[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Koo J.C., Lim C.O., Choi Y.J., Kim C.Y., Bahk J.D., Lee S.Y., Cho M.J.; Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 990 / QMB1466; PubMed=16453672 [NCBI, ExPASy, EBI, Israel, Japan] Jones J.D.G., Grady K.L., Suslow T.V., Bedbrook J.R.; "Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens."; EMBO J. 5:467-473(1986).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-31. STRAIN=BJL200; DOI=10.1016/0378-1097(94)00462-5; PubMed=7851747 [NCBI, ExPASy, EBI, Israel, Japan] Brurberg M.B., Eijsink V.G.H., Nes I.F.; "Characterization of a chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product."; FEMS Microbiol. Lett. 124:399-404(1994).
[4]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SEQUENCE REVISION. DOI=10.1016/S0969-2126(94)00119-7; PubMed=7704527 [NCBI, ExPASy, EBI, Israel, Japan] Perrakis A., Tews I., Dauter Z., Oppenheim A.B., Chet I., Wilson K.S., Vorgias C.E.; "Crystal structure of a bacterial chitinase at 2.3-A resolution."; Structure 2:1169-1180(1994).

Comments

CATALYTIC ACTIVITY: Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L01455; AAA26551.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03657; CAA27292.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z36294; CAA85291.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25090; A25090.
S60651; S60651.

3D structure databases

PDB

1CTN; X-ray; 2.30 A; A=24-563.	[ExPASy / RCSB / EBI]
1EHN; X-ray; 1.90 A; A=24-563.	[ExPASy / RCSB / EBI]
1EIB; X-ray; 1.80 A; A=24-563.	[ExPASy / RCSB / EBI]
1FFQ; X-ray; 1.90 A; A=24-563.	[ExPASy / RCSB / EBI]
1FFR; X-ray; 1.80 A; A=24-563.	[ExPASy / RCSB / EBI]
1K9T; X-ray; 1.80 A; A=24-563.	[ExPASy / RCSB / EBI]
1NH6; X-ray; 2.05 A; A=24-563.	[ExPASy / RCSB / EBI]
1RD6; X-ray; 2.60 A; A=1-563.	[ExPASy / RCSB / EBI]
1X6L; X-ray; 1.90 A; A=1-563.	[ExPASy / RCSB / EBI]
1X6N; X-ray; 2.00 A; A=1-563.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1CTN; -.
1EHN; -.
1EIB; -.
1FFQ; -.
1FFR; -.
1K9T; -.
1NH6; -.
1RD6; -.
1X6L; -.
1X6N; -.

ModBase

P07254.

Family and domain databases

InterPro

IPR011583; Chitinase_II.
IPR013540; ChitinaseA_N.
IPR001223; Glyco_hydro18cat.
IPR001579; Glyco_hydro_18_chit_AS.
IPR013781; Glyco_hydro_sub_cat.
IPR013783; Ig-like_fold.
IPR000601; PKD.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
G3DSA:2.60.40.10; Ig-like_fold; 1.

Pfam

PF08329; ChitinaseA_N; 1.
PF00704; Glyco_hydro_18; 1.
Pfam graphical view of domain structure.

ProDom

PD000471; Chitinase_II; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00636; Glyco_18; 1.
SM00089; PKD; 1.
SMART graphical view of domain structure.

PROSITE

PS01095; CHITINASE_18; 1.

Other

P07254; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Carbohydrate metabolism; Chitin degradation; Direct protein sequencing; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 563`	`540`	`Chitinase A.`	`PRO_0000011908`
`REGION`	`150 563`	`414`	`Catalytic.`
`ACT_SITE`	`315 315`		`Proton donor (Probable).`
`CONFLICT`	`52 52`		`N -> S (in Ref. 3; CAA85291).`
`CONFLICT`	`73 73`		`A -> T (in Ref. 3; CAA85291).`
`CONFLICT`	`76 77`		`TA -> GP (in Ref. 2; CAA27292).`
`CONFLICT`	`79 79`		`I -> V (in Ref. 3; CAA85291).`
`CONFLICT`	`121 121`		`T -> S (in Ref. 3; CAA85291).`
`CONFLICT`	`139 139`		`A -> P (in Ref. 2; CAA27292).`
`CONFLICT`	`226 226`		`V -> I (in Ref. 2; CAA27292).`
`CONFLICT`	`395 395`		`P -> A (in Ref. 1, 2 and 3).`
`CONFLICT`	`410 429`		`PAWKPDTAYTTVNGVNALLA -> RPGSRHRLHHGERRQCAAG (in Ref. 1 and 2).`
`CONFLICT`	`437 437`		`V -> I (in Ref. 2 and 3).`
`CONFLICT`	`464 467`		`ATGP -> HRA (in Ref. 2; CAA27292).`
`CONFLICT`	`473 473`		`K -> E (in Ref. 2 and 3).`
`CONFLICT`	`484 484`		`G -> S (in Ref. 2; CAA27292).`
`STRAND`	`37 43`	`7`
`HELIX`	`50 53`	`4`
`STRAND`	`54 56`	`3`
`STRAND`	`58 67`	`10`
`STRAND`	`75 81`	`7`
`STRAND`	`84 90`	`7`
`STRAND`	`93 102`	`10`
`STRAND`	`106 116`	`11`
`STRAND`	`119 122`	`4`
`STRAND`	`126 131`	`6`
`STRAND`	`159 165`	`7`
`HELIX`	`166 169`	`4`
`STRAND`	`170 172`	`3`
`HELIX`	`176 178`	`3`
`HELIX`	`181 183`	`3`
`STRAND`	`185 192`	`8`
`TURN`	`198 200`	`3`
`HELIX`	`202 206`	`5`
`HELIX`	`210 217`	`8`
`TURN`	`218 220`	`3`
`HELIX`	`231 235`	`5`
`HELIX`	`251 262`	`12`
`STRAND`	`267 277`	`11`
`HELIX`	`279 283`	`5`
`HELIX`	`287 303`	`17`
`STRAND`	`309 315`	`7`
`HELIX`	`331 353`	`23`
`STRAND`	`358 364`	`7`
`HELIX`	`367 370`	`4`
`HELIX`	`375 378`	`4`
`TURN`	`379 381`	`3`
`STRAND`	`383 388`	`6`
`HELIX`	`420 430`	`11`
`HELIX`	`434 436`	`3`
`STRAND`	`437 449`	`13`
`HELIX`	`459 461`	`3`
`STRAND`	`465 467`	`3`
`STRAND`	`471 473`	`3`
`STRAND`	`476 478`	`3`
`HELIX`	`479 485`	`7`
`STRAND`	`486 488`	`3`
`STRAND`	`492 496`	`5`
`TURN`	`497 500`	`4`
`STRAND`	`501 506`	`6`
`TURN`	`507 510`	`4`
`STRAND`	`511 514`	`4`
`HELIX`	`518 531`	`14`
`STRAND`	`535 539`	`5`
`HELIX`	`541 543`	`3`
`HELIX`	`547 555`	`9`

Sequence information

Length: 563 AA [This is the length of the unprocessed precursor]

Molecular weight: 60979 Da [This is the MW of the unprocessed precursor]

CRC64: 0696FEF6AF83AA35 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRKFNKPLLA LLIGSTLCSA AQAAAPGKPT IAWGNTKFAI VEVDQAATAY NNLVKVKNAA 

        70         80         90        100        110        120 
DVSVSWNLWN GDAGTTAKIL LNGKEAWSGP STGSSGTANF KVNKGGRYQM QVALCNADGC 

       130        140        150        160        170        180 
TASDATEIVV ADTDGSHLAP LKEPLLEKNK PYKQNSGKVV GSYFVEWGVY GRNFTVDKIP 

       190        200        210        220        230        240 
AQNLTHLLYG FIPICGGNGI NDSLKEIEGS FQALQRSCQG REDFKVSIHD PFAALQKAQK 

       250        260        270        280        290        300 
GVTAWDDPYK GNFGQLMALK QAHPDLKILP SIGGWTLSDP FFFMGDKVKR DRFVGSVKEF 

       310        320        330        340        350        360 
LQTWKFFDGV DIDWEFPGGK GANPNLGSPQ DGETYVLLMK ELRAMLDQLS AETGRKYELT 

       370        380        390        400        410        420 
SAISAGKDKI DKVAYNVAQN SMDHIFLMSY DFYGPFDLKN LGHQTALNAP AWKPDTAYTT 

       430        440        450        460        470        480 
VNGVNALLAQ GVKPGKVVVG TAMYGRGWTG VNGYQNNIPF TGTATGPVKG TWKNGIVDYR 

       490        500        510        520        530        540 
QIAGQFMSGE WQYTYDATAE APYVFKPSTG DLITFDDARS VQAKGKYVLD KQLGGLFSWE 

       550        560 
IDADNGDILN SMNASLGNSA GVQ

P07254 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools