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P13670

- CHB_VIBHA

UniProt

P13670 - CHB_VIBHA

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Protein

N,N'-diacetylchitobiase

Gene

chb

Organism
Vibrio harveyi (Beneckea harveyi)
Status
Reviewed - Annotation score: 4 out of 5- 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei537 – 5371Proton donorBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. chitin catabolic process Source: UniProtKB-UniPathway
  2. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate 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

  1. cell outer membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Add
BLAST
Chaini18 – 883866N,N'-diacetylchitobiasePRO_0000012019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi18 – 181N-palmitoyl cysteineCurated
Lipidationi18 – 181S-diacylglycerol cysteine1 PublicationPROSITE-ProRule annotation
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

Expressioni

Inductioni

By chitobiose.

Structurei

3D structure databases

ProteinModelPortaliP13670.
SMRiP13670. Positions 25-882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
2.60.40.320. 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.
IPR004867. CHB_HEX_C_dom.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF03173. CHB_HEX. 1 hit.
PF03174. CHB_HEX_C. 1 hit.
PF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PRINTSiPR00738. GLHYDRLASE20.
SMARTiSM01081. CHB_HEX. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05004 Genomic DNA. Translation: AAA88682.1 .
PIRi A36511.

3D structure databases

ProteinModelPortali P13670.
SMRi P13670. Positions 25-882.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00349 .

Family and domain databases

Gene3Di 2.60.40.290. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProi IPR025705. Beta_hexosaminidase_sua/sub.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR004866. CHB/HEX_N_dom.
IPR004867. CHB_HEX_C_dom.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF03173. CHB_HEX. 1 hit.
PF03174. CHB_HEX_C. 1 hit.
PF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view ]
PRINTSi PR00738. GLHYDRLASE20.
SMARTi SM01081. CHB_HEX. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "N,N'-diacetylchitobiase of Vibrio harveyi. Primary structure, processing, and evolutionary relationships."
    Soto-Gil R.W., Zysking J.W.
    J. Biol. Chem. 264:14778-14783(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL AT CYS-18.

Entry informationi

Entry nameiCHB_VIBHA
AccessioniPrimary (citable) accession number: P13670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: October 29, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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