CHI1_COCPS
ID CHI1_COCPS Reviewed; 427 AA.
AC P0CB51; E9DFQ8; P54196; Q00432; Q00435; Q400W4; Q400W5; Q400W6; Q9C0M7;
AC Q9C2W1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Endochitinase 1;
DE EC=3.2.1.14;
DE AltName: Full=CiX1;
DE AltName: Full=Complement-fixation antigen;
DE Short=CF-AG;
DE Short=CF-antigen;
DE Flags: Precursor;
GN Name=CTS1; ORFNames=CPSG_08657;
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=RMSCC 757 / Silveira;
RX PubMed=8675298; DOI=10.1128/iai.64.6.1992-1997.1996;
RA Yang C., Zhu Y., Magee D.M., Cox R.A.;
RT "Molecular cloning and characterization of the Coccidioides immitis
RT complement fixation/chitinase antigen.";
RL Infect. Immun. 64:1992-1997(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=RMSCC 757 / Silveira;
RX PubMed=8945534; DOI=10.1128/iai.64.12.4967-4975.1996;
RA Zimmermann C.R., Johnson S.M., Martens G.W., White A.G., Pappagianis D.;
RT "Cloning and expression of the complement fixation antigen-chitinase of
RT Coccidioides immitis.";
RL Infect. Immun. 64:4967-4975(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-151.
RC STRAIN=IFM 45809 / Silveira, IFM 45810 / Silveira, IFM 45811, IFM 45812,
RC IFM 45813, IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM 51112,
RC IFM 54194, IFM 54195, and IFM 54196;
RX PubMed=16699492; DOI=10.3314/jjmm.47.113;
RA Sano A., Miyaji M., Kamei K., Mikami Y., Nishimura K.;
RT "Reexamination of Coccidioides spp. reserved in the Research Center for
RT Pathogenic Fungi and Microbial Toxicoses, Chiba University, based on a
RT multiple gene analysis.";
RL Nippon Ishinkin Gakkai Zasshi 47:113-117(2006).
RN [5]
RP PROTEIN SEQUENCE OF 18-38.
RC STRAIN=RMSCC 757 / Silveira;
RX PubMed=8514419; DOI=10.1128/iai.61.7.3090-3092.1993;
RA Johnson S.M., Zimmermann C.R., Pappagianis D.;
RT "Amino-terminal sequence analysis of the Coccidioides immitis
RT chitinase/immunodiffusion-complement fixation protein.";
RL Infect. Immun. 61:3090-3092(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-145, AND VARIANT SER-26.
RC STRAIN=RMSCC 1036 / AZ1, RMSCC 2128 / TX1, and RMSCC 757 / Silveira;
RX PubMed=9144263; DOI=10.1073/pnas.94.10.5478;
RA Koufopanou V., Burt A., Taylor J.W.;
RT "Concordance of gene genealogies reveals reproductive isolation in the
RT pathogenic fungus Coccidioides immitis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5478-5482(1997).
RN [7]
RP ERRATUM OF PUBMED:9144263.
RA Koufopanou V., Burt A., Taylor J.W.;
RL Proc. Natl. Acad. Sci. U.S.A. 95:8414-8414(1998).
RN [8]
RP PROTEIN SEQUENCE OF 26-52.
RC STRAIN=RMSCC 757 / Silveira;
RX PubMed=2312685; DOI=10.1128/jcm.28.2.385-388.1990;
RA Resnick S., Zimmer B., Pappagianis D., Eakin A., McKerrow J.;
RT "Purification and amino-terminal sequence analysis of the complement-fixing
RT and precipitin antigens from Coccidioides immitis.";
RL J. Clin. Microbiol. 28:385-388(1990).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=RMSCC 757 / Silveira;
RX PubMed=11327866; DOI=10.1021/bi001537s;
RA Fukamizo T., Sasaki C., Schelp E., Bortone K., Robertus J.D.;
RT "Kinetic properties of chitinase-1 from the fungal pathogen Coccidioides
RT immitis.";
RL Biochemistry 40:2448-2454(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 36-427, PROTEIN SEQUENCE OF 27-41,
RP AND MUTAGENESIS OF GLU-171.
RC STRAIN=RMSCC 757 / Silveira;
RX PubMed=10752616; DOI=10.1110/ps.9.3.544;
RA Hollis T., Monzingo A.F., Bortone K., Ernst S., Cox R.A., Robertus J.D.;
RT "The X-ray structure of a chitinase from the pathogenic fungus Coccidioides
RT immitis.";
RL Protein Sci. 9:544-551(2000).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 36-427 OF WILD-TYPE IN COMPLEX
RP WITH INHIBITOR AND OF MUTANTS ASN-169 AND GLN-171.
RC STRAIN=RMSCC 757 / Silveira;
RX PubMed=12079386; DOI=10.1016/s0022-2836(02)00444-8;
RA Bortone K., Monzingo A.F., Ernst S., Robertus J.D.;
RT "The structure of an allosamidin complex with the Coccidioides immitis
RT chitinase defines a role for a second acid residue in substrate-assisted
RT mechanism.";
RL J. Mol. Biol. 320:293-302(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. Active from pH 4 to 8.
CC {ECO:0000269|PubMed:11327866};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE20289.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20290.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20291.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20292.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20293.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20294.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20295.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20301.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20302.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20304.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE20307.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U51271; AAA96515.1; -; Genomic_DNA.
DR EMBL; U33265; AAB06687.1; -; mRNA.
DR EMBL; U60806; AAB48566.1; -; Genomic_DNA.
DR EMBL; U60807; AAB48567.1; -; mRNA.
DR EMBL; GL636504; EFW14650.1; -; Genomic_DNA.
DR EMBL; AB232745; BAE20289.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232746; BAE20290.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232747; BAE20291.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232748; BAE20292.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232749; BAE20293.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232750; BAE20294.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232751; BAE20295.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232754; BAE20298.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232757; BAE20301.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232758; BAE20302.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232760; BAE20304.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232761; BAE20305.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232762; BAE20306.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB232763; BAE20307.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ408862; CAC29128.1; -; Genomic_DNA.
DR EMBL; AJ408863; CAC29129.1; -; Genomic_DNA.
DR EMBL; AJ408864; CAC29130.1; -; Genomic_DNA.
DR PIR; JC4565; JC4565.
DR PDB; 1D2K; X-ray; 2.20 A; A=36-427.
DR PDB; 1LL4; X-ray; 2.80 A; A/B/C/D=36-427.
DR PDB; 1LL6; X-ray; 2.80 A; A/B/C/D=36-427.
DR PDB; 1LL7; X-ray; 2.00 A; A/B=36-427.
DR PDBsum; 1D2K; -.
DR PDBsum; 1LL4; -.
DR PDBsum; 1LL6; -.
DR PDBsum; 1LL7; -.
DR AlphaFoldDB; P0CB51; -.
DR SMR; P0CB51; -.
DR STRING; 443226.P0CB51; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR CLAE; CHI18A_COCIM; -.
DR EnsemblFungi; EFW14650; EFW14650; CPSG_08657.
DR VEuPathDB; FungiDB:CPSG_08657; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_002833_1_3_1; -.
DR EvolutionaryTrace; P0CB51; -.
DR Proteomes; UP000002497; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.10; -; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF54556; SSF54556; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:8514419"
FT CHAIN 18..427
FT /note="Endochitinase 1"
FT /id="PRO_0000011927"
FT DOMAIN 38..401
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 102..103
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 129..132
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 172
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 237..240
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT BINDING 378
FT /ligand="chitin"
FT /ligand_id="ChEBI:CHEBI:17029"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT SITE 169
FT /note="Transition state stabilizer"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 13
FT /note="T -> I (in strain: IFM 50993)"
FT VARIANT 26
FT /note="Y -> S (in strain: IFM 45811, IFM 45812, IFM 45813,
FT IFM 45817, IFM 4935, IFM 4945, IFM 50993, IFM 50994, IFM
FT 51112, IFM 54194, IFM 54195, IFM 54196, RMSCC 1036 / AZ1
FT and RMSCC 2128 / TX1)"
FT /evidence="ECO:0000269|PubMed:9144263"
FT VARIANT 103
FT /note="N -> K (in strain: IFM 45811, IFM 45817, IFM 4945
FT and IFM 50994)"
FT VARIANT 109
FT /note="I -> T (in strain: IFM 45811, IFM 45817, IFM 4945
FT and IFM 50994)"
FT MUTAGEN 169
FT /note="D->N: Loss of function."
FT MUTAGEN 171
FT /note="E->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:10752616"
FT CONFLICT 19
FT /note="S -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="E -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="S -> A (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="W -> R (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="K -> N (in Ref. 1; AAA96515/AAB06687)"
FT /evidence="ECO:0000305"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1LL7"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1LL4"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1D2K"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 144..161
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 176..198
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:1LL7"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:1LL7"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 357..369
FT /evidence="ECO:0007829|PDB:1LL7"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 386..388
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 390..397
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:1LL7"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:1LL7"
SQ SEQUENCE 427 AA; 47474 MW; 911CE4777F35D2D9 CRC64;
MRFLIGALLT LQTLVQASSM SSMPNYYPVP EAPAEGGFRS VVYFVNWAIY GRGHNPQDLK
ADQFTHILYA FANIRPSGEV YLSDTWADTD KHYPGDKWDE PGNNVYGCIK QMYLLKKNNR
NLKTLLSIGG WTYSPNFKTP ASTEEGRKKF ADTSLKLMKD LGFDGIDIDW EYPEDEKQAN
DFVLLLKACR EALDAYSAKH PNGKKFLLTI ASPAGPQNYN KLKLAEMDKY LDFWNLMAYD
FSGSWDKVSG HMSNVFPSTT KPESTPFSSD KAVKDYIKAG VPANKIVLGM PLYGRAFAST
DGIGTSFNGV GGGSWENGVW DYKDMPQQGA QVTELEDIAA SYSYDKNKRY LISYDTVKIA
GKKAEYITKN GMGGGMWWES SSDKTGNESL VGTVVNGLGG TGKLEQRENE LSYPESVYDN
LKNGMPS
