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Protein

N,N'-diacetylchitobiase

Gene

chb

Organism
Vibrio harveyi (Beneckea harveyi)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Hydrolysis of terminal, non-reducing N-acetyl-beta-D-glucosamine residues in chitobiose and higher analogs, and in glycoproteins.

Catalytic activityi

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

Pathwayi: chitin degradation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei537Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00349

Protein family/group databases

CAZyiGH20 Glycoside Hydrolase Family 20

Names & Taxonomyi

Protein namesi
Recommended name:
N,N'-diacetylchitobiase (EC:3.2.1.52)
Short name:
Chitobiase
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
Gene namesi
Name:chb
OrganismiVibrio harveyi (Beneckea harveyi)
Taxonomic identifieri669 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Add BLAST17
ChainiPRO_000001201918 – 883N,N'-diacetylchitobiaseAdd BLAST866

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi18N-palmitoyl cysteineCurated1
Lipidationi18S-diacylglycerol cysteinePROSITE-ProRule annotation1 Publication1
Disulfide bondi54 ↔ 64By similarity
Disulfide bondi394 ↔ 402By similarity
Disulfide bondi502 ↔ 577By similarity

Post-translational modificationi

This protein is probably a lipoprotein, its processing is inhibited by globomycin.

Keywords - PTMi

Disulfide bond, Lipoprotein, Palmitate

Proteomic databases

PRIDEiP13670

Expressioni

Inductioni

By chitobiose.

Structurei

3D structure databases

ProteinModelPortaliP13670
SMRiP13670
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105E2D Bacteria
COG3525 LUCA

Family and domain databases

CDDicd02847 E_set_Chitobiase_C, 1 hit
Gene3Di2.60.40.10, 1 hit
2.60.40.290, 1 hit
3.30.379.10, 1 hit
InterProiView protein in InterPro
IPR025705 Beta_hexosaminidase_sua/sub
IPR008965 CBM2/CBM3_carb-bd_dom_sf
IPR012291 CBM2_carb-bd_dom_sf
IPR004866 CHB/HEX_N_dom
IPR004867 CHB_C_dom
IPR015883 Glyco_hydro_20_cat
IPR017853 Glycoside_hydrolase_SF
IPR029018 Hex-like_dom2
IPR015882 HEX_bac_N
IPR013783 Ig-like_fold
IPR014756 Ig_E-set
PfamiView protein in Pfam
PF03173 CHB_HEX, 1 hit
PF03174 CHB_HEX_C, 1 hit
PF00728 Glyco_hydro_20, 1 hit
PF02838 Glyco_hydro_20b, 1 hit
PRINTSiPR00738 GLHYDRLASE20
SMARTiView protein in SMART
SM01081 CHB_HEX, 1 hit
SUPFAMiSSF49384 SSF49384, 1 hit
SSF51445 SSF51445, 1 hit
SSF55545 SSF55545, 1 hit
SSF81296 SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS51257 PROKAR_LIPOPROTEIN, 1 hit

Sequencei

Sequence statusi: Complete.

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

P13670-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKHSLIAAS VITTLAGCSS LQSSEQQVVN SLADNLDIQY EVLTNHGANE
60 70 80 90 100
GLACQDMGAE WASCNKVNMT LVNQGEAVDS KDWAIYFHSI RLILDVDNEQ
110 120 130 140 150
FKISRVTGDL HKLEPTDKFD GFAAGEEVVL PLVGEYWQLF ETDFMPGAFV
160 170 180 190 200
SAPNAEPKMI ASLNTEDVAS FVTGLEGNNL KRTPDDNNVF ANAVSRFEKN
210 220 230 240 250
EDLATQDVST TLLPTPMHVE AGKGKVDIAD GIALPKDAFD ATQFAAIQDR
260 270 280 290 300
AEVVGVDVRG DLPVSITVVP ADFTGELAKS GAYEMSIKGD GIVIKAFDQA
310 320 330 340 350
GAFYAVQSIF GLVDSQNADS LPQLSIKDAP RFDYRGVMVD VARNFHSKDA
360 370 380 390 400
ILATLDQMAA YKMNKLHLHL TDDEGWRLEI PGLPELTEVG ANRCFDTQEK
410 420 430 440 450
SCLLPQLGSG PTTDNFGSGY FSKADYVEIL KYAKARNIEV IPEIDMPAHA
460 470 480 490 500
RAAVVSMEAR YDRLMEEGKE AEANEYRLMD PQDTSNVTTV QFYNKQSFIN
510 520 530 540 550
PCMESSTRFV DKVISEVAAM HQEAGAPLTT WHFGGDEAKN IKLGAGFQDV
560 570 580 590 600
NAEDKVSWKG TIDLSKQDKP FAQSPQCQTL ITDGTVSDFA HLPSHFAEEV
610 620 630 640 650
SKIVAEKGIP NFQAWQDGLK YSDGEKAFAT ENTRVNFWDV LYWGGTSSVY
660 670 680 690 700
EWSKKGYDVI VSNPDYVYMD MPYEVDPKER GYYWATRATD TRKMFGFAPE
710 720 730 740 750
NMPQNAETSV DRDGNGFTGK GEIEAKPFYG LSAQLWSETV RNDEQYEYMV
760 770 780 790 800
FPRVLAAAQR AWHRADWEND YKVGVEYSQN SNLVDKASLN QDYNRFANVL
810 820 830 840 850
GQRELAKLEK SGIDYRLPVP GAKVEDGKLA MNVQFPGVTL QYSLDGENWL
860 870 880
TYADNARPNV TGEVFIRSVS ATGEKVSRIT SVK
Length:883
Mass (Da):97,771
Last modified:January 1, 1990 - v1
Checksum:i8ED14598B1FEEBCE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05004 Genomic DNA Translation: AAA88682.1
PIRiA36511

Similar proteinsi

Entry informationi

Entry nameiCHB_VIBHA
AccessioniPrimary (citable) accession number: P13670
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 23, 2018
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

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