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Protein

Alpha-L-arabinofuranosidase C

Gene

xynC

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

Functioni

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

Miscellaneous

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

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

Keywordsi

Molecular functionGlycosidase, Hydrolase

Enzyme and pathway databases

BioCyciCJAP498211:G1GB3-3271-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 lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio
Proteomesi
  • UP000001036 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Proteomic databases

PRIDEiP23031

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_3281

Structurei

3D structure databases

ProteinModelPortaliP23031
SMRiP23031
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

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
InterProiView protein in InterPro
IPR001919 CBD2
IPR008965 CBM2/CBM3_carb-bd_dom_sf
IPR012291 CBM2_carb-bd_dom_sf
IPR018366 CBM2_CS
IPR005084 CMB_fam6
IPR008979 Galactose-bd-like_sf
IPR005193 GH62_arabinosidase
IPR023296 Glyco_hydro_beta-prop_sf
PANTHERiPTHR40631 PTHR40631, 1 hit
PfamiView protein in Pfam
PF00553 CBM_2, 1 hit
PF03422 CBM_6, 1 hit
PF03664 Glyco_hydro_62, 1 hit
SMARTiView protein in SMART
SM00637 CBD_II, 1 hit
SUPFAMiSSF49384 SSF49384, 1 hit
SSF49785 SSF49785, 1 hit
SSF75005 SSF75005, 1 hit
PROSITEiView protein in PROSITE
PS51173 CBM2, 1 hit
PS00561 CBM2_A, 1 hit
PS51175 CBM6, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiXYNC_CELJU
AccessioniPrimary (citable) accession number: P23031
Secondary accession number(s): B3PEH9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 20, 2010
Last modified: May 23, 2018
This is version 114 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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