CAZyme Information: OTA33385.1

Basic Information

• Species: Hortaea werneckii
• Lineage: Ascomycota; Dothideomycetes; ; Teratosphaeriaceae; Hortaea; Hortaea werneckii
• CAZyme ID: OTA33385.1
• CAZy Family: GH43
• CAZyme Description: Chitinase [Source:UniProtKB/TrEMBL;Acc:A0A1Z5TBH0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
604		65644.68	4.6504

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HwerneckiiEXF-2000	15649	1157616	29	15620

Full Sequence      

MWSRIGNSYGQGSGELAQQRLATYCADTDIDVIPMAFLYQITTGIDGQPVVNFANQQNNC
ITFPGTGLLNCPEIADDIVTCQLKYKKTIFLSVGGATYTEGGFSSRDVAKQAAEKIWATF
GPKQDESTLRPFGSAVIDGFDIDFETTMNNAAPFANRLRELMDSDATKQYFLTAAPQCPY
PDIADDEMLSGGTYFDAIFIQFYNNYCGVNSFVPGSAEQINFNFETWNNWARTVSANPDV
KILLGVPANTGAAGTGYLPVSGLGPIIAYCKQFPSFAGVMMWDVSQATSTTNNIQAQGSS
GETNMASDDARVQNNKDFQLNELFNVKNKVALITGGGSGIGLMYTQALAVNGAKVYICGR
TGEKLDTVAKTYSQDIPGSIIPITADITSKQEIQKLYDELEKREGHLDILVNNAGIMSDK
TITTEAQTPEEMKKNMFDDDKNSFQDWDDIYRTNVSQCYFMSTCFIPLLAKATQHTHGYS
GTIINVSSISGQVKTSQHHPQYNASKAACIHLTRMLANEIAQNEIKIRVNTIAPGVFPSE
MTAGSSGANQKSAIPKDKYENKVPAARPGNDRDMASTLLFCATNTYLNGQTITVDGGYTL
AAGM

Enzyme Prediction     

EC	3.2.1.14:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	20	255	1e-22	0.625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
119356	GH18_hevamine_XipI_class_III	2.17e-100	9	292	7	273	This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.
212491	SDR_c	1.64e-55	331	595	1	234	classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.
223959	FabG	2.57e-52	324	599	1	251	NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism, General function prediction only].
235500	fabG	3.68e-51	324	601	1	248	3-ketoacyl-(acyl-carrier-protein) reductase; Validated
187646	RhlG_SDR_c	2.25e-50	323	597	1	250	RhlG and related beta-ketoacyl reductases, classical (c) SDRs. Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGA16639.1|GH18	QGA16639.1|GH18	2.14e-116	7	300	38	328
APA13982.1|CBM1|GH18	APA13982.1|CBM1|GH18	8.31e-115	7	286	39	311
QVM12361.1|GH18	QVM12361.1|GH18	1.66e-114	7	295	37	323
AAP46398.1|GH18	AAP46398.1|GH18	1.05e-112	7	295	37	323
BCR98914.1|GH18	BCR98914.1|GH18	3.85e-112	7	287	39	317

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2UY2_A	2UY2_A	3.58e-54	9	293	12	275	ScCTS1_apo crystal structure [Saccharomyces cerevisiae],2UY3_A ScCTS1_8-chlorotheophylline crystal structure [Saccharomyces cerevisiae],2UY4_A ScCTS1_acetazolamide crystal structure [Saccharomyces cerevisiae],2UY5_A ScCTS1_kinetin crystal structure [Saccharomyces cerevisiae],4TXE_A ScCTS1 in complex with compound 5 [Saccharomyces cerevisiae]
2XTK_A	2XTK_A	3.48e-36	2	293	1	293	ChiA1 from Aspergillus fumigatus in complex with acetazolamide [Aspergillus fumigatus A1163],2XTK_B ChiA1 from Aspergillus fumigatus in complex with acetazolamide [Aspergillus fumigatus A1163],2XUC_A Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XUC_B Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XUC_C Natural product-guided discovery of a fungal chitinase inhibitor [Aspergillus fumigatus],2XVP_A ChiA1 from Aspergillus fumigatus, apostructure [Aspergillus fumigatus A1163],2XVP_B ChiA1 from Aspergillus fumigatus, apostructure [Aspergillus fumigatus A1163]
2XVN_A	2XVN_A	4.67e-36	3	293	1	292	A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus],2XVN_B A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus],2XVN_C A. fumigatus chitinase A1 phenyl-methylguanylurea complex [Aspergillus fumigatus]
4TX6_A	4TX6_A	4.78e-36	3	293	2	293	AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163],4TX6_B AfChiA1 in complex with compound 1 [Aspergillus fumigatus A1163]
2GSJ_A	2GSJ_A	1.21e-31	9	283	7	254	cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity [Parkia platycephala]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B4X4|CHI33_ARTBC	sp|D4B4X4|CHI33_ARTBC	5.93e-99	29	292	39	302	Class III chitinase ARB_03514 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_03514 PE=1 SV=2
sp|Q12713|CHI33_TRIHA	sp|Q12713|CHI33_TRIHA	9.60e-80	9	291	33	310	Endochitinase 33 OS=Trichoderma harzianum OX=5544 GN=chit33 PE=1 SV=1
sp|P40954|CHI3_CANAL	sp|P40954|CHI3_CANAL	1.46e-53	3	293	23	298	Chitinase 3 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT3 PE=1 SV=2
sp|P29029|CHIT_YEAST	sp|P29029|CHIT_YEAST	8.44e-51	9	293	33	296	Endochitinase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=CTS1 PE=1 SV=2
sp|P29026|CHI1_RHIOL	sp|P29026|CHI1_RHIOL	1.09e-50	2	287	24	297	Chitinase 1 OS=Rhizopus oligosporus OX=4847 GN=CHI1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999783	0.000261

TMHMM  Annotations     

There is no transmembrane helices in OTA33385.1.