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Protein

Alpha-L-arabinofuranosidase C

Gene

xynC

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: 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: hemicellulose degradation

This protein is involved in the pathway hemicellulose degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway hemicellulose degradation and in Glycan metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

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 lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
Proteomesi
  • UP000001036 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 371 PublicationAdd BLAST37
ChainiPRO_000000803338 – 619Alpha-L-arabinofuranosidase CAdd BLAST582

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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)DescriptionActionsGraphical viewLength
Domaini38 – 136CBM2PROSITE-ProRule annotationAdd BLAST99
Domaini163 – 289CBM6PROSITE-ProRule annotationAdd BLAST127

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi135 – 162Ser-rich (linker)Add BLAST28
Compositional biasi300 – 320Ser-rich (linker)Add BLAST21

Sequence similaritiesi

Belongs to the glycosyl hydrolase 62 family.Curated
Contains 1 CBM2 (carbohydrate binding type-2) domain.PROSITE-ProRule annotation
Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108EUP. Bacteria.
ENOG410XNWA. LUCA.
OMAiWYLITQW.
OrthoDBiPOG091H0CR4.

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.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
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

        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 differs from that shown. Reason: Frameshift at positions 527 and 544.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti556 – 590NNNVE…VDPCN → MMFCFTMASSLKVYTCY in CAA38390 (PubMed:2125205).CuratedAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54523 Genomic DNA. Translation: CAA38390.1. Frameshift.
CP000934 Genomic DNA. Translation: ACE85320.1.
RefSeqiWP_012488857.1. NC_010995.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54523 Genomic DNA. Translation: CAA38390.1. Frameshift.
CP000934 Genomic DNA. Translation: ACE85320.1.
RefSeqiWP_012488857.1. NC_010995.1.

3D structure databases

ProteinModelPortaliP23031.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi498211.CJA_3281.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4108EUP. Bacteria.
ENOG410XNWA. LUCA.
OMAiWYLITQW.
OrthoDBiPOG091H0CR4.

Enzyme and pathway databases

UniPathwayiUPA00697.

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.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 104 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.