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CAZyme Information: MGYG000000813_01128

You are here: Home > Sequence: MGYG000000813_01128

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Zag1 sp000437435
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag1; Zag1 sp000437435
CAZyme ID MGYG000000813_01128
CAZy Family GT2
CAZyme Description 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
509 58560.18 8.978
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000813 1978596 MAG China Asia
Gene Location Start: 340907;  End: 342436  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000813_01128.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 7 129 3.4e-16 0.6941176470588235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03349 LbH_XAT 8.21e-54 338 472 1 138
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 7.21e-34 338 458 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.
cd03357 LbH_MAT_GAT 8.28e-28 338 458 62 169
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).
COG0110 WbbJ 8.95e-26 325 472 18 189
Acetyltransferase (isoleucine patch superfamily) [General function prediction only].
cd03358 LbH_WxcM_N_like 4.54e-24 337 459 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AEF84575.1 5.86e-49 4 503 31 573
SDT46839.1 7.91e-43 6 257 4 255
AMR32929.1 6.43e-38 1 258 4 263
QKJ31486.1 1.52e-37 6 260 4 258
AEE16252.1 3.66e-28 2 264 3 261

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MFK_A 4.65e-21 361 492 65 211
ChainA, Chloramphenicol acetyltransferase [Elizabethkingia anophelis]
1KHR_A 4.12e-19 337 493 28 199
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]
3EEV_A 5.16e-18 338 464 24 168
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]
6PU9_A 6.68e-16 361 462 59 166
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]
6PXA_A 1.12e-15 343 466 62 179
Thecrystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_B The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_C The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_D The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_E The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_F The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_G The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_H The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_I The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_J The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_K The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114],6PXA_L The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid [Aliivibrio fischeri ES114]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P23364 5.52e-20 338 465 22 167
Chloramphenicol acetyltransferase OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=cat PE=3 SV=1
P26840 1.81e-19 361 464 24 134
Probable macrolide acetyltransferase (Fragment) OS=Lysinibacillus sphaericus OX=1421 PE=3 SV=1
P50868 1.25e-18 338 464 22 167
Chloramphenicol acetyltransferase OS=Klebsiella aerogenes OX=548 GN=catB4 PE=3 SV=1
P50870 2.26e-18 337 493 28 199
Streptogramin A acetyltransferase OS=Enterococcus faecium OX=1352 GN=vatD PE=1 SV=1
P26838 9.26e-17 361 464 57 167
Chloramphenicol acetyltransferase OS=Escherichia coli OX=562 GN=catB2 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000040 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000813_01128.