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P23031

- XYNC_CELJU

UniProt

P23031 - XYNC_CELJU

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Protein
Alpha-L-arabinofuranosidase C
Gene
xynC, abf62A, CJA_3281
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
Complete GO annotation...

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-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 Publication
Add
BLAST
Chaini38 – 619582Alpha-L-arabinofuranosidase C
PRO_0000008033Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_3281.

Structurei

3D structure databases

ProteinModelPortaliP23031.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 13699CBM2
Add
BLAST
Domaini163 – 289127CBM6
Add
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

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.

P23031-1 [UniParc]FASTAAdd to Basket

« Hide

MINHNKTPNI LAKVFKRTCG LVSTGAALAI LSQAASAACT YTIDSEWSTG    50
FTANITLKND TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW 100
NGSIAPGQSI SFGLQGEKNG STAERPTVTG AACNSATTSS VASSSSTPTT 150
SSSSASSVAS ALLLQEAQAG FCRVDGTIDN NHTGFTGSGF ANTNNAQGAA 200
VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN YTVSLPTTGA 250
WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS 300
VSSSSSVQSS SSSSSTPSQT CELKAPLRWT STGPLISPKN PGWISIKDPS 350
IVKYNDTYHV YATYYDTAYR SMYTSFTDWN TAQQAPHISM NGSRVGNTVA 400
PQVFYFRPHN KWYLITQWAG AYATTDDIRN PNWSAKQKLL QGEPNGALDF 450
WVICNDTHCY LYFSRDDGVL YVSKTTLANF PNFSGYSIVM EDHRGNGNSY 500
LFEAANVYKL DGQNRYLLMV EAYISGPRFF RSWTATSLDG PWTPLADTEA 550
NPFAGNNNVE WSTGKWADGI SHGELIRSGH DEKMTVDPCN LEFLYQGASG 600
PGSTYNTIPY KLGLLRLKK 619
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti556 – 59035NNNVE…VDPCN → MMFCFTMASSLKVYTCY in CAA38390. 1 Publication
Add
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...

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: May 14, 2014
This is version 90 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

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

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