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CAZyme Information: MGYG000003984_00479

You are here: Home > Sequence: MGYG000003984_00479

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 Mediterraneibacter sp900752395
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900752395
CAZyme ID MGYG000003984_00479
CAZy Family GT4
CAZyme Description Alpha-monoglucosyldiacylglycerol synthase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
441 MGYG000003984_4|CGC1 50161.46 6.7392
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003984 2095190 MAG United Kingdom Europe
Gene Location Start: 52224;  End: 53549  Strand: +

Full Sequence      Download help

MKIAMLTNNY  RPFVGGVPIS  VERQAKELIK  LGHKVTVFAP  MYGETEEEKA  AVLAADASAF60
EQVVRYGTQR  RKMDNGMVYP  SFYPSEIMET  FERETFDCIH  VHHPMFVGPC  ALYLKRKYRL120
PLIYTYHTRY  EDYLHYIPGL  RVDENSFELK  KKAVGLIQTK  LIPAYMSWFA  NQCDLVLAPS180
AGMQKILWKY  GMRSRSAVFP  TGLEESFFRT  DEQRAQEIRE  TYIGKKKHLY  VTVSRLEKEK240
NYEFILRGIA  KIKEEAGDDF  HVMILGDGSQ  KRELKTKAAL  LGISDLVTFA  GNVQNEDVKH300
YVHAADLFLF  ASKSETQGIV  LAEAMAAGTP  VVAVHAVGSD  DIVEDGINGF  LTEEEESKWA360
EKVIEASQPK  NRFKMKKAAL  AEAQNYRSGT  LALYEEMLYN  QCICEKAMDQ  QKDGKGEYFY420
ENGEDHGERT  AMAVHKISHI  A441

Enzyme Prediction      help

No EC number prediction in MGYG000003984_00479.

CAZyme Signature Domains help

Created with Snap22446688110132154176198220242264286308330352374396418223375GT4
Family Start End Evalue family coverage
GT4 223 375 1.1e-33 0.95625

CDD Domains      download full data without filtering help

Created with Snap224466881101321541761982202422642863083303523743964182397GT4_UGDG-like2386GT4-like2384GT4_PimA-like1401RfaB2387GT4_GT28_WabH-like
Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd03817 GT4_UGDG-like 3.17e-95 2 397 1 372
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.
cd03814 GT4-like 7.79e-54 2 386 1 351
glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.
cd03801 GT4_PimA-like 7.42e-52 2 384 1 349
phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
COG0438 RfaB 2.14e-47 1 401 1 381
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].
cd03811 GT4_GT28_WabH-like 3.79e-39 2 387 1 346
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.

CAZyme Hits      help

Created with Snap224466881101321541761982202422642863083303523743964181438QHB24224.1|GT41438QEI31728.1|GT41438QRT30460.1|GT41438QRO35716.1|GT41438QBF75925.1|GT4
Hit ID E-Value Query Start Query End Hit Start Hit End
QHB24224.1 1.88e-144 1 438 1 427
QEI31728.1 1.88e-144 1 438 1 427
QRT30460.1 2.16e-143 1 438 1 427
QRO35716.1 9.54e-112 1 438 1 422
QBF75925.1 9.54e-112 1 438 1 422

PDB Hits      download full data without filtering help

Created with Snap22446688110132154176198220242264286308330352374396418853532JJM_A853533MBO_A14093C4Q_A14093C48_A123995D00_A
Hit ID E-Value Query Start Query End Hit Start Hit End Description
2JJM_A 4.69e-15 85 353 89 333
CrystalStructure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_B Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_C Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_D Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_E Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_F Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_G Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_H Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_I Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_J Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_K Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_L Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames]
3MBO_A 5.22e-15 85 353 109 353
CrystalStructure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_B Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_C Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_D Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_E Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_F Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_G Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_H Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis]
3C4Q_A 4.17e-14 1 409 1 412
Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum]
3C48_A 4.37e-14 1 409 21 432
Structureof the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum]
5D00_A 1.41e-13 12 399 14 372
Crystalstructure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits      download full data without filtering help

Created with Snap224466881101321541761982202422642863083303523743964181351sp|Q8CWR6|AMGDS_STRR61356sp|Q93P60|AMGDS_ACHLA1350sp|Q59002|Y1607_METJA1351sp|Q8NT41|MGTA_CORGL97351sp|Q8S4F6|SQD2_ARATH
Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8CWR6 1.12e-38 1 351 1 330
Alpha-monoglucosyldiacylglycerol synthase OS=Streptococcus pneumoniae (strain ATCC BAA-255 / R6) OX=171101 GN=spr0982 PE=1 SV=1
Q93P60 6.75e-27 1 356 1 342
Alpha-monoglucosyldiacylglycerol synthase OS=Acholeplasma laidlawii OX=2148 GN=mgs PE=1 SV=1
Q59002 1.80e-15 1 350 1 329
Uncharacterized glycosyltransferase MJ1607 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1607 PE=3 SV=1
Q8NT41 4.97e-15 1 351 7 321
GDP-mannose-dependent alpha-mannosyltransferase OS=Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) OX=196627 GN=mgtA PE=1 SV=1
Q8S4F6 1.27e-14 97 351 191 426
Sulfoquinovosyl transferase SQD2 OS=Arabidopsis thaliana OX=3702 GN=SQD2 PE=1 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
1.000065 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003984_00479.