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Protein

Chitinase A

Gene

chiA

Organism
Serratia marcescens
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei315Proton donorCurated1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17691.
BRENDAi3.2.1.14. 5690.
SABIO-RKP07254.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitinase A (EC:3.2.1.14)
Gene namesi
Name:chiA
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5423.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000001190824 – 563Chitinase AAdd BLAST540

Interactioni

Chemistry databases

BindingDBiP07254.

Structurei

Secondary structure

1563
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 43Combined sources7
Helixi50 – 53Combined sources4
Beta strandi54 – 56Combined sources3
Beta strandi58 – 67Combined sources10
Beta strandi69 – 71Combined sources3
Beta strandi75 – 81Combined sources7
Beta strandi84 – 90Combined sources7
Beta strandi93 – 102Combined sources10
Beta strandi106 – 116Combined sources11
Beta strandi119 – 122Combined sources4
Beta strandi126 – 131Combined sources6
Beta strandi156 – 165Combined sources10
Helixi166 – 169Combined sources4
Beta strandi170 – 172Combined sources3
Helixi176 – 178Combined sources3
Helixi181 – 183Combined sources3
Beta strandi185 – 192Combined sources8
Turni198 – 200Combined sources3
Helixi202 – 206Combined sources5
Helixi210 – 217Combined sources8
Turni218 – 220Combined sources3
Helixi231 – 235Combined sources5
Helixi251 – 262Combined sources12
Beta strandi267 – 273Combined sources7
Turni275 – 277Combined sources3
Helixi279 – 283Combined sources5
Helixi287 – 303Combined sources17
Beta strandi309 – 313Combined sources5
Helixi331 – 353Combined sources23
Beta strandi358 – 364Combined sources7
Helixi367 – 370Combined sources4
Helixi375 – 378Combined sources4
Helixi379 – 381Combined sources3
Beta strandi383 – 388Combined sources6
Beta strandi392 – 394Combined sources3
Beta strandi398 – 400Combined sources3
Helixi420 – 430Combined sources11
Helixi434 – 436Combined sources3
Beta strandi437 – 450Combined sources14
Helixi459 – 461Combined sources3
Beta strandi465 – 467Combined sources3
Beta strandi471 – 473Combined sources3
Beta strandi476 – 478Combined sources3
Helixi479 – 485Combined sources7
Beta strandi486 – 488Combined sources3
Beta strandi492 – 496Combined sources5
Turni497 – 500Combined sources4
Beta strandi501 – 506Combined sources6
Turni507 – 510Combined sources4
Beta strandi511 – 514Combined sources4
Helixi518 – 531Combined sources14
Beta strandi535 – 539Combined sources5
Helixi541 – 543Combined sources3
Helixi547 – 555Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CTNX-ray2.30A24-563[»]
1EHNX-ray1.90A24-563[»]
1EIBX-ray1.80A24-563[»]
1FFQX-ray1.90A24-563[»]
1FFRX-ray1.80A24-563[»]
1K9TX-ray1.80A24-563[»]
1NH6X-ray2.05A24-563[»]
1RD6X-ray2.60A1-563[»]
1X6LX-ray1.90A1-563[»]
1X6NX-ray2.00A1-563[»]
2WK2X-ray2.05A24-563[»]
2WLYX-ray2.40A24-563[»]
2WLZX-ray1.82A24-563[»]
2WM0X-ray1.90A24-563[»]
ProteinModelPortaliP07254.
SMRiP07254.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07254.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 563CatalyticAdd BLAST414

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR013540. ChitinaseA_N.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR022409. PKD/Chitinase_dom.
[Graphical view]
PfamiPF08329. ChitinaseA_N. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
SM00089. PKD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P07254-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKFNKPLLA LLIGSTLCSA AQAAAPGKPT IAWGNTKFAI VEVDQAATAY
60 70 80 90 100
NNLVKVKNAA DVSVSWNLWN GDAGTTAKIL LNGKEAWSGP STGSSGTANF
110 120 130 140 150
KVNKGGRYQM QVALCNADGC TASDATEIVV ADTDGSHLAP LKEPLLEKNK
160 170 180 190 200
PYKQNSGKVV GSYFVEWGVY GRNFTVDKIP AQNLTHLLYG FIPICGGNGI
210 220 230 240 250
NDSLKEIEGS FQALQRSCQG REDFKVSIHD PFAALQKAQK GVTAWDDPYK
260 270 280 290 300
GNFGQLMALK QAHPDLKILP SIGGWTLSDP FFFMGDKVKR DRFVGSVKEF
310 320 330 340 350
LQTWKFFDGV DIDWEFPGGK GANPNLGSPQ DGETYVLLMK ELRAMLDQLS
360 370 380 390 400
AETGRKYELT SAISAGKDKI DKVAYNVAQN SMDHIFLMSY DFYGPFDLKN
410 420 430 440 450
LGHQTALNAP AWKPDTAYTT VNGVNALLAQ GVKPGKVVVG TAMYGRGWTG
460 470 480 490 500
VNGYQNNIPF TGTATGPVKG TWKNGIVDYR QIAGQFMSGE WQYTYDATAE
510 520 530 540 550
APYVFKPSTG DLITFDDARS VQAKGKYVLD KQLGGLFSWE IDADNGDILN
560
SMNASLGNSA GVQ
Length:563
Mass (Da):60,979
Last modified:February 1, 1995 - v3
Checksum:i0696FEF6AF83AA35
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti52N → S in CAA85291 (PubMed:7851747).Curated1
Sequence conflicti73A → T in CAA85291 (PubMed:7851747).Curated1
Sequence conflicti76 – 77TA → GP in CAA27292 (PubMed:16453672).Curated2
Sequence conflicti79I → V in CAA85291 (PubMed:7851747).Curated1
Sequence conflicti121T → S in CAA85291 (PubMed:7851747).Curated1
Sequence conflicti139A → P in CAA27292 (PubMed:16453672).Curated1
Sequence conflicti226V → I in CAA27292 (PubMed:16453672).Curated1
Sequence conflicti395P → A (Ref. 1) Curated1
Sequence conflicti395P → A (PubMed:16453672).Curated1
Sequence conflicti395P → A (PubMed:7851747).Curated1
Sequence conflicti410 – 429PAWKP…NALLA → RPGSRHRLHHGERRQCAAG (Ref. 1) CuratedAdd BLAST20
Sequence conflicti410 – 429PAWKP…NALLA → RPGSRHRLHHGERRQCAAG (PubMed:16453672).CuratedAdd BLAST20
Sequence conflicti437V → I (PubMed:16453672).Curated1
Sequence conflicti437V → I (PubMed:7851747).Curated1
Sequence conflicti464 – 467ATGP → HRA in CAA27292 (PubMed:16453672).Curated4
Sequence conflicti473K → E (PubMed:16453672).Curated1
Sequence conflicti473K → E (PubMed:7851747).Curated1
Sequence conflicti484G → S in CAA27292 (PubMed:16453672).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01455 Genomic DNA. Translation: AAA26551.1.
X03657 Genomic DNA. Translation: CAA27292.1.
Z36294 Genomic DNA. Translation: CAA85291.1.
PIRiA25090.
S60651.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01455 Genomic DNA. Translation: AAA26551.1.
X03657 Genomic DNA. Translation: CAA27292.1.
Z36294 Genomic DNA. Translation: CAA85291.1.
PIRiA25090.
S60651.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CTNX-ray2.30A24-563[»]
1EHNX-ray1.90A24-563[»]
1EIBX-ray1.80A24-563[»]
1FFQX-ray1.90A24-563[»]
1FFRX-ray1.80A24-563[»]
1K9TX-ray1.80A24-563[»]
1NH6X-ray2.05A24-563[»]
1RD6X-ray2.60A1-563[»]
1X6LX-ray1.90A1-563[»]
1X6NX-ray2.00A1-563[»]
2WK2X-ray2.05A24-563[»]
2WLYX-ray2.40A24-563[»]
2WLZX-ray1.82A24-563[»]
2WM0X-ray1.90A24-563[»]
ProteinModelPortaliP07254.
SMRiP07254.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP07254.
ChEMBLiCHEMBL5423.

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17691.
BRENDAi3.2.1.14. 5690.
SABIO-RKP07254.

Miscellaneous databases

EvolutionaryTraceiP07254.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR013540. ChitinaseA_N.
IPR001223. Glyco_hydro18_cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR022409. PKD/Chitinase_dom.
[Graphical view]
PfamiPF08329. ChitinaseA_N. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SMARTiSM00636. Glyco_18. 1 hit.
SM00089. PKD. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS01095. CHITINASE_18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHIA_SERMA
AccessioniPrimary (citable) accession number: P07254
Secondary accession number(s): Q54275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.