CAZyme Information: EAQ93216.1

Basic Information

• Species: Chaetomium globosum
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
• CAZyme ID: EAQ93216.1
• CAZy Family: GT39
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
487		52733.03	6.8445

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CglobosumCBS148.51	11232	306901	184	11048

• Gene Location: location=CH408029:4456930-4459150(-)

Full Sequence      

MMKAALLFLATVAGVNSAALAPRQKETLCELYAYWSGNGYELLNNLWGKDAATSGSQCTY
LDGASSEGVQWHTTWTWEGGPNNVKSYPYVGRQVAKGRTISSISKMPTSVKWDYDNENIR
ANVAYDVFTAEDPNHVNSSGDFELMIWLARYGNVYPIGSSVGTVTVAGKTWDLWTGFNGA
MRVYSFVPPSGTVKEFSADVKEFYTYLEQNYQFPSSKQNVIDYPPSIASHPALSLSVPWE
NPTPHHHPRTITTSPRSSTRPRVAIVTGASARHRACHRHPPRTRRTTASPPRDLPALQPH
LDSLITELTSTSISTTNTHTPPQPPHHAFPADVTSPEQVAALVHASATTLGPLDTMVANA
GIAQVKPLLELTAEDFRRMLDVNVAGVHHCFQAAARAMIAQQKEEHQGGGGDGVGGRERE
GEEVRGRLIAAASIVAFKPLRCWGLTARVIRGGEGVESGVCDGVGGAWDYGECVRAGDCG
YQDVGAD

Enzyme Prediction     

EC	3.2.1.4:107	3.2.1.151:22	3.2.1.73:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH12	98	222	6.8e-43	0.8141025641025641

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396303	Glyco_hydro_12	2.54e-66	38	223	1	183	Glycosyl hydrolase family 12.
235746	PRK06215	7.66e-32	3	193	13	190	hypothetical protein; Provisional
187624	meso-BDH-like_SDR_c	1.86e-23	327	434	55	141	meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs. 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-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.
212491	SDR_c	2.51e-20	326	444	48	144	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.
395056	adh_short	1.48e-19	327	444	52	147	short chain dehydrogenase. This family contains a wide variety of dehydrogenases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VBB80352.1|GH12	1.52e-120	2	223	1	222
CAP66908.1|GH12	1.23e-119	2	221	1	220
CDP28650.1|GH12	1.23e-119	2	221	1	220
ABJ29220.1|GH12|3.2.1.4	2.05e-104	1	223	1	230
ACP76239.1|GH12|3.2.1.4	2.05e-104	1	223	1	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1OLR_A	1.19e-101	26	223	3	200	The Humicola grisea Cel12A Enzyme Structure at 1.2 A Resolution [Trichocladium griseum],1UU4_A X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH CELLOBIOSE [Trichocladium griseum],1UU5_A X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A SOAKED WITH CELLOTETRAOSE [Trichocladium griseum],1UU6_A X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH A SOAKED CELLOPENTAOSE [Trichocladium griseum],1W2U_A X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMICOLA GRISEA CEL12A IN COMPLEX WITH A SOAKED THIO CELLOTETRAOSE [Trichocladium griseum]
7EE2_A	2.85e-92	20	221	1	201	Chain A, glycoside hydrolase family 12 beta-1,3-1,4-glucanase [Chaetomium sp.],7EEE_A Chain A, glycoside hydrolase family 12 beta-1,3-1,4-glucanase [Chaetomium sp.],7EEJ_A Chain A, glycoside hydrolase family 12 beta-1,3-1,4-glucanase [Chaetomium sp.]
5M2D_A	2.28e-75	6	221	3	209	CRYSTAL STRUCTURE 4Ac Endoglucanase-like protein from Acremonium chrysogenum [Acremonium chrysogenum ATCC 11550],5M2D_B CRYSTAL STRUCTURE 4Ac Endoglucanase-like protein from Acremonium chrysogenum [Acremonium chrysogenum ATCC 11550]
5GM3_A	1.26e-69	28	221	3	193	Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 [Aspergillus aculeatus],5GM3_B Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 [Aspergillus aculeatus]
5GM4_A	1.26e-69	28	221	3	193	Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 in complex with cellotetrose [Aspergillus aculeatus],5GM4_B Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 in complex with cellotetrose [Aspergillus aculeatus],5GM4_C Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 in complex with cellotetrose [Aspergillus aculeatus],5GM4_D Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 in complex with cellotetrose [Aspergillus aculeatus],5GM4_E Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 in complex with cellotetrose [Aspergillus aculeatus],5GM4_F Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 in complex with cellotetrose [Aspergillus aculeatus],5GM4_G Crystal structure of FI-CMCase from Aspergillus aculeatus F-50 in complex with cellotetrose [Aspergillus aculeatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G4NAZ1|CE12A_MAGO7	4.05e-88	4	218	5	228	Endoglucanase cel12A OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=cel12A PE=1 SV=1
sp|G4N5V2|CE12B_MAGO7	5.94e-74	27	223	37	239	Endoglucanase cel12B OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=cel12B PE=1 SV=1
sp|P22669|GUN_ASPAC	3.74e-70	12	221	7	211	Endoglucanase-1 OS=Aspergillus aculeatus OX=5053 PE=1 SV=1
sp|Q12679|GUNA_ASPKW	1.15e-57	21	221	12	213	Endoglucanase A OS=Aspergillus kawachii (strain NBRC 4308) OX=1033177 GN=cekA PE=2 SV=2
sp|Q5BG78|XGEA_EMENI	5.63e-48	11	217	7	210	Xyloglucan-specific endo-beta-1,4-glucanase A OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xgeA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000252	0.999712	CS pos: 17-18. Pr: 0.9775

TMHMM  Annotations     

There is no transmembrane helices in EAQ93216.1.