P23031 (XYNC_CELJU) Reviewed, UniProtKB/Swiss-Prot

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
Synonyms:	abf62A
Ordered Locus Names:	CJA_3281

Organism

Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa) [Complete proteome] [HAMAP]

Taxonomic identifier

498211 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio

Protein attributes

Sequence length	619 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.
Sequence caution	The sequence CAA38390.1 differs from that shown. Reason: Frameshift at positions 527 and 544.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Complete proteome 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 – 619	582	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
Experimental info
	Sequence conflict	556 – 590	35	NNNVE…VDPCN → MMFCFTMASSLKVYTCY in CAA38390. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23031 [UniParc]. Last modified April 20, 2010. Version 2. Checksum: 9CA48261A2D0FD0F	FASTA	619	66,440
	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 EAYISGPRFF RSWTATSLDG 550 560 570 580 590 600 PWTPLADTEA NPFAGNNNVE WSTGKWADGI SHGELIRSGH DEKMTVDPCN LEFLYQGASG 610 PGSTYNTIPY KLGLLRLKK

References

	« Hide 'large scale' referencesShow 'large scale' 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.
[2]	"Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus." DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E. J. Bacteriol. 190:5455-5463(2008) [PubMed: 18556790] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ueda107.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X54523 Genomic DNA. Translation: CAA38390.1. Frameshift. CP000934 Genomic DNA. Translation: ACE85320.1.
RefSeq	YP_001983735.1. NC_010995.1.
3D structure databases
ProteinModelPortal	P23031.
ModBase	Search...
Protein family/group databases
CAZy	CBM2. Carbohydrate-Binding Module Family 2. CBM35. Carbohydrate-Binding Module Family 35. GH62. Glycoside Hydrolase Family 62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6413842.
GenomeReviews	Gene locus CJA_3281 in contig CP000934_GR.
KEGG	cja:CJA_3281.
PATRIC	21329953. VBICelJap122165_3241.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	WYLITQW.
ProtClustDB	CLSK2544292.
Family and domain databases
InterPro	IPR008965. Carb-bd_dom. IPR012291. CBD_carb-bd_dom. IPR018366. CBM2_CS. IPR001919. Cellulose-bd_dom_fam2_bac. IPR005084. CMB_fam6. IPR008979. Galactose-bd-like. IPR005193. GH62_arabinosidase. IPR023296. Glyco_hydro_43_beta-prop. [Graphical view]
Gene3D	G3DSA:2.60.40.290. CBD_carb_bd. 1 hit. G3DSA:2.115.10.20. Glyco_hydro_43_beta-prop. 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]
SUPFAM	SSF49384. Cellul_bind. 1 hit. SSF49785. Gal_bind_like. 1 hit. SSF75005. Glyco_hydro_43_beta-prop. 1 hit.
PROSITE	PS51173. CBM2. 1 hit. PS00561. CBM2_A. 1 hit. PS51175. CBM6. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYNC_CELJU

Accession

Primary (citable) accession number: P23031
Secondary accession number(s): B3PEH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	April 20, 2010
Last modified:	January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program