logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001838_01932

You are here: Home > Sequence: MGYG000001838_01932

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 sp000438175
Lineage Bacteria; Cyanobacteria; Vampirovibrionia; Gastranaerophilales; Gastranaerophilaceae; Zag1; Zag1 sp000438175
CAZyme ID MGYG000001838_01932
CAZy Family GT2
CAZyme Description 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
508 MGYG000001838_26|CGC1 58526.52 9.038
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001838 2186237 MAG Denmark Europe
Gene Location Start: 20017;  End: 21543  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001838_01932.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 7 129 3.4e-17 0.6941176470588235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03349 LbH_XAT 2.91e-51 338 470 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 1.33e-32 338 458 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 2.85e-28 337 456 61 167
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 1.74e-25 347 472 53 189
Acetyltransferase (isoleucine patch superfamily) [General function prediction only].
cd03358 LbH_WxcM_N_like 1.73e-22 361 459 35 119
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
SDT46839.1 7.68e-44 6 264 4 262
AEF84575.1 6.85e-41 318 503 389 573
AMR32929.1 8.92e-39 1 274 4 282
QKJ31486.1 1.06e-36 6 272 4 277
AEE16252.1 6.22e-27 3 242 4 239

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6MFK_A 4.77e-19 361 462 65 173
ChainA, Chloramphenicol acetyltransferase [Elizabethkingia anophelis]
1KHR_A 3.55e-18 338 493 29 199
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]
6PU9_A 1.24e-17 361 471 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 4.41e-17 361 471 59 176
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]
6PXA_A 6.93e-15 361 470 71 183
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
P26840 3.80e-20 361 470 24 140
Probable macrolide acetyltransferase (Fragment) OS=Lysinibacillus sphaericus OX=1421 PE=3 SV=1
P50868 1.69e-18 361 483 57 199
Chloramphenicol acetyltransferase OS=Klebsiella aerogenes OX=548 GN=catB4 PE=3 SV=1
P50870 1.94e-17 338 493 29 199
Streptogramin A acetyltransferase OS=Enterococcus faecium OX=1352 GN=vatD PE=1 SV=1
P26838 4.99e-17 361 470 57 173
Chloramphenicol acetyltransferase OS=Escherichia coli OX=562 GN=catB2 PE=3 SV=2
P23364 9.04e-17 361 470 56 172
Chloramphenicol acetyltransferase OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=cat PE=3 SV=1

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
1.000059 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001838_01932.