Q873X9 (Q873X9_ASPFM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Chitinase EMBL AAO61686.1

Gene names

Name:

chiB1 EMBL AAO61686.1

Organism

Neosartorya fumigata (Aspergillus fumigatus) EMBL AAO61686.1

Taxonomic identifier

746128 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length	433 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 2A3B PDB 2IUZ PDB 2A3A PDB 2A3E PDB 2A3C PDB 1W9V PDB 1W9U PDB 1W9P PDB 3CHC PDB 3CHE PDB 3CHD PDB 3CHF PDB 3CH9
Gene Ontology (GO)
Biological process	chitin catabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	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
Sites
	Binding site	52	1	Caffeine 2 PDB 2A3B
	Binding site	137	1	Caffeine 1; via amide nitrogen PDB 2A3B
	Binding site	137	1	Caffeine 3 PDB 2A3B
	Binding site	245	1	Caffeine 1 PDB 2A3B
	Binding site	246	1	Caffeine 3 PDB 2A3B
	Binding site	251	1	Caffeine 3 PDB 2A3B
	Binding site	384	1	Caffeine 1 PDB 2A3B

Sequences

	Sequence		Length	Mass (Da)
	Q873X9 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 95AECA3DCE917D30	FASTA	433	47,622
	10 20 30 40 50 60 MRFATSTIVK VALLLSSLCV DAAVMWNRDT SSTDLEARAS SGYRSVVYFV NWAIYGRNHN 70 80 90 100 110 120 PQDLPVERLT HVLYAFANVR PETGEVYMTD SWADIEKHYP GDSWSDTGNN VYGCIKQLYL 130 140 150 160 170 180 LKKQNRNLKV LLSIGGWTYS PNFAPAASTD AGRKNFAKTA VKLLQDLGFD GLDIDWEYPE 190 200 210 220 230 240 NDQQANDFVL LLKEVRTALD SYSAANAGGQ HFLLTVASPA GPDKIKVLHL KDMDQQLDFW 250 260 270 280 290 300 NLMAYDYAGS FSSLSGHQAN VYNDTSNPLS TPFNTQTALD LYRAGGVPAN KIVLGMPLYG 310 320 330 340 350 360 RSFANTDGPG KPYNGVGQGS WENGVWDYKA LPQAGATEHV LPDIMASYSY DATNKFLISY 370 380 390 400 410 420 DNPQVANLKS GYIKSLGLGG AMWWDSSSDK TGSDSLITTV VNALGGTGVF EQSQNELDYP 430 VSQYDNLRNG MQT

References

[1]	"Disruption of the gene encoding the ChiB1 chitinase of Aspergillus fumigatus and characterization of a recombinant gene product." Jaques A.K., Fukamizo T., Hall D., Barton R.C., Escott G.M., Parkinson T., Hitchcock C.A., Adams D.J. Microbiology 149:2931-2939(2003) [PubMed: 14523125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 13073 EMBL AAO61686.1.
[2]	"Screening-based discovery and structural dissection of a novel family 18 chitinase inhibitor." Schuttelkopf A.W., Andersen O.A., Rao F.V., Allwood M., Lloyd C., Eggleston I.M., van Aalten D.M. J. Biol. Chem. 281:27278-27285(2006) [PubMed: 16844689] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
[3]	"Methylxanthine drugs are chitinase inhibitors: investigation of inhibition and binding modes." Rao F.V., Andersen O.A., Vora K.A., Demartino J.A., van Aalten D.M. Chem. Biol. 12:973-980(2005) [PubMed: 16183021] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CAFFEINE.
[4]	"Specificity and affinity of natural product cyclopentapeptide inhibitors against A. fumigatus, human, and bacterial chitinases." Rao F.V., Houston D.R., Boot R.G., Aerts J.M., Hodkinson M., Adams D.J., Shiomi K., Omura S., van Aalten D.M. Chem. Biol. 12:65-76(2005) [PubMed: 15664516] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
[5]	"Structure-based dissection of the natural product cyclopentapeptide chitinase inhibitor argifin." Andersen O.A., Nathubhai A., Dixon M.J., Eggleston I.M., van Aalten D.M. Chem. Biol. 15:295-301(2008) [PubMed: 18355729] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY217660 Genomic DNA. Translation: AAO61686.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W9P	X-ray	1.70	A/B	1-433	[»]
1W9U	X-ray	1.85	A/B	1-433	[»]
1W9V	X-ray	2.00	A/B	1-433	[»]
2A3A	X-ray	2.10	A/B	1-433	[»]
2A3B	X-ray	1.90	A/B	1-433	[»]
2A3C	X-ray	2.07	A/B	1-433	[»]
2A3E	X-ray	1.95	A/B	1-433	[»]
2IUZ	X-ray	1.95	A/B	1-433	[»]
3CH9	X-ray	2.20	A/B	1-433	[»]
3CHC	X-ray	1.90	A/B	1-433	[»]
3CHD	X-ray	2.00	A/B	1-433	[»]
3CHE	X-ray	2.05	A/B	1-433	[»]
3CHF	X-ray	1.95	A/B	1-433	[»]

ProteinModelPortal

Q873X9.

SMR

Q873X9. Positions 39-433.

ModBase

Search...

Protein-protein interaction databases

STRING

Q873X9.

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

CADAFUAT00000818; CADAFUAP00000818; CADAFUAG00000818.

Phylogenomic databases

eggNOG

fuNOG07634.

GeneTree

EFGT00050000001575.

HOGENOM

HBG741095.

OrthoDB

EOG4VDT77.

Family and domain databases

InterPro

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:3.20.20.80. Glyco_hydro_cat. 2 hits.

Pfam

PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

SMART

SM00636. Glyco_18. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS01095. CHITINASE_18. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q873X9_ASPFM

Accession

Primary (citable) accession number: Q873X9
Secondary accession number(s): Q4WB85

Entry history

Integrated into UniProtKB/TrEMBL:	June 1, 2003
Last sequence update:	June 1, 2003
Last modified:	December 14, 2011
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)