Reviewed, UniProtKB/Swiss-Prot P23031 (XYNC_PSEFL)

Names and origin

Protein names

Recommended name:
    Alpha-L-arabinofuranosidase C
    EC=3.2.1.55
Alternative name(s):
    Xylanase C

Gene names

Name:

xynC

Organism

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	571 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	Xylanase C contributes to hydrolyse hemicellulose, the major component of plant cell-walls.
Catalytic activity	Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Pathway	Glycan metabolism; hemicellulose degradation.
Subcellular location	Secreted.
Miscellaneous	Acts only on high MW substrates, in which arabinose is linked to a polymeric backbone.
Sequence similarities	Belongs to the glycosyl hydrolase 62 family. Contains 1 CBM2 (carbohydrate binding type-2) domain. Contains 1 CBM6 (carbohydrate binding type-6) domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	L-arabinose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-N-arabinofuranosidase activity Inferred from electronic annotation. Source: EC polysaccharide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 37	37	Ref.1
	Chain	38 – 571	534	Alpha-L-arabinofuranosidase C		PRO_0000008033
Regions
	Domain	38 – 136	99	CBM2
	Domain	163 – 289	127	CBM6
	Compositional bias	135 – 162	28	Ser-rich (linker)
	Compositional bias	300 – 320	21	Ser-rich (linker)
Amino acid modifications
	Disulfide bond	39 ↔ 133		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P23031-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: AD19585F5E3D5555	FASTA	571	61,073
	10 20 30 40 50 60 MINHNKTPNI LAKVFKRTCG LVSTGAALAI LSQAASAACT YTIDSEWSTG FTANITLKND 70 80 90 100 110 120 TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW NGSIAPGQSI SFGLQGEKNG 130 140 150 160 170 180 STAERPTVTG AACNSATTSS VASSSSTPTT SSSSASSVAS ALLLQEAQAG FCRVDGTIDN 190 200 210 220 230 240 NHTGFTGSGF ANTNNAQGAA VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN 250 260 270 280 290 300 YTVSLPTTGA WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS 310 320 330 340 350 360 VSSSSSVQSS SSSSSTPSQT CELKAPLRWT STGPLISPKN PGWISIKDPS IVKYNDTYHV 370 380 390 400 410 420 YATYYDTAYR SMYTSFTDWN TAQQAPHISM NGSRVGNTVA PQVFYFRPHN KWYLITQWAG 430 440 450 460 470 480 AYATTDDIRN PNWSAKQKLL QGEPNGALDF WVICNDTHCY LYFSRDDGVL YVSKTTLANF 490 500 510 520 530 540 PNFSGYSIVM EDHRGNGNSY LFEAANVYKL DGQNRYLLMV EAYISGRAFS APGQRPAWMA 550 560 570 HGPLADTEAN PFAGMMFCFT MASSLKVYTC Y

References

[1]

"Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes." Kellett L.E., Poole D.M., Ferreira L.M.A., Durrant A.J., Hazlewood G.P., Gilbert H.J. Biochem. J. 272:369-376(1990) [PubMed: 2125205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-46. Strain: Sp. Cellulosa.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X54523 Genomic DNA. Translation: CAA38390.1.
3D structure databases
HSSP	HSSP built from PDB template 1EXG based on UniProtKB P07986.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. CBM35. Carbohydrate-Binding Module Family 35. GH62. Glycoside Hydrolase Family 62.
Enzyme and pathway databases
BRENDA	3.2.1.55. 329.
Family and domain databases
InterPro	IPR001919. CBD_bac. IPR012291. CBD_carb_bd. IPR018366. CBM2_CS. IPR005084. CBM_6. IPR005193. GH62_arabinosidase. [Graphical view]
Gene3D	G3DSA:2.60.40.290. CBD_carb_bd. 1 hit.
Pfam	PF00553. CBM_2. 1 hit. PF03422. CBM_6. 1 hit. PF03664. Glyco_hydro_62. 1 hit. [Graphical view]
SMART	SM00637. CBD_II. 1 hit. [Graphical view]
PROSITE	PS51173. CBM2. 1 hit. PS00561. CBM2_A. 1 hit. PS51175. CBM6. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNC_PSEFL

Accession

Primary (citable) accession number: P23031

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	June 16, 2009
This is version 64 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)