CAZyme Information: MGYG000002398_01225

Basic Information

• Species: Laribacter hongkongensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Aquaspirillaceae; Laribacter; Laribacter hongkongensis
• CAZyme ID: MGYG000002398_01225
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
550		60591.5	9.4221

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002398	3424272	Isolate	China	Asia

• Gene Location: Start: 1252469; End: 1254121 Strand: +

Full Sequence      

MTPSPEQSPVPVPALSAAPQVSVVVIGRNEGERLVRCLASVMAADWHGISREVIYVDSCS
RDDSLTQARHQGALALLLDDASPCAAKARNLGWHAARGDCILFLDGDTELDAGFVRLACT
TLQAHADVCAVWGHRRESDPQQSWFTRVLDLDWVYPAGPSLYFGGDVLIRREALLASGGF
DPQLKAGEEPELCARLRAAGWKIMHVDAPMTRHDLAIRSWRAYWLRAYRSGMAYAEVAER
MRKLGDPLWQHEARRDFLHGWLFLAAGAAWLVSWFWWPWMAVGLTLAGGLLLARTAWRCR
WKVPGQPGLCWLYAVHVHLQKIPSLFGQLHWRRHRQAGGSGLIDYKQSPSRSPRRVKSWL
ADGLTPLARLWQRWGLARWLRVWSVARLQAATGRQVAPSNVVLGPVEVHGSGNIRLGERA
LIYPGCYFETQGAGRIEIGDDVVLSRGVHIVAFDRVTLGAGCMVGEYSSLRDANHRSGPD
GIRHSGHDSAPLDIGRNVWIGRGVAVLKGARLGDNCIVAANAVVNRPVAAGAIVGGLPAR
PLPRHPREES

Enzyme Prediction     

No EC number prediction in MGYG000002398_01225.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04647	LbH_MAT_like	1.52e-33	435	542	1	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.
COG0110	WbbJ	3.27e-23	373	541	9	174	Acetyltransferase (isoleucine patch superfamily) [General function prediction only].
COG1215	BcsA	1.30e-22	11	282	46	333	Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
cd00761	Glyco_tranf_GTA_type	2.38e-21	23	206	1	156	Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
cd04186	GT_2_like_c	1.60e-20	23	206	1	157	Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASJ24095.1	0.0	1	550	1	550
ACO73821.1	0.0	1	550	1	550
QXP83974.1	6.46e-95	13	346	4	338
QXP90770.1	2.56e-94	13	346	4	338
AAU92280.1	2.56e-94	13	346	4	338

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1KQA_A	4.73e-09	416	540	58	180	GalactosideAcetyltransferase In Complex With Coenzyme A [Escherichia coli],1KQA_B Galactoside Acetyltransferase In Complex With Coenzyme A [Escherichia coli],1KQA_C Galactoside Acetyltransferase In Complex With Coenzyme A [Escherichia coli],1KRR_A Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRR_B Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRR_C Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A [Escherichia coli],1KRU_A Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRU_B Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRU_C Galactoside Acetyltransferase in Complex with IPTG and Coenzyme A [Escherichia coli],1KRV_A Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli],1KRV_B Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli],1KRV_C Galactoside Acetyltransferase in Complex with CoA and PNP-beta-Gal [Escherichia coli]
3ECT_A	1.40e-08	416	540	59	181	CrystalStructure of the Hexapeptide-Repeat Containing-Acetyltransferase VCA0836 from Vibrio cholerae [Vibrio cholerae],3NZ2_A Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_B Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_C Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_D Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_E Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_F Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_G Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_H Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_I Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_J Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_K Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3NZ2_L Crystal Structure of Hexapeptide-Repeat containing-Acetyltransferase VCA0836 Complexed with Acetyl Co Enzyme A from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961]
2IC7_A	2.46e-07	417	540	58	179	CrystalStructure 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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P37750	3.02e-13	367	548	2	189	Putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ OS=Escherichia coli (strain K12) OX=83333 GN=wbbJ PE=3 SV=2
O53281	1.69e-09	334	540	65	267	Probable acetyltransferase Rv3034c OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv3034c PE=1 SV=1
P37515	4.16e-09	416	540	57	179	Probable maltose O-acetyltransferase OS=Bacillus subtilis (strain 168) OX=224308 GN=maa PE=3 SV=1
P07464	2.59e-08	416	540	58	180	Galactoside O-acetyltransferase OS=Escherichia coli (strain K12) OX=83333 GN=lacA PE=1 SV=1
P52984	5.56e-07	416	538	59	180	Galactoside O-acetyltransferase OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=lacA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
270	292