CAZyme Information: An08g09290-T-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: An08g09290-T-p1
• CAZy Family: GH28
• CAZyme Description: Has domain(s) with predicted catalytic activity, hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds activity and role in carbohydrate metabolic process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
317		34936.37	4.8432

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerCBS513-88	14403	425011	346	14057

• Gene Location: location=An08_A_niger_CBS_513_88:2205094-2206124(-)

Full Sequence      

MTSLGDLCAGPTCCSDESLIVPAATPGNNAAPSSPTDRHNTHFQPHPPSPMPPSSWPDSA
KAAVSITFDNVGESRDVGVGAWPKEKPVGQHPSVLEVTPIILDILDKHDVKVTYFMEAWG
IQTYPKMLSEVQSRGHEIGYHAYQHEEWKTLSPLQEEKIINKSLPIAQELGVCYKGFRPP
GGSMNAGTKDLLRRHGIKYASILGQDISTDKDGFVTLPFQWRAVDAFYILDAFDFLRAEY
GEQGSIFTCEAFQQALFDQIDAAVEKGAFIDILFHPFLHTSPETRAVIEAVVARVSNDPD
IWCAPTYEVAEWAAAHQ

Enzyme Prediction     

No EC number prediction in An08g09290-T-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CE4	61	201	7.8e-20	0.9076923076923077

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200567	CE4_u11	8.31e-144	63	314	1	252	Putative catalytic domain of uncharacterized bacterial proteins from the carbohydrate esterase 4 superfamily. This family corresponds to a group of uncharacterized bacterial proteins with high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily.
200563	CE4_HpPgdA_like	2.03e-37	63	314	1	258	Catalytic domain of Helicobacter pylori peptidoglycan deacetylase (HpPgdA) and similar proteins. This family is represented by a peptidoglycan deacetylase (HP0310, HpPgdA) from the gram-negative pathogen Helicobacter pylori. HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. It functions as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. In contrast to typical NodB-like DCAs, HpPgdA does not exhibit a solvent-accessible polysaccharide binding groove, suggesting that the enzyme binds a small molecule at the active site.
213021	CE4_PuuE_HpPgdA_like	4.82e-32	63	312	1	247	Catalytic domain of bacterial PuuE allantoinases, Helicobacter pylori peptidoglycan deacetylase (HpPgdA), and similar proteins. This family is a member of the very large and functionally diverse carbohydrate esterase 4 (CE4) superfamily. It contains bacterial PuuE (purine utilization E) allantoinases, a peptidoglycan deacetylase from Helicobacter pylori (HpPgdA), Escherichia coli ArnD, and many uncharacterized homologs from all three kingdoms of life. PuuE allantoinase appears to be metal-independent and specifically catalyzes the hydrolysis of (S)-allantoin into allantoic acid. Different from PuuE allantoinase, HpPgdA has the ability to bind a metal ion at the active site and is responsible for a peptidoglycan modification that counteracts the host immune response. Both PuuE allantoinase and HpPgdA function as a homotetramer. The monomer is composed of a 7-stranded barrel with detectable sequence similarity to the 6-stranded barrel NodB homology domain of polysaccharide deacetylase (DCA)-like proteins in the CE4 superfamily, which removes N-linked or O-linked acetyl groups from cell wall polysaccharides. However, in contrast with the typical DCAs, PuuE allantoinase and HpPgdA might not exhibit a solvent-accessible polysaccharide binding groove and only recognize a small substrate molecule. ArnD catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol.
396211	Polysacc_deac_1	1.26e-23	96	200	19	124	Polysaccharide deacetylase. This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyzes glucosidic bonds in xylan.
223798	CDA1	6.88e-22	96	273	78	243	Peptidoglycan/xylan/chitin deacetylase, PgdA/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VBB81060.1|CE0	1.48e-80	50	316	4	268
AEO59736.1|CE0	6.58e-79	52	316	4	265
AEO68279.1|CE0	9.71e-76	53	316	2	262
UQD84776.1|CE4	5.66e-24	53	310	5	267
AZR72406.1|CE4	2.67e-14	58	185	51	158

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QBU_A	7.34e-14	99	237	77	212	Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_B Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_C Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],3QBU_D Crystal structure of putative peptidoglycan deactelyase (HP0310) from Helicobacter pylori [Helicobacter pylori G27],4LY4_A Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_B Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_C Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27],4LY4_D Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori [Helicobacter pylori G27]
5O6Y_A	1.55e-08	95	184	33	123	Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]
6HM9_A	8.91e-08	96	183	98	186	Crystal structure of a BA3943 mutant,a CE4 family pseudoenzyme with restored enzymatic activity. [Bacillus anthracis]
7BKF_A	1.64e-07	83	183	83	187	Chain A, Putative polysaccharide deacetylase [Bacillus anthracis]
5O6Y_B	1.74e-07	95	184	33	123	Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_C Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579],5O6Y_D Crystal structure of the Bc1960 peptidoglycan N-acetylglucosamine deacetylase in complex with 4-naphthalen-1-yl-~{N}-oxidanyl-benzamide [Bacillus cereus ATCC 14579]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B5ZA76|PGDAE_HELPG	2.84e-13	99	237	44	179	Peptidoglycan deacetylase OS=Helicobacter pylori (strain G27) OX=563041 GN=pgdA PE=1 SV=1
sp|O25080|PGDAE_HELPY	1.49e-11	99	237	44	179	Peptidoglycan deacetylase OS=Helicobacter pylori (strain ATCC 700392 / 26695) OX=85962 GN=pgdA PE=1 SV=1
sp|I1S2J6|FGM2_GIBZE	7.53e-09	101	206	82	191	Peptidoglycan deacetylase-like protein FGM2 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=FGM2 PE=2 SV=1
sp|P50850|YLXY_BACSU	9.28e-09	101	191	148	239	Uncharacterized protein YlxY OS=Bacillus subtilis (strain 168) OX=224308 GN=ylxY PE=3 SV=2
sp|Q04729|YFUM2_GEOSE	1.29e-07	58	198	63	184	Uncharacterized 30.6 kDa protein in fumA 3'region OS=Geobacillus stearothermophilus OX=1422 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999332	0.000706

TMHMM  Annotations     

There is no transmembrane helices in An08g09290-T-p1.