CAZyme Information: EPrPVT00000018144-p1

Basic Information

• Species: Phytopythium vexans
• Lineage: Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
• CAZyme ID: EPrPVT00000018144-p1
• CAZy Family: GH28
• CAZyme Description: Maltose O-acetyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
805	PvexDAOMBR484_SC0272|CGC1	88178.66	4.7198

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PvexansDAOMBR484	11991	1223560	34	11957

• Gene Location: location=PvexDAOMBR484_SC0272:4816-7410(-)

Full Sequence      

MQLVPTVLALLLGAAAAHDDFLPLQAPQLFVSPCAAQWELMTSTFDASGSSGARRPLALE
SEPSELHVDLSVAFARFESRYVGFNTRTYNAQIPAPTIKVCPGDRLVVNLVNALDAGAAN
VTNLHLHGMHVSPEGAEDNVMVQVPPGGARTYDYRIRPDHPAGTFWYHPHAHGLVNTQLQ
GMMAGALIVADRPGDFPAALAAMDDHMLILQAICVEKCHNTYDILPDAIRSEYAIPMPGM
ANMKRRRVQEGMDMGGMDMSGMDMEEDEEEDGQDAREEEGFPVDLRVAADAPLNDTSLPT
VYVNGQYQPELHMAPGVFKRLRFLNAIANNVAELVAPDCELHVLAMDGIYRDAPMQKSVV
VLPPGGRADLAVKCDEPGVFFIETESSPDRNHLLGRVNQHRMPSQKVLSLRVLDTEELSK
HDDEDAEALATTLPTQLPRRPEYMRSTLDLETPVPDSNKYAYEFSVWTEEGVPGMVYGVN
HEPLRLDSANHSMRADELQEWALSVRNYGMECDDNAKADLNFDTEQDVMATHSMAGMNAH
GCHTMNHPFHMHSSHFQVVDCDRDVDPDGVLFDVGDWRDTLPLYKNDVTIRFVPGEHTVG
KILTHCHISSHADGGMGQLVEPLGSLRDSRVCCSSGSPSPTSDRMETEKAKMLRGELYDS
LDPDLFRERRAARALVTKYNSLTFADDTSARDLLKEMLGSVGDECFIRIGDRVLFAPGVQ
LYTATHPVETDVRATGLELGKPITIGDDVWIGGGAIVLPGVTIGNGAVIGAGSVVTKDVP
PMCVYAGNPARLVRKIEPSKDSKRS

Enzyme Prediction     

No EC number prediction in EPrPVT00000018144-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA1	86	616	1.3e-30	0.9664804469273743

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
100047	LbH_MAT_GAT	1.39e-70	657	793	1	169	Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).
259922	CuRO_1_Tth-MCO_like	1.45e-59	65	189	1	138	The first cupredoxin domain of the bacterial laccases similar to Tth-MCO from Thermus Thermophilus. The subfamily of bacterial laccases includes Tth-MCO and similar proteins. Tth-MCO is a hyperthermophilic multicopper oxidase (MCO) from thermus thermophilus HB27. Laccase is a blue multi-copper enzyme that catalyzes the oxidation of a variety aromatic - notably phenolic and inorganic substances coupled to the reduction of molecular oxygen to water. It has been implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 1 of 3-domain MCOs contains part the trinuclear copper binding site, which is located at the interface of domains 1 and 3.
182235	PRK10092	6.07e-53	645	796	1	183	maltose O-acetyltransferase; Provisional
100053	LbH_MAT_like	4.84e-42	700	793	9	109	Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.
225043	SufI	9.86e-38	47	617	14	443	Multicopper oxidase with three cupredoxin domains (includes cell division protein FtsP and spore coat protein CotA) [Cell cycle control, cell division, chromosome partitioning, Inorganic ion transport and metabolism, Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ21019.1|AA1	1.85e-41	120	623	5	469
CCO14930.1|AA1	8.89e-18	96	615	20	468
CAK44017.1|AA1	6.60e-12	90	205	107	217
CAG1849678.1|AA1	3.08e-10	85	377	45	275
QIW99401.1|AA1	4.07e-10	90	210	94	212

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6AG8_A	1.57e-34	645	796	1	183	Crystal structure of Maltose O-acetyltransferase from E. coli [Escherichia coli K-12],6AG8_C Crystal structure of Maltose O-acetyltransferase from E. coli [Escherichia coli K-12]
1OCX_A	5.70e-34	647	796	2	182	E. coli maltose-O-acetyltransferase [Escherichia coli],1OCX_B E. coli maltose-O-acetyltransferase [Escherichia coli],1OCX_C E. coli maltose-O-acetyltransferase [Escherichia coli]
2IC7_A	1.38e-32	645	794	1	182	Crystal Structure of Maltose Transacetylase from Geobacillus kaustophilus [Geobacillus kaustophilus],2IC7_B Crystal Structure of Maltose Transacetylase from Geobacillus kaustophilus [Geobacillus kaustophilus],2IC7_C Crystal Structure of Maltose Transacetylase from Geobacillus kaustophilus [Geobacillus kaustophilus],2P2O_A Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal form [Geobacillus kaustophilus HTA426],2P2O_B Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal form [Geobacillus kaustophilus HTA426],2P2O_C Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal form [Geobacillus kaustophilus HTA426],2P2O_D Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal form [Geobacillus kaustophilus HTA426],2P2O_E Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal form [Geobacillus kaustophilus HTA426],2P2O_F Crystal structure of maltose transacetylase from Geobacillus kaustophilus P2(1) crystal form [Geobacillus kaustophilus HTA426]
3HJJ_A	4.15e-30	642	797	1	189	Crystal Structure of Maltose O-acetyltransferase from Bacillus anthracis [Bacillus anthracis],3HJJ_B Crystal Structure of Maltose O-acetyltransferase from Bacillus anthracis [Bacillus anthracis],3HJJ_C Crystal Structure of Maltose O-acetyltransferase from Bacillus anthracis [Bacillus anthracis],3IGJ_A Crystal Structure of Maltose O-acetyltransferase Complexed with Acetyl Coenzyme A from Bacillus anthracis [Bacillus anthracis],3IGJ_B Crystal Structure of Maltose O-acetyltransferase Complexed with Acetyl Coenzyme A from Bacillus anthracis [Bacillus anthracis],3IGJ_C Crystal Structure of Maltose O-acetyltransferase Complexed with Acetyl Coenzyme A from Bacillus anthracis [Bacillus anthracis]
3SRT_A	4.64e-29	647	797	5	187	Chain A, Maltose O-acetyltransferase [Clostridioides difficile 630],3SRT_B Chain B, Maltose O-acetyltransferase [Clostridioides difficile 630],4ISX_A Chain A, Maltose O-acetyltransferase [Clostridioides difficile 630],4ISX_B Chain B, Maltose O-acetyltransferase [Clostridioides difficile 630]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P37515|MAA_BACSU	1.02e-34	645	796	2	184	Probable maltose O-acetyltransferase OS=Bacillus subtilis (strain 168) OX=224308 GN=maa PE=3 SV=1
sp|P77791|MAA_ECOLI	6.40e-34	645	796	1	183	Maltose O-acetyltransferase OS=Escherichia coli (strain K12) OX=83333 GN=maa PE=1 SV=3
sp|Q54UU2|Y0825_DICDI	1.14e-31	647	796	7	186	Putative acetyltransferase DDB_G0280825 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0280825 PE=3 SV=1
sp|Q552S7|Y5913_DICDI	9.99e-29	643	796	2	185	Putative acetyltransferase DDB_G0275913 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0275913 PE=3 SV=1
sp|P40892|YJV8_YEAST	4.13e-26	655	802	10	189	Putative acetyltransferase YJL218W OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=YJL218W PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000282	0.999691	CS pos: 17-18. Pr: 0.9645

TMHMM  Annotations     

There is no transmembrane helices in EPrPVT00000018144-p1.