVF TTFGDLAKVP WAKEAIDAMA SRGVIKGTGE NTFSPAASIK 

      1330       1340       1350       1360       1370       1380 
RADFIALLVR ALELHGTGTT DTAMFSDVPA NAYYYNELAV AKQLGIATGF EDNTFKPDSS 

      1390       1400       1410       1420       1430       1440 
ISRQDMMVLT TRALAVLGKQ LPAGGSLNAF SDAASVAGYA QDSVAALVKA GVVQGSGSKL 

      1450       1460 
APNDQLTRAE AAVILYRIWK LQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Paenibacillus sp. strain JDR-2 and XynA1: a novel system for methylglucuronoxylan utilization." Stjohn F.J., Rice J.D., Preston J.F. Appl. Environ. Microbiol. 72:1496-1506(2006) [PubMed: 16461704] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. Strain: JDR-2.
[2]	"Complete sequence of Paenibacillus sp. JDR-2." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Shanmugam K.T., Ingram L.O., Preston J. Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JDR-2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ938162 Genomic DNA. Translation: CAI79477.1. CP001656 Genomic DNA. Translation: ACS98901.1.
RefSeq	YP_003008988.1. NC_012914.1.
3D structure databases
ProteinModelPortal	C6CRV0.
ModBase	Search...
Protein-protein interaction databases
STRING	C6CRV0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8127565.
GenomeReviews	Gene locus Pjdr2_0221 in contig CP001656_GR.
KEGG	pjd:Pjdr2_0221.
PATRIC	22830917. VBIPaeSp118865_0225.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	FYIGDIL.
ProtClustDB	CLSK2482236.
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. IPR001119. S-layer_homology_dom. [Graphical view]
Gene3D	G3DSA:2.60.40.1190. CBD9. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K01181.
Pfam	PF02018. CBM_4_9. 3 hits. PF06452. DUF1083. 1 hit. 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. 1 hit. SSF49785. Gal_bind_like. 3 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00591. GLYCOSYL_HYDROL_F10. 1 hit. PS51272. SLH. 3 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNA1_PAESJ

Accession

Primary (citable) accession number: C6CRV0
Secondary accession number(s): Q53I45

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 31, 2011
Last sequence update:	September 1, 2009
Last modified:	January 25, 2012
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents