dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Histoplasma capsulatum

Lineage

Ascomycota; Eurotiomycetes; ; Ajellomycetaceae; Histoplasma; Histoplasma capsulatum

CAZyme ID

AGR95_065820.mRNA-p1

CAZy Family

GH5

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1060		119786.62	7.2164

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_HcapsulatumG217B	11221	447094	0	11221

Gene Location

Enzyme Prediction help

EC	3.2.1.28:32

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH37	474	1033	1.6e-148	0.9918533604887984

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
224541	TreA	0.0	405	1041	8	558	Neutral trehalase [Carbohydrate transport and metabolism].
395961	Trehalase	0.0	472	1036	1	509	Trehalase. Trehalase (EC:3.2.1.28) is known to recycle trehalose to glucose. Trehalose is a physiological hallmark of heat-shock response in yeast and protects of proteins and membranes against a variety of stresses. This family is found in conjunction with pfam07492 in fungi.
187646	RhlG_SDR_c	2.26e-90	6	254	1	244	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.
181295	PRK08213	1.58e-56	1	249	2	244	gluconate 5-dehydrogenase; Provisional
212491	SDR_c	5.89e-56	14	249	1	225	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.

CAZyme Hits help

E-Value	Query Start	Query End	Hit Start
323	1060	1	738
323	1060	1	738
1	1060	1	1013
335	1059	8	727
335	1059	8	727

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.78e-284	336	1052	17	737	Neutral trehalase Nth1 from Saccharomyces cerevisiae [Saccharomyces cerevisiae]
4.30e-282	336	1052	22	742	CRYSTAL STRUCTURE OF THE 14-3-3:NEUTRAL TREHALASE NTH1 COMPLEX [Saccharomyces cerevisiae S288C]
2.93e-279	410	1052	6	642	Neutral trehalase Nth1 from Saccharomyces cerevisiae [Saccharomyces cerevisiae S288C]
6.11e-256	460	1052	3	589	Neutral trehalase Nth1 from Saccharomyces cerevisiae in complex with trehalose [Saccharomyces cerevisiae]
4.67e-48	7	254	25	267	Pseudomonas aeruginosa RhlG/NADP active-site complex [Pseudomonas aeruginosa],2B4Q_B Pseudomonas aeruginosa RhlG/NADP active-site complex [Pseudomonas aeruginosa]

Swiss-Prot Hits download full data without filtering help

E-Value	Query Start	Query End	Hit Start	Hit End
337	1055	8	723	Cytosolic neutral trehalase OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=NTH1 PE=2 SV=2
336	1055	11	731	Cytosolic neutral trehalase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=treB PE=2 SV=2
334	1059	19	740	Cytosolic neutral trehalase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=treB PE=1 SV=2
323	1055	1	724	Cytosolic neutral trehalase OS=Botryotinia fuckeliana (strain B05.10) OX=332648 GN=TRE1 PE=3 SV=1
328	1055	3	730	Cytosolic neutral trehalase OS=Beauveria bassiana (strain ARSEF 2860) OX=655819 GN=NTH1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000031	0.000000

TMHMM Annotations help

There is no transmembrane helices in AGR95_065820.mRNA-p1.

You are here: Home > Sequence: AGR95_065820.mRNA-p1