Reviewed, UniProtKB/Swiss-Prot P0CB51 (CHI1_COCPO)

Names and origin

Protein names

Recommended name:
    Endochitinase 1
    EC=3.2.1.14
Alternative name(s):
    Complement-fixation antigen
      Short name=CF-antigen
      Short name=CF-AG
    CiX1

Gene names

Name:

CTS1

Organism

Coccidioides posadasii (Valley fever fungus)

Taxonomic identifier

199306 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Onygenales › mitosporic Onygenales › Coccidioides

Protein attributes

Sequence length	427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Random hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 6.0. Active from pH 4 to 8.
Sequence caution	The sequence BAE20289.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20290.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20291.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20292.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20293.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20294.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20295.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20298.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20301.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20302.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20304.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20305.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20306.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAE20307.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Chitin degradation Polysaccharide degradation
Domain	Signal
Ligand	Chitin-binding
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Ref.4

Chain

18 – 427

410

Endochitinase 1

PRO_0000011927

Sites

Active site

171

1

Proton donor

Site

169

1

Transition state stabilizer

Amino acid modifications

Glycosylation

387

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

13

1

T → I in strain: IFM 50993.

Natural variant

26

1

Y → S in strain: IFM 45809, IFM 45810, IFM 45811, IFM 45812, IFM 45813, IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM 51112, IFM 54194, IFM 54195, IFM 54196, RMSCC 1036 / AZ1 and RMSCC 2128 / TX1. Ref.5

Natural variant

103

1

N → K in strain: IFM 45811, IFM 45817, IFM 4945 and IFM 50994.

Natural variant

109

1

I → T in strain: IFM 45811, IFM 45817, IFM 4945 and IFM 50994.

Experimental info

Mutagenesis

169

1

D → N: Loss of function.

Mutagenesis

171

1

E → Q: Loss of function. Ref.9

Sequence conflict

19

1

S → P AA sequence Ref.4

Sequence conflict

31

1

E → G AA sequence Ref.4

Sequence conflict

40

1

S → A AA sequence Ref.7

Sequence conflict

47

1

W → R AA sequence Ref.7

Sequence conflict

199

1

K → N in AAA96515. Ref.1

Sequence conflict

199

1

K → N in AAB06687. Ref.1

Secondary structure

1

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427

Helix Strand Turn

Details...

Beta strand

38 – 45

8

Helix

46 – 49

4

Helix

56 – 58

3

Helix

61 – 63

3

Beta strand

65 – 74

10

Beta strand

80 – 83

4

Helix

85 – 88

4

Beta strand

101 – 103

3

Helix

107 – 118

12

Beta strand

123 – 129

7

Helix

130 – 133

4

Helix

134 – 136

3

Helix

138 – 141

4

Helix

144 – 161

18

Beta strand

164 – 169

6

Helix

176 – 198

23

Beta strand

207 – 213

7

Helix

216 – 219

4

Helix

224 – 228

5

Beta strand

232 – 237

6

Helix

262 – 264

3

Helix

269 – 278

10

Helix

283 – 285

3

Beta strand

286 – 297

12

Beta strand

314 – 316

3

Beta strand

319 – 321

3

Helix

322 – 324

3

Beta strand

331 – 335

5

Turn

336 – 339

4

Beta strand

340 – 345

6

Turn

346 – 349

4

Beta strand

350 – 353

4

Helix

357 – 369

13

Beta strand

374 – 378

5

Helix

390 – 397

8

Helix

401 – 403

3

Helix

419 – 422

4

Sequences

	Sequence		Length	Mass (Da)
	P0CB51-1 [UniParc]. Last modified November 3, 2009. Version 1. Checksum: 911CE4777F35D2D9	FASTA	427	47,474
	10 20 30 40 50 60 MRFLIGALLT LQTLVQASSM SSMPNYYPVP EAPAEGGFRS VVYFVNWAIY GRGHNPQDLK 70 80 90 100 110 120 ADQFTHILYA FANIRPSGEV YLSDTWADTD KHYPGDKWDE PGNNVYGCIK QMYLLKKNNR 130 140 150 160 170 180 NLKTLLSIGG WTYSPNFKTP ASTEEGRKKF ADTSLKLMKD LGFDGIDIDW EYPEDEKQAN 190 200 210 220 230 240 DFVLLLKACR EALDAYSAKH PNGKKFLLTI ASPAGPQNYN KLKLAEMDKY LDFWNLMAYD 250 260 270 280 290 300 FSGSWDKVSG HMSNVFPSTT KPESTPFSSD KAVKDYIKAG VPANKIVLGM PLYGRAFAST 310 320 330 340 350 360 DGIGTSFNGV GGGSWENGVW DYKDMPQQGA QVTELEDIAA SYSYDKNKRY LISYDTVKIA 370 380 390 400 410 420 GKKAEYITKN GMGGGMWWES SSDKTGNESL VGTVVNGLGG TGKLEQRENE LSYPESVYDN LKNGMPS

References

[1]	"Molecular cloning and characterization of the Coccidioides immitis complement fixation/chitinase antigen." Yang C., Zhu Y., Magee D.M., Cox R.A. Infect. Immun. 64:1992-1997(1996) [PubMed: 8675298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: RMSCC 757 / Silveira.
[2]	"Cloning and expression of the complement fixation antigen-chitinase of Coccidioides immitis." Zimmermann C.R., Johnson S.M., Martens G.W., White A.G., Pappagianis D. Infect. Immun. 64:4967-4975(1996) [PubMed: 8945534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: RMSCC 757 / Silveira.
[3]	"Reexamination of Coccidioides spp. reserved in the Research Center for Pathogenic Fungi and Microbial Toxicoses, Chiba University, based on a multiple gene analysis." Sano A., Miyaji M., Kamei K., Mikami Y., Nishimura K. Nippon Ishinkin Gakkai Zasshi 47:113-117(2006) [PubMed: 16699492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-151. Strain: IFM 45809, IFM 45810, IFM 45811, IFM 45812, IFM 45813, IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM 51112, IFM 54194, IFM 54195 and IFM 54196.
[4]	"Amino-terminal sequence analysis of the Coccidioides immitis chitinase/immunodiffusion-complement fixation protein." Johnson S.M., Zimmermann C.R., Pappagianis D. Infect. Immun. 61:3090-3092(1993) [PubMed: 8514419] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-38. Strain: RMSCC 757 / Silveira.
[5]	"Concordance of gene genealogies reveals reproductive isolation in the pathogenic fungus Coccidioides immitis." Koufopanou V., Burt A., Taylor J.W. Proc. Natl. Acad. Sci. U.S.A. 94:5478-5482(1997) [PubMed: 9144263] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-145, VARIANT SER-26. Strain: RMSCC 1036 / AZ1, RMSCC 2128 / TX1 and RMSCC 757 / Silveira.
[6]	Erratum Koufopanou V., Burt A., Taylor J.W. Proc. Natl. Acad. Sci. U.S.A. 95:8414-8414(1998)
[7]	"Purification and amino-terminal sequence analysis of the complement-fixing and precipitin antigens from Coccidioides immitis." Resnick S., Zimmer B., Pappagianis D., Eakin A., McKerrow J. J. Clin. Microbiol. 28:385-388(1990) [PubMed: 2312685] [Abstract] Cited for: PROTEIN SEQUENCE OF 26-52. Strain: RMSCC 757 / Silveira.
[8]	"Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides immitis." Fukamizo T., Sasaki C., Schelp E., Bortone K., Robertus J.D. Biochemistry 40:2448-2454(2001) [PubMed: 11327866] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"The X-ray structure of a chitinase from the pathogenic fungus Coccidioides immitis." Hollis T., Monzingo A.F., Bortone K., Ernst S., Cox R.A., Robertus J.D. Protein Sci. 9:544-551(2000) [PubMed: 10752616] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 36-427, PROTEIN SEQUENCE OF 27-41, MUTAGENESIS OF GLU-171. Strain: RMSCC 757 / Silveira.
[10]	"The structure of an allosamidin complex with the Coccidioides immitis chitinase defines a role for a second acid residue in substrate-assisted mechanism." Bortone K., Monzingo A.F., Ernst S., Robertus J.D. J. Mol. Biol. 320:293-302(2002) [PubMed: 12079386] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 36-427 OF WILD-TYPE IN COMPLEX WITH INHIBITOR AND OF MUTANTS ASN-169 AND GLN-171.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U51271 Genomic DNA. Translation: AAA96515.1.
U33265 mRNA. Translation: AAB06687.1.
U60806 Genomic DNA. Translation: AAB48566.1.
U60807 mRNA. Translation: AAB48567.1.
AB232745 Genomic DNA. Translation: BAE20289.1. Sequence problems.
AB232746 Genomic DNA. Translation: BAE20290.1. Sequence problems.
AB232747 Genomic DNA. Translation: BAE20291.1. Sequence problems.
AB232748 Genomic DNA. Translation: BAE20292.1. Sequence problems.
AB232749 Genomic DNA. Translation: BAE20293.1. Sequence problems.
AB232750 Genomic DNA. Translation: BAE20294.1. Sequence problems.
AB232751 Genomic DNA. Translation: BAE20295.1. Sequence problems.
AB232754 Genomic DNA. Translation: BAE20298.1. Sequence problems.
AB232757 Genomic DNA. Translation: BAE20301.1. Sequence problems.
AB232758 Genomic DNA. Translation: BAE20302.1. Sequence problems.
AB232760 Genomic DNA. Translation: BAE20304.1. Sequence problems.
AB232761 Genomic DNA. Translation: BAE20305.1. Sequence problems.
AB232762 Genomic DNA. Translation: BAE20306.1. Sequence problems.
AB232763 Genomic DNA. Translation: BAE20307.1. Sequence problems.
AJ408862 Genomic DNA. Translation: CAC29128.1.
AJ408863 Genomic DNA. Translation: CAC29129.1.
AJ408864 Genomic DNA. Translation: CAC29130.1.

PIR

JC4565.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D2K	X-ray	2.20	A	36-427	[»]
1LL4	X-ray	2.80	A/B/C/D	36-427	[»]
1LL6	X-ray	2.80	A/B/C/D	36-427	[»]
1LL7	X-ray	2.00	A/B	36-427	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH18. Glycoside Hydrolase Family 18.

Enzyme and pathway databases

BRENDA

3.2.1.14. 281080.

Family and domain databases

PROSITE

PS01095. CHITINASE_18. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CHI1_COCPO

Accession

Primary (citable) accession number: P0CB51
Secondary accession number(s): P54196 , Q00432, Q00435, Q400W4, Q400W5, Q400W6, Q9C0M7, Q9C2W1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	November 24, 2009
This is version 2 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)