Reviewed, UniProtKB/Swiss-Prot P96156 (CHID_VIBFU)

Names and origin

Protein names

Recommended name:
    Chitodextrinase
    EC=3.2.1.14

Gene names

Name:

endo I

Organism

Vibrio furnissii

Taxonomic identifier

29494 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	1046 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes chitin oligosaccharides; (GlcNAc)4 to (GlcNAc)2 and (GlcNAc)5,6 to (GlcNAc)2 and (GlcNAc)3. Inactive towards chitin, glucosamine oligosaccharides, glycoproteins and glycopeptides containing (GlcNAc)2.
Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Enzyme regulation	Inhibited by (GlcNAc)4, (GlcNAc)5, (GlcNAc)6, and PNP-(GlcNAc)3.
Pathway	Glycan degradation; chitin degradation.
Subcellular location	Periplasm Probable.
Induction	By (GlcNAc)2.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5-7.0. Temperature dependence: Optimum temperature is 35-37 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Cellular component	Periplasm
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro chitinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	Ref.1
	Chain	31 – 1046	1016	Chitodextrinase		PRO_0000011959

Sequences

	Sequence		Length	Mass (Da)
	P96156-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 40680F1642D55A1F	FASTA	1,046	112,380
	10 20 30 40 50 60 MRLHRAKVSK SVFTLSTLTA SCLMAFNSYA AVDCSALAEW QSDTIYTGGD QVQYNGSAYQ 70 80 90 100 110 120 ANYWTQNNDP EQFSGDYAQW KLLDACTTDG GDDNQAPNAT LTSPSASDVL TTGDVVTLAA 130 140 150 160 170 180 SASDNDGTIA RVDFLVDGVV VAQASSAPYS ATWTAVAGTH QISAIAYDDK ALASTASQVS 190 200 210 220 230 240 VSVTDSTQPG NEAPTVDITL SASQVDVGDV VTLTANAADA DGSVDKVDFY VAGSLVGTVA 250 260 270 280 290 300 STPYTLDYTT TRSGRWLCLR ARLITSARQR IRPRRRLTVA AGPWSVPVVL MVCIKPKGQC 310 320 330 340 350 360 AVLYGVREDG REKMGADHPR RVIGYFTSWR AGDDDQTAYL VKDIPWEQLT HINYAFVSIG 370 380 390 400 410 420 SDGKVNVGDV NDANNAAVGK EWDGVEIDPT LGFKGHFGAL ATYKQKYGVK TLISIGGWAE 430 440 450 460 470 480 TGGHFDNDGN RVADGGFYTM TTNADGSINQ QGIETFADSA VEMMRKYRFD GLDIDLRISN 490 500 510 520 530 540 IDGGTGNPDD TAFSESRRAY LMNSYHELMR VLREKLDVAS AQDGVHYMLT IAAPSSAYLL 550 560 570 580 590 600 RGMETMAVTQ YLDYVNIMSY DLHGAWNDHV GHNAALYDTG KDSELAQWNV YGTAQYGGIG 610 620 630 640 650 660 YLNTDWAFHY FRGSMPAGRI NIGVPYYTRG WQGVTGGDNG LWGARLAKSK RVSNRYGEGE 670 680 690 700 710 720 KNNCGYGATG LDNMWHDVNA AGDEMGAGSN PMWHAKNLEH GIWGSYLAVY GLDPTTAPLV 730 740 750 760 770 780 GTYARNYDSV AIAPWLWNAE KKVFLSTEDK QSIDVKADYV IDKEIGGIMF WELAGDYNCY 790 800 810 820 830 840 VLDANGQRTS IDSTEQACES GQGEYHMGNT MTKAIYDKFK AATPYGNTVA TGAVPSETVD 850 860 870 880 890 900 IAVSIGGFKV GDQNYPINPK VTFTNNTGVD IPGGTAFQFD IPVSAPDNAK DQSGGGLSVI 910 920 930 940 950 960 ASGHTRADNI GGLDGTMHRV AFSLPAWKTL PAGDTYELDM VYYLPISGPA NYSVNINGVD 970 980 990 1000 1010 1020 YAFKFEQPDL PLADLSSGNG GGTGGGDTGG GTTEPGDVVE WVPGSTQVSD GTTVTYNGKC 1030 1040 FVAQNSPGVW ESPTQTNWFW EEVTCP

References

[1]

"The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation, and characterization of a periplasmic chitodextrinase." Keyhani N.O., Roseman S. J. Biol. Chem. 271:33414-33424(1996) [PubMed: 8969204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-51.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U41418 Genomic DNA. Translation: AAC44673.1.
PIR	T30199.
3D structure databases
SMR	P96156. Positions 38-87, 231-777, 319-866.
ModBase	Search...
Protein family/group databases
CAZy	CBM5. Carbohydrate-Binding Module Family 5. GH18. Glycoside Hydrolase Family 18.
Enzyme and pathway databases
BRENDA	3.2.1.14. 258010.
Family and domain databases
InterPro	IPR003610. Carb-bd_dom_fam5/12. IPR009470. Chi_C. IPR011583. Chitinase_II. IPR001223. Glyco_hydro18cat. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF02839. CBM_5_12. 1 hit. PF06483. ChiC. 1 hit. PF00704. Glyco_hydro_18. 1 hit. [Graphical view]
SMART	SM00495. ChtBD3. 2 hits. SM00636. Glyco_18. 1 hit. [Graphical view]
PROSITE	PS01095. CHITINASE_18. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CHID_VIBFU

Accession

Primary (citable) accession number: P96156

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	May 1, 1997
Last modified:	January 19, 2010
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)