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P07254

- CHIA_SERMA

UniProt

P07254 - CHIA_SERMA

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Protein

Chitinase A

Gene

chiA

Organism
Serratia marcescens
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei315 – 3151Proton donorCurated

GO - Molecular functioni

  1. chitinase activity Source: UniProtKB-EC

GO - Biological processi

  1. chitin catabolic process Source: UniProtKB-KW
  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

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 563540Chitinase APRO_0000011908Add
BLAST

Interactioni

Structurei

Secondary structure

1
563
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 437Combined sources
Helixi50 – 534Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 6710Combined sources
Beta strandi69 – 713Combined sources
Beta strandi75 – 817Combined sources
Beta strandi84 – 907Combined sources
Beta strandi93 – 10210Combined sources
Beta strandi106 – 11611Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi156 – 16510Combined sources
Helixi166 – 1694Combined sources
Beta strandi170 – 1723Combined sources
Helixi176 – 1783Combined sources
Helixi181 – 1833Combined sources
Beta strandi185 – 1928Combined sources
Turni198 – 2003Combined sources
Helixi202 – 2065Combined sources
Helixi210 – 2178Combined sources
Turni218 – 2203Combined sources
Helixi231 – 2355Combined sources
Helixi251 – 26212Combined sources
Beta strandi267 – 2737Combined sources
Turni275 – 2773Combined sources
Helixi279 – 2835Combined sources
Helixi287 – 30317Combined sources
Beta strandi309 – 3135Combined sources
Helixi331 – 35323Combined sources
Beta strandi358 – 3647Combined sources
Helixi367 – 3704Combined sources
Helixi375 – 3784Combined sources
Helixi379 – 3813Combined sources
Beta strandi383 – 3886Combined sources
Beta strandi392 – 3943Combined sources
Beta strandi398 – 4003Combined sources
Helixi420 – 43011Combined sources
Helixi434 – 4363Combined sources
Beta strandi437 – 45014Combined sources
Helixi459 – 4613Combined sources
Beta strandi465 – 4673Combined sources
Beta strandi471 – 4733Combined sources
Beta strandi476 – 4783Combined sources
Helixi479 – 4857Combined sources
Beta strandi486 – 4883Combined sources
Beta strandi492 – 4965Combined sources
Turni497 – 5004Combined sources
Beta strandi501 – 5066Combined sources
Turni507 – 5104Combined sources
Beta strandi511 – 5144Combined sources
Helixi518 – 53114Combined sources
Beta strandi535 – 5395Combined sources
Helixi541 – 5433Combined sources
Helixi547 – 5559Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 24-563.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07254.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 563414CatalyticAdd
BLAST

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_hydro18cat.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521N → S in CAA85291. (PubMed:7851747)Curated
Sequence conflicti73 – 731A → T in CAA85291. (PubMed:7851747)Curated
Sequence conflicti76 – 772TA → GP in CAA27292. (PubMed:16453672)Curated
Sequence conflicti79 – 791I → V in CAA85291. (PubMed:7851747)Curated
Sequence conflicti121 – 1211T → S in CAA85291. (PubMed:7851747)Curated
Sequence conflicti139 – 1391A → P in CAA27292. (PubMed:16453672)Curated
Sequence conflicti226 – 2261V → I in CAA27292. (PubMed:16453672)Curated
Sequence conflicti395 – 3951P → A1 PublicationCurated
Sequence conflicti395 – 3951P → A(PubMed:16453672)Curated
Sequence conflicti395 – 3951P → A(PubMed:7851747)Curated
Sequence conflicti410 – 42920PAWKP…NALLA → RPGSRHRLHHGERRQCAAG1 PublicationCuratedAdd
BLAST
Sequence conflicti410 – 42920PAWKP…NALLA → RPGSRHRLHHGERRQCAAG(PubMed:16453672)CuratedAdd
BLAST
Sequence conflicti437 – 4371V → I(PubMed:16453672)Curated
Sequence conflicti437 – 4371V → I(PubMed:7851747)Curated
Sequence conflicti464 – 4674ATGP → HRA in CAA27292. (PubMed:16453672)Curated
Sequence conflicti473 – 4731K → E(PubMed:16453672)Curated
Sequence conflicti473 – 4731K → E(PubMed:7851747)Curated
Sequence conflicti484 – 4841G → S in CAA27292. (PubMed:16453672)Curated

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 .
PIRi A25090.
S60651.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CTN X-ray 2.30 A 24-563 [» ]
1EHN X-ray 1.90 A 24-563 [» ]
1EIB X-ray 1.80 A 24-563 [» ]
1FFQ X-ray 1.90 A 24-563 [» ]
1FFR X-ray 1.80 A 24-563 [» ]
1K9T X-ray 1.80 A 24-563 [» ]
1NH6 X-ray 2.05 A 24-563 [» ]
1RD6 X-ray 2.60 A 1-563 [» ]
1X6L X-ray 1.90 A 1-563 [» ]
1X6N X-ray 2.00 A 1-563 [» ]
2WK2 X-ray 2.05 A 24-563 [» ]
2WLY X-ray 2.40 A 24-563 [» ]
2WLZ X-ray 1.82 A 24-563 [» ]
2WM0 X-ray 1.90 A 24-563 [» ]
ProteinModelPortali P07254.
SMRi P07254. Positions 24-563.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P07254.
ChEMBLi CHEMBL5423.

Protein family/group databases

CAZyi GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17691.
BRENDAi 3.2.1.14. 5690.
SABIO-RK P07254.

Miscellaneous databases

EvolutionaryTracei P07254.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.10.50.10. 1 hit.
3.20.20.80. 2 hits.
InterProi IPR011583. Chitinase_II.
IPR029070. Chitinase_insertion.
IPR013540. ChitinaseA_N.
IPR001223. Glyco_hydro18cat.
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 ]
Pfami PF08329. ChitinaseA_N. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view ]
SMARTi SM00636. Glyco_18. 1 hit.
SM00089. PKD. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
SSF54556. SSF54556. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS01095. CHITINASE_18. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Isolation and characterization of genes encoding two chitinase enzymes from Serratia marcescens."
    Jones J.D.G., Grady K.L., Suslow T.V., Bedbrook J.R.
    EMBO J. 5:467-473(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 990 / QMB1466.
  3. "Characterization of a chitinase gene (chiA) from Serratia marcescens BJL200 and one-step purification of the gene product."
    Brurberg M.B., Eijsink V.G.H., Nes I.F.
    FEMS Microbiol. Lett. 124:399-404(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-31.
    Strain: BJL200.
  4. "Crystal structure of a bacterial chitinase at 2.3-A resolution."
    Perrakis A., Tews I., Dauter Z., Oppenheim A.B., Chet I., Wilson K.S., Vorgias C.E.
    Structure 2:1169-1180(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), SEQUENCE REVISION.

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 26, 2014
This is version 112 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

External Data

Dasty 3