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Protein

Putative beta-hexosaminidase

Gene
N/A
Organism
Pinctada margaritifera (Black-lipped pearl oyster)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.By similarity

Pathwayi

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC
  2. polysaccharide binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. chitin catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

UniPathwayiUPA00349.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative beta-hexosaminidaseBy similarity (EC:3.2.1.52By similarity)
Alternative name(s):
Beta-N-acetylhexosaminidaseBy similarity
ChitobiaseBy similarity
N-acetyl-beta-glucosaminidaseBy similarity
OrganismiPinctada margaritifera (Black-lipped pearl oyster)
Taxonomic identifieri102329 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaPteriomorphiaPterioidaPterioideaPteriidaePinctada

Subcellular locationi

  1. Secreted 1 Publication

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 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 11351112Putative beta-hexosaminidaseSequence AnalysisPRO_0000418019Add
BLAST

Expressioni

Tissue specificityi

Prismatic layer of shell (at protein level). Expressed primarily in the mantle with highest level in the mantle edge and lower level in the mantle pallium.1 Publication

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi937 – 100468Pro-richSequence AnalysisAdd
BLAST
Compositional biasi1006 – 1133128Gln-richSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Sequence Analysis

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR004866. CHB/HEX_N_dom.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03173. CHB_HEX. 1 hit.
PF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

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

H2A0L6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWVKSGVGI LGILLTICHA VTSQGHILDI TDSLKITFKT LSNFGPRAQS
60 70 80 90 100
IQNVTIENVG IKDIPDSGWR CYFCHDQLLF PGTFNLARNQ YFLRPILDNY
110 120 130 140 150
VVLSDGFLLE FIKGCMYRIT PIPRNAPIKT RDKREFTLLA EQFSVSKYDS
160 170 180 190 200
FPKWYCETIS GGNTEVGIIR NTENLKYVED FDSSYNWFRI PHDFRSVPLQ
210 220 230 240 250
PQDRFSANHK ASSVDECKYK VIPTPVKASV SKVQRNFGTT VYYGTTDTSI
260 270 280 290 300
RGREKLFKVA EQLALKHNLG LVEITPGLTV NNGISLVVTG NYVERNIPSP
310 320 330 340 350
DEAYSLTVTA DLISIEAPAL PGLINGIETI HSLSAWDMAL PYGGIKDFPR
360 370 380 390 400
FPFRGIFLDI ASNFPGYNYI KKFLTVMAQY KLNKLVLPMY NNEGFRLQLN
410 420 430 440 450
DSPRYEFQAL HMIGGKRCHD LKEEKCLFSQ LGSGPDSSGG YLTKAQMTDL
460 470 480 490 500
IKTADLLNIE IIMSMNIGES ARGAIVPLKQ SPHSRLLYDP DDTDFVDRFY
510 520 530 540 550
PQKDTSMNPC REETTYFYDH MLKQLKDIYN AASVPLKTIM IGSKVNFDQV
560 570 580 590 600
LNSKYCYASN LNSTQRLMAR GNLERNINGF KLNFTKRLVK TAHDNGIKEV
610 620 630 640 650
MAIDDVFTTE FDAEGNTPNT VYDTKNSDNS TRFNATVTAV HSRYDTVRDE
660 670 680 690 700
RLWKRGDRFA ELGYKVILSP PILDFNYAVE PDPDRPGDYD SVIRNISFSK
710 720 730 740 750
LFRFVPDSRC CNIPNAIQHD CALESDCTTA GAKDSYIGTL GKLDTRKLRS
760 770 780 790 800
LKDWNELLFP RLLIFAERSW HKSSWEDSFG PHRASVNNIT RQLITNYTVP
810 820 830 840 850
NWNDINNEES KVLGCISRKE KLRLMHEDGL KPYVEPPGAR LLGGNTMRIA
860 870 880 890 900
ASTTEDSFWV QASVNGNPWT DNVKILDVNP TDSVRLRTVH PAKAELRSKE
910 920 930 940 950
VKLNLTSLPT PRERFRKIAQ DALSRRIGID IQRARMPPMP VNPAYRPPVP
960 970 980 990 1000
LPSFDPADDR APDLAAIAAA HPPPLPPGMP SHMMPNMPPP FPPRPPFGPP
1010 1020 1030 1040 1050
MLPPGQMRAL GQQAGQALRG QGTALGPQTG QQPMPAQPRG PLTGQAAGTG
1060 1070 1080 1090 1100
VAGQTGQQPS TAGQGTQQGL PGQQRGGVLP GQWPFFPGMP AAQFPPMFNP
1110 1120 1130
QMQRALQMRG QGQIPQRTQG AAAGAGQSRI PQQAG
Length:1,135
Mass (Da):126,661
Last modified:March 21, 2012 - v1
Checksum:i208E25A2E93AA61E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE610383 mRNA. Translation: CCE46157.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HE610383 mRNA. Translation: CCE46157.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00349.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR004866. CHB/HEX_N_dom.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF03173. CHB_HEX. 1 hit.
PF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF55545. SSF55545. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization."
    Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F., Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.
    BMC Genomics 11:613-613(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION.
    Tissue: Mantle.
  2. "Different secretory repertoires control the biomineralization processes of prism and nacre deposition of the pearl oyster shell."
    Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C., Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.
    Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 259-266, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Shell.

Entry informationi

Entry nameiHEX_PINMG
AccessioniPrimary (citable) accession number: H2A0L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2012
Last sequence update: March 21, 2012
Last modified: January 7, 2015
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

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

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 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.