Q54276 (Q54276_SERMA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Chitinase EMBL CAA85292.1

Gene names

Name:

chiB EMBL CAA85292.1

Organism

Serratia marcescens EMBL CAA85292.1

Taxonomic identifier

615 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 18 family. RuleBase RU004453

Ontologies

Keywords
Molecular function	Glycosidase RuleBase RU000489 Hydrolase
Technical term	3D-structure PDB 1W1T PDB 1E6N PDB 1UR8 PDB 1E6Z PDB 1GOI PDB 1W1V PDB 1W1Y PDB 1W1P PDB 1E6R PDB 1E15 PDB 1E6P PDB 1GPF PDB 1UR9
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
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: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 499	499	chitinase EMBL CAA85292.1		PRO_5000147550
Regions
	Region	97 – 98	2	N-acetyl-D-glucosamine binding PDB 1E6N PDB 1UR8 PDB 1E6Z PDB 1UR9
	Region	142 – 145	4	N-acetyl-D-glucosamine binding PDB 1E6N
	Region	214 – 215	2	N-acetyl-D-glucosamine binding PDB 1E6N
	Region	220 – 221	2	N-acetyl-D-glucosamine binding PDB 1E6N PDB 1E6Z
	Region	480 – 481	2	N-acetyl-D-glucosamine binding PDB 1E6N
Sites
	Binding site	12	1	N-acetyl-D-glucosamine PDB 1E6N PDB 1UR8 PDB 1UR9
	Binding site	191	1	N-acetyl-D-glucosamine PDB 1E6Z
	Binding site	294	1	N-acetyl-D-glucosamine PDB 1E6N
	Binding site	316	1	N-acetyl-D-glucosamine PDB 1E6Z
	Binding site	403	1	N-acetyl-D-glucosamine PDB 1E6N PDB 1UR8 PDB 1UR9
	Binding site	407	1	N-acetyl-D-glucosamine PDB 1UR8 PDB 1UR9

Sequences

	Sequence		Length	Mass (Da)
	Q54276 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 58C933A9064D526B	FASTA	499	55,469
	10 20 30 40 50 60 MSTRKAVIGY YFIPTNQINN YTETDTSVVP FPVSNITPAK AKQLTHINFS FLDINSNLEC 70 80 90 100 110 120 AWDPATNDAK ARDVVNRLTA LKAHNPSLRI MFSIGGWYYS NDLGVSHANY VNAVKTPASR 130 140 150 160 170 180 AKFAQSCVRI MKDYGFDGVD IDWEYPQAAE VDGFIAALQE IRTLLNQQTI TDGRQALPYQ 190 200 210 220 230 240 LTIAGAGGAF FLSRYYSKLA QIVAPLDYIN LMTYDLAGPW EKVTNHQAAL FGDAAGPTFY 250 260 270 280 290 300 NALREANLGW SWEELTRAFP SPFSLTVDAA VQQHLMMEGV PSAKIVMGVP FYGRAFKGVS 310 320 330 340 350 360 GGNGGQYSSH STPGEDPYPS TDYWLVGCEE CVRDKDPRIA SYRQLEQMLQ GNYGYQRLWN 370 380 390 400 410 420 DKTKTPYLYH AQNGLFVTYD DAESFKYKAK YIKQQQLGGV MFWHLGQDNR NGDLLAALDR 430 440 450 460 470 480 YFNAADYDDS QLDMGTGLRY TGVGPGNLPI MTAPAYVPGT TYAQGALVSY QGYVWQTKWG 490 YITSAPGSDS AWLKVGRVA

References

[1]	"Chitinase B from Serratia marcescens BJL200 is exported to the periplasm without processing." Brurberg M.B., Eijsink V.G., Haandrikman A.J., Venema G., Nes I.F. Microbiology 141:123-131(1995) [PubMed: 7894703] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	Brurberg M. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9-A resolution." van Aalten D.M., Synstad B., Brurberg M.B., Hough E., Riise B.W., Eijsink V.G., Wierenga R.K. Proc. Natl. Acad. Sci. U.S.A. 97:5842-5847(2000) [PubMed: 10823940] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).
[4]	"Structural insights into the catalytic mechanism of a family 18 exo-chitinase." van Aalten D.M., Komander D., Synstad B., Gaseidnes S., Peter M.G., Eijsink V.G. Proc. Natl. Acad. Sci. U.S.A. 98:8979-8984(2001) [PubMed: 11481469] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE.
[5]	"Psammaplin A, a chitinase inhibitor isolated from the Fijian marine sponge Aplysinella rhax." Tabudravu J.N., Eijsink V.G., Gooday G.W., Jaspars M., Komander D., Legg M., Synstad B., van Aalten D.M. Bioorg. Med. Chem. 10:1123-1128(2002) [PubMed: 11836123] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[6]	"Interactions of a family 18 chitinase with the designed inhibitor HM508 and its degradation product, chitobiono-delta-lactone." Vaaje-Kolstad G., Vasella A., Peter M.G., Netter C., Houston D.R., Westereng B., Synstad B., Eijsink V.G., van Aalten D.M. J. Biol. Chem. 279:3612-3619(2004) [PubMed: 14597613] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-498 IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE.
[7]	"Structure of the D140N mutant of chitinase B from Serratia marcescens at 1.45 A resolution." Kolstad G., Synstad B., Eijsink V.G., van Aalten D.M. Acta Crystallogr. D Biol. Crystallogr. 58:377-379(2002) [PubMed: 11807282] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[8]	"Structure-based exploration of cyclic dipeptide chitinase inhibitors." Houston D.R., Synstad B., Eijsink V.G., Stark M.J., Eggleston I.M., van Aalten D.M. J. Med. Chem. 47:5713-5720(2004) [PubMed: 15509170] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z36295 Genomic DNA. Translation: CAA85292.1.

PIR

S52422.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E15	X-ray	1.90	A/B	1-499	[»]
1E6P	X-ray	1.70	A/B	1-499	[»]
1E6R	X-ray	2.50	A/B	1-499	[»]
1E6Z	X-ray	1.99	A/B	2-499	[»]
1GPF	X-ray	1.85	A/B	1-499	[»]
1UR8	X-ray	1.90	A/B	1-499	[»]
1UR9	X-ray	1.80	A/B	1-498	[»]
1W1P	X-ray	2.10	A/B	1-499	[»]
1W1T	X-ray	1.90	A/B	1-499	[»]
1W1V	X-ray	1.85	A/B	1-499	[»]
1W1Y	X-ray	1.85	A/B	1-499	[»]

ProteinModelPortal

Q54276.

SMR

Q54276. Positions 2-499.

ModBase

Search...

Protein family/group databases

CAZy

CBM5. Carbohydrate-Binding Module Family 5.
GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR003610. CBM_fam5/12.
IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR001579. Glyco_hydro_18_chit_AS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.10.10.20. G3DSA:2.10.10.20. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 2 hits.

Pfam

PF02839. CBM_5_12. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

SMART

SM00495. ChtBD3. 1 hit.
SM00636. Glyco_18. 1 hit.
[Graphical view]

SUPFAM

SSF51055. CBM_5_12. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS01095. CHITINASE_18. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

Q54276_SERMA

Accession

Primary (citable) accession number: Q54276

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)