CAZyme Information: MGYG000001899_01942

Basic Information

• Lineage: Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag1
• CAZyme ID: MGYG000001899_01942
• CAZy Family: GT2
• CAZyme Description: 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
510		58273.92	9.2156

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001899	1916473	MAG	Denmark	Europe

• Gene Location: Start: 208; End: 1740 Strand: +

Full Sequence      

MQEPLLSICIPTYNRACNLWRTLNSITTQKGFLFTNFVEIVISDNCSTDGTEQVVLEFVK
KYPNKIRYIKRDKNISGDENFVYVLSQASGKFVKLHNDTCYVLDNSISDIINDIQTADKL
GADACFFANSGAKNSGIINNFNDMLASASYFITWIGSHAYRRSFLQKLDGINRYSNLNFV
QVDILGRLFENGSSVYLTNNVYFSTIYVDKKGGYNIAKVFGYNYFSILDIYRKKGLISNK
IFAKNKYDTLMKHIIPFYFDFMHKYNFEKDGYFKYMKYFWFEPYFYFSFFKVFKMLLKYV
KSKLKHKITIEEKQNNIWRIQNFDNHTNLIINGSLFENIAVGKGSYGDINAIFSNKSSVA
LIIGNYVSIAPDVWFIPESEHGYKALSTYPFKVMLGLQTYEAGSKGSIVIEDDVWIGARA
TVLSGVRIGQGAIVAAGSVVTKDVEPYSIVAGIPAKHIKYRFSPKVVEELKHFNLGLLTK
DVVKDNIDLVYRTLTDENINEVLSILKGES

Enzyme Prediction     

No EC number prediction in MGYG000001899_01942.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT2	7	134	1.1e-17	0.7235294117647059

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd03349	LbH_XAT	4.12e-52	338	470	1	136	Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.
cd04647	LbH_MAT_like	3.08e-31	338	456	1	107	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.
cd03357	LbH_MAT_GAT	8.77e-27	338	456	62	167	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).
COG0110	WbbJ	1.56e-26	291	472	5	189	Acetyltransferase (isoleucine patch superfamily) [General function prediction only].
cd03358	LbH_WxcM_N_like	4.20e-21	337	459	3	119	WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEF84575.1	4.47e-50	4	503	31	573
SDT46839.1	1.52e-44	6	256	4	254
AMR32929.1	9.31e-40	1	244	4	249
QKJ31486.1	5.90e-39	6	272	4	277
AEE16252.1	2.93e-29	3	238	4	235

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MFK_A	1.18e-20	361	492	65	211	ChainA, Chloramphenicol acetyltransferase [Elizabethkingia anophelis]
6PU9_A	1.68e-19	361	471	59	175	CrystalStructure of the Type B Chloramphenicol O-Acetyltransferase from Vibrio vulnificus [Vibrio vulnificus CMCP6],6PU9_B Crystal Structure of the Type B Chloramphenicol O-Acetyltransferase from Vibrio vulnificus [Vibrio vulnificus CMCP6],6PU9_C Crystal Structure of the Type B Chloramphenicol O-Acetyltransferase from Vibrio vulnificus [Vibrio vulnificus CMCP6]
3EEV_A	1.51e-18	338	463	24	167	CrystalStructure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3EEV_B Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],3EEV_C Crystal Structure of Chloramphenicol Acetyltransferase VCA0300 from Vibrio cholerae O1 biovar eltor [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_A The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_B The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUA_C The 2.0 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae [Vibrio cholerae O1 biovar El Tor str. N16961],6PUB_A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the Complex with Crystal Violet [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_A The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_B The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961],6U9C_C The 2.2 A Crystal Structure of the Type B Chloramphenicol Acetyltransferase from Vibrio cholerae in the complex with Acetyl CoA [Vibrio cholerae O1 biovar El Tor str. N16961]
1KHR_A	1.66e-17	337	503	28	206	CrystalStructure of Vat(D) in Complex with Virginiamycin and Coenzyme A [Enterococcus faecium],1KHR_B Crystal Structure of Vat(D) in Complex with Virginiamycin and Coenzyme A [Enterococcus faecium],1KHR_C Crystal Structure of Vat(D) in Complex with Virginiamycin and Coenzyme A [Enterococcus faecium],1KHR_D Crystal Structure of Vat(D) in Complex with Virginiamycin and Coenzyme A [Enterococcus faecium],1KHR_E Crystal Structure of Vat(D) in Complex with Virginiamycin and Coenzyme A [Enterococcus faecium],1KHR_F Crystal Structure of Vat(D) in Complex with Virginiamycin and Coenzyme A [Enterococcus faecium],1KK4_A Crystal Structure of Vat(D) in Complex with Acetyl-CoA [Enterococcus faecium],1KK4_B Crystal Structure of Vat(D) in Complex with Acetyl-CoA [Enterococcus faecium],1KK4_C Crystal Structure of Vat(D) in Complex with Acetyl-CoA [Enterococcus faecium],1KK4_D Crystal Structure of Vat(D) in Complex with Acetyl-CoA [Enterococcus faecium],1KK4_E Crystal Structure of Vat(D) in Complex with Acetyl-CoA [Enterococcus faecium],1KK4_F Crystal Structure of Vat(D) in Complex with Acetyl-CoA [Enterococcus faecium],1KK5_A Crystal Structure of Vat(D) (Form II) [Enterococcus faecium],1KK5_B Crystal Structure of Vat(D) (Form II) [Enterococcus faecium],1KK5_C Crystal Structure of Vat(D) (Form II) [Enterococcus faecium],1KK5_D Crystal Structure of Vat(D) (Form II) [Enterococcus faecium],1KK5_E Crystal Structure of Vat(D) (Form II) [Enterococcus faecium],1KK5_F Crystal Structure of Vat(D) (Form II) [Enterococcus faecium],1KK6_A Crystal Structure of Vat(D) (Form I) [Enterococcus faecium],1KK6_B Crystal Structure of Vat(D) (Form I) [Enterococcus faecium],1KK6_C Crystal Structure of Vat(D) (Form I) [Enterococcus faecium],1MR7_A Crystal Structure of Streptogramin A Acetyltransferase [Enterococcus faecium],1MR7_B Crystal Structure of Streptogramin A Acetyltransferase [Enterococcus faecium],1MR7_C Crystal Structure of Streptogramin A Acetyltransferase [Enterococcus faecium],1MR7_X Crystal Structure of Streptogramin A Acetyltransferase [Enterococcus faecium],1MR7_Y Crystal Structure of Streptogramin A Acetyltransferase [Enterococcus faecium],1MR7_Z Crystal Structure of Streptogramin A Acetyltransferase [Enterococcus faecium],1MRL_A Crystal structure of streptogramin A acetyltransferase with dalfopristin [Enterococcus faecium],1MRL_B Crystal structure of streptogramin A acetyltransferase with dalfopristin [Enterococcus faecium],1MRL_C Crystal structure of streptogramin A acetyltransferase with dalfopristin [Enterococcus faecium],3DHO_A Structure of Streptogramin Acetyltransferase in Complex with an Inhibitor [Enterococcus faecium],3DHO_B Structure of Streptogramin Acetyltransferase in Complex with an Inhibitor [Enterococcus faecium],3DHO_C Structure of Streptogramin Acetyltransferase in Complex with an Inhibitor [Enterococcus faecium],3DHO_D Structure of Streptogramin Acetyltransferase in Complex with an Inhibitor [Enterococcus faecium],3DHO_E Structure of Streptogramin Acetyltransferase in Complex with an Inhibitor [Enterococcus faecium],3DHO_F Structure of Streptogramin Acetyltransferase in Complex with an Inhibitor [Enterococcus faecium]
1XAT_A	1.74e-15	361	470	57	173	StructureOf The Hexapeptide Xenobiotic Acetyltransferase From Pseudomonas Aeruginosa [Pseudomonas aeruginosa],2XAT_A Complex Of The Hexapeptide Xenobiotic Acetyltransferase With Chloramphenicol And Desulfo-Coenzyme A [Pseudomonas aeruginosa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26840	3.39e-19	361	490	24	160	Probable macrolide acetyltransferase (Fragment) OS=Lysinibacillus sphaericus OX=1421 PE=3 SV=1
P50868	1.08e-17	352	477	47	183	Chloramphenicol acetyltransferase OS=Klebsiella aerogenes OX=548 GN=catB4 PE=3 SV=1
P23364	4.92e-17	338	463	22	165	Chloramphenicol acetyltransferase OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=cat PE=3 SV=1
P50870	9.10e-17	337	503	28	206	Streptogramin A acetyltransferase OS=Enterococcus faecium OX=1352 GN=vatD PE=1 SV=1
P50869	5.85e-16	361	490	57	193	Chloramphenicol acetyltransferase OS=Morganella morganii OX=582 GN=cat 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
1.000067	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001899_01942.