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P23031

- XYNC_CELJU

UniProt

P23031 - XYNC_CELJU

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Protein

Alpha-L-arabinofuranosidase C

Gene

xynC

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Xylanase C contributes to hydrolyse hemicellulose, the major component of plant cell-walls.

Catalytic activityi

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

Pathwayi

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC
  2. polysaccharide binding Source: InterPro

GO - Biological processi

  1. L-arabinose metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciCJAP498211:GHIT-3270-MONOMER.
UniPathwayiUPA00697.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
CBM35. Carbohydrate-Binding Module Family 35.
GH62. Glycoside Hydrolase Family 62.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-L-arabinofuranosidase C (EC:3.2.1.55)
Alternative name(s):
Xylanase C
Gene namesi
Name:xynC
Synonyms:abf62A
Ordered Locus Names:CJA_3281
OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri498211 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
ProteomesiUP000001036: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 619582Alpha-L-arabinofuranosidase CPRO_0000008033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 133By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_3281.

Structurei

3D structure databases

ProteinModelPortaliP23031.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 13699CBM2Add
BLAST
Domaini163 – 289127CBM6PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi135 – 16228Ser-rich (linker)Add
BLAST
Compositional biasi300 – 32021Ser-rich (linker)Add
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 62 family.Curated
Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

OMAiWYLITQW.
OrthoDBiEOG6ZH2FF.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
2.60.120.260. 1 hit.
2.60.40.290. 1 hit.
InterProiIPR008965. 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_beta-prop.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF03422. CBM_6. 1 hit.
PF03664. Glyco_hydro_62. 1 hit.
[Graphical view]
SMARTiSM00637. CBD_II. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51175. CBM6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23031 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MINHNKTPNI LAKVFKRTCG LVSTGAALAI LSQAASAACT YTIDSEWSTG
60 70 80 90 100
FTANITLKND TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW
110 120 130 140 150
NGSIAPGQSI SFGLQGEKNG STAERPTVTG AACNSATTSS VASSSSTPTT
160 170 180 190 200
SSSSASSVAS ALLLQEAQAG FCRVDGTIDN NHTGFTGSGF ANTNNAQGAA
210 220 230 240 250
VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN YTVSLPTTGA
260 270 280 290 300
WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS
310 320 330 340 350
VSSSSSVQSS SSSSSTPSQT CELKAPLRWT STGPLISPKN PGWISIKDPS
360 370 380 390 400
IVKYNDTYHV YATYYDTAYR SMYTSFTDWN TAQQAPHISM NGSRVGNTVA
410 420 430 440 450
PQVFYFRPHN KWYLITQWAG AYATTDDIRN PNWSAKQKLL QGEPNGALDF
460 470 480 490 500
WVICNDTHCY LYFSRDDGVL YVSKTTLANF PNFSGYSIVM EDHRGNGNSY
510 520 530 540 550
LFEAANVYKL DGQNRYLLMV EAYISGPRFF RSWTATSLDG PWTPLADTEA
560 570 580 590 600
NPFAGNNNVE WSTGKWADGI SHGELIRSGH DEKMTVDPCN LEFLYQGASG
610
PGSTYNTIPY KLGLLRLKK
Length:619
Mass (Da):66,440
Last modified:April 20, 2010 - v2
Checksum:i9CA48261A2D0FD0F
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti556 – 59035NNNVE…VDPCN → MMFCFTMASSLKVYTCY in CAA38390. (PubMed:2125205)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54523 Genomic DNA. Translation: CAA38390.1. Frameshift.
CP000934 Genomic DNA. Translation: ACE85320.1.
RefSeqiYP_001983735.1. NC_010995.1.

Genome annotation databases

EnsemblBacteriaiACE85320; ACE85320; CJA_3281.
GeneIDi6413842.
KEGGicja:CJA_3281.
PATRICi21329953. VBICelJap122165_3241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X54523 Genomic DNA. Translation: CAA38390.1 . Frameshift.
CP000934 Genomic DNA. Translation: ACE85320.1 .
RefSeqi YP_001983735.1. NC_010995.1.

3D structure databases

ProteinModelPortali P23031.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 498211.CJA_3281.

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
CBM35. Carbohydrate-Binding Module Family 35.
GH62. Glycoside Hydrolase Family 62.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACE85320 ; ACE85320 ; CJA_3281 .
GeneIDi 6413842.
KEGGi cja:CJA_3281.
PATRICi 21329953. VBICelJap122165_3241.

Phylogenomic databases

OMAi WYLITQW.
OrthoDBi EOG6ZH2FF.

Enzyme and pathway databases

UniPathwayi UPA00697 .
BioCyci CJAP498211:GHIT-3270-MONOMER.

Family and domain databases

Gene3Di 2.115.10.20. 1 hit.
2.60.120.260. 1 hit.
2.60.40.290. 1 hit.
InterProi 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_beta-prop.
[Graphical view ]
Pfami PF00553. CBM_2. 1 hit.
PF03422. CBM_6. 1 hit.
PF03664. Glyco_hydro_62. 1 hit.
[Graphical view ]
SMARTi SM00637. CBD_II. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51175. CBM6. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ueda107.

Entry informationi

Entry nameiXYNC_CELJU
AccessioniPrimary (citable) accession number: P23031
Secondary accession number(s): B3PEH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 20, 2010
Last modified: October 29, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Acts only on high MW substrates, in which arabinose is linked to a polymeric backbone.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3